The Enzyme Database

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EC 1.1.1.284     
Accepted name: S-(hydroxymethyl)glutathione dehydrogenase
Reaction: S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H + H+
Other name(s): NAD-linked formaldehyde dehydrogenase (incorrect); formaldehyde dehydrogenase (incorrect); formic dehydrogenase (incorrect); class III alcohol dehydrogenase; ADH3; χ-ADH; FDH (incorrect); formaldehyde dehydrogenase (glutathione) (incorrect); GS-FDH (incorrect); glutathione-dependent formaldehyde dehydrogenase (incorrect); GD-FALDH; NAD- and glutathione-dependent formaldehyde dehydrogenase; NAD-dependent formaldehyde dehydrogenase (incorrect)
Systematic name: S-(hydroxymethyl)glutathione:NAD+ oxidoreductase
Comments: The substrate, S-(hydroxymethyl)glutathione, forms spontaneously from glutathione and formaldehyde; its rate of formation is increased in some bacteria by the presence of EC 4.4.1.22, S-(hydroxymethyl)glutathione synthase. This enzyme forms part of the pathway that detoxifies formaldehyde, since the product is hydrolysed by EC 3.1.2.12, S-formylglutathione hydrolase. The human enzyme belongs to the family of zinc-dependent alcohol dehydrogenases. Also specifically reduces S-nitrosylglutathione.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD
References:
1.  Jakoby, W.B. Aldehyde dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 203–221.
2.  Rose, Z.B. and Racker, E. Formaldehyde dehydrogenase. Methods Enzymol. 9 (1966) 357–360.
3.  Liu, L., Hausladen, A., Zeng, M., Que, L., Heitman, J. and Stamler, J.S. A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. Nature 410 (2001) 490–494. [DOI] [PMID: 11260719]
4.  Sanghani, P.C., Stone, C.L., Ray, B.D., Pindel, E.V., Hurley, T.D. and Bosron, W.F. Kinetic mechanism of human glutathione-dependent formaldehyde dehydrogenase. Biochemistry 39 (2000) 10720–10729. [DOI] [PMID: 10978156]
5.  van Ophem, P.W. and Duine, J.A. NAD- and co-substrate (GSH or factor)-dependent formaldehyde dehydrogenases from methylotrophic microorganisms act as a class III alcohol dehydrogenase. FEMS Microbiol. Lett. 116 (1994) 87–94.
6.  Ras, J., van Ophem, P.W., Reijnders, W.N., Van Spanning, R.J., Duine, J.A., Stouthamer, A.H. and Harms, N. Isolation, sequencing, and mutagenesis of the gene encoding NAD- and glutathione-dependent formaldehyde dehydrogenase (GD-FALDH) from Paracoccus denitrificans, in which GD-FALDH is essential for methylotrophic growth. J. Bacteriol. 177 (1995) 247–251. [DOI] [PMID: 7798140]
7.  Barber, R.D., Rott, M.A. and Donohue, T.J. Characterization of a glutathione-dependent formaldehyde dehydrogenase from Rhodobacter sphaeroides. J. Bacteriol. 178 (1996) 1386–1393. [DOI] [PMID: 8631716]
[EC 1.1.1.284 created 2005 (EC 1.2.1.1 created 1961, modified 1982, modified 2002, part transferred 2005 to EC 1.1.1.284)]
 
 
EC 1.1.1.306     
Accepted name: S-(hydroxymethyl)mycothiol dehydrogenase
Reaction: S-(hydroxymethyl)mycothiol + NAD+ = S-formylmycothiol + NADH + H+
Glossary: mycothiol = 1-O-[2-(N2-acetyl-L-cysteinamido)-2-deoxy-α-D-glucopyranosyl]-1D-myo-inositol
Other name(s): NAD/factor-dependent formaldehyde dehydrogenase; mycothiol-dependent formaldehyde dehydrogenase
Systematic name: S-(hydroxymethyl)mycothiol:NAD+ oxidoreductase
Comments: S-hydroxymethylmycothiol is believed to form spontaneously from formaldehyde and mycothiol. This enzyme oxidizes the product of this spontaneous reaction to S-formylmycothiol, in a reaction that is analogous to EC 1.1.1.284, S-(hydroxymethyl)glutathione dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 192140-85-5
References:
1.  Misset-Smits, M., Van Ophem, P.W., Sakuda, S. and Duine, J.A. Mycothiol, 1-O-(2′-[N-acetyl-L-cysteinyl]amido-2′-deoxy-α-D-glucopyranosyl)-D-myo-inositol, is the factor of NAD/factor-dependent formaldehyde dehydrogenase. FEBS Lett. 409 (1997) 221–222. [DOI] [PMID: 9202149]
2.  Norin, A., Van Ophem, P.W., Piersma, S.R., Person, B., Duine, J.A. and Jornvall, H. Mycothiol-dependent formaldehyde dehydrogenase, a prokaryotic medium-chain dehydrogenase/reductase, phylogenetically links different eukaryotic alcohol dehydrogenase's - primary structure, conformational modelling and functional correlations. Eur. J. Biochem. 248 (1997) 282–289. [DOI] [PMID: 9346279]
3.  Vogt, R.N., Steenkamp, D.J., Zheng, R. and Blanchard, J.S. The metabolism of nitrosothiols in the Mycobacteria: identification and characterization of S-nitrosomycothiol reductase. Biochem. J. 374 (2003) 657–666. [DOI] [PMID: 12809551]
4.  Rawat, M. and Av-Gay, Y. Mycothiol-dependent proteins in actinomycetes. FEMS Microbiol. Rev. 31 (2007) 278–292. [DOI] [PMID: 17286835]
[EC 1.1.1.306 created 2010 as EC 1.2.1.66, transferred 2010 to EC 1.1.1.306]
 
 
EC 1.1.1.398     
Accepted name: 2-glutathionyl-2-methylbut-3-en-1-ol dehydrogenase
Reaction: 2-(glutathion-S-yl)-2-methylbut-3-en-1-ol + 2 NAD+ + H2O = 2-(glutathion-S-yl)-2-methylbut-3-enoate + 2 NADH + 2 H+ (overall reaction)
(1a) 2-(glutathion-S-yl)-2-methylbut-3-en-1-ol + NAD+ = 2-(glutathion-S-yl)-2-methylbut-3-enal + NADH + H+
(1b) 2-(glutathion-S-yl)-2-methylbut-3-enal + NAD+ + H2O = 2-(glutathion-S-yl)-2-methylbut-3-enoate + NADH + H+
For diagram of isoprene biosynthesis and metabolism, click here
Other name(s): isoH (gene name); 4-hydroxy-3-glutathionyl-3-methylbut-1-ene dehydrogenase
Systematic name: 2-(glutathion-S-yl)-2-methylbut-3-en-1-ol:NAD+ oxidoreductase
Comments: The enzyme, characterized from the bacterium Rhodococcus sp. AD45, is involved in isoprene degradation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  van Hylckama Vlieg, J.E., Kingma, J., Kruizinga, W. and Janssen, D.B. Purification of a glutathione S-transferase and a glutathione conjugate-specific dehydrogenase involved in isoprene metabolism in Rhodococcus sp. strain AD45. J. Bacteriol. 181 (1999) 2094–2101. [PMID: 10094686]
[EC 1.1.1.398 created 2016]
 
 
EC 1.2.1.1      
Deleted entry:  glutathione-dependent formaldehyde dehydrogenase. This enzyme was classified on the basis of an incorrect reaction. It has been replaced by two enzymes, EC 1.1.1.284, S-(hydroxymethyl)glutathione dehydrogenase and EC 4.4.1.22, S-(hydroxymethyl)glutathione synthase
[EC 1.2.1.1 created 1961, modified 1982, modified 2002, deleted 2005]
 
 
EC 1.5.1.46     
Accepted name: agroclavine dehydrogenase
Reaction: agroclavine + NADP+ = 6,8-dimethyl-6,7,8,9-tetradehydroergoline + NADPH + H+
For diagram of ergot alkaloid biosynthesis, click here
Glossary: agroclavine = 6,8-dimethyl-8,9-didehydroergoline
Other name(s): easG (gene name)
Systematic name: agroclavine:NADP+ oxidoreductase
Comments: The enzyme participates in the biosynthesis of ergotamine, an ergot alkaloid produced by some fungi of the Clavicipitaceae family. The reaction is catalysed in the opposite direction to that shown. The substrate for the enzyme is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Matuschek, M., Wallwey, C., Xie, X. and Li, S.M. New insights into ergot alkaloid biosynthesis in Claviceps purpurea: an agroclavine synthase EasG catalyses, via a non-enzymatic adduct with reduced glutathione, the conversion of chanoclavine-I aldehyde to agroclavine. Org. Biomol. Chem. 9 (2011) 4328–4335. [DOI] [PMID: 21494745]
[EC 1.5.1.46 created 2013]
 
 
EC 1.5.4.1     
Accepted name: pyrimidodiazepine synthase
Reaction: 2-amino-6-acetyl-3,7,8,9-tetrahydro-3H-pyrimido[4,5-b][1,4]diazepin-4-one + glutathione disulfide + H2O = 6-pyruvoyltetrahydropterin + 2 glutathione
For diagram of 6-pyruvyltetrahydropterin metabolism, click here
Glossary: 2-amino-6-acetyl-3,7,8,9-tetrahydro-3H-pyrimido[4,5-b][1,4]diazepin-4-one = pyrimidodiazepine
Other name(s): PDA synthase; pyrimidodiazepine:oxidized-glutathione oxidoreductase (ring-opening, cyclizing); pyrimidodiazepine:glutathione-disulfide oxidoreductase (ring-opening, cyclizing)
Systematic name: 2-amino-6-acetyl-3,7,8,9-tetrahydro-3H-pyrimido[4,5-b][1,4]diazepin-4-one:glutathione-disulfide oxidoreductase (ring-opening, cyclizing)
Comments: In the reverse direction, the reduction of 6-pyruvoyl-tetrahydropterin is accompanied by the opening of the 6-membered pyrazine ring and the formation of the 7-membered diazepine ring. The pyrimidodiazepine formed is an acetyldihydro derivative. Involved in the formation of the eye pigment drosopterin in Drosophila melanogaster.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 93586-06-2
References:
1.  Wiederrecht, G.J. and Brown, G.M. Purification and properties of the enzymes from Drosophila melanogaster that catalyze the conversion of dihydroneopterin triphosphate to the pyrimidodiazepine precursor of the drosopterins. J. Biol. Chem. 259 (1984) 14121–14127. [PMID: 6438092]
2.  Kim, J., Suh, H., Kim, S., Kim, K., Ahn, C. and Yim, J. Identification and characteristics of the structural gene for the Drosophila eye colour mutant sepia, encoding PDA synthase, a member of the ω class glutathione S-transferases. Biochem. J. 398 (2006) 451–460. [DOI] [PMID: 16712527]
[EC 1.5.4.1 created 1990, modified 2014]
 
 
EC 1.6.1.5      
Transferred entry: proton-translocating NAD(P)+ transhydrogenase. Now EC 7.1.1.1, proton-translocating NAD(P)+ transhydrogenase
[EC 1.6.1.5 created 2015, deleted 2018]
 
 
EC 1.6.4.2      
Transferred entry: glutathione reductase (NADPH). Now EC 1.8.1.7, glutathione-disulfide reductase
[EC 1.6.4.2 created 1961, modified 1989, deleted 2002]
 
 
EC 1.6.4.6      
Transferred entry: CoA-glutathione reductase (NADPH). Now EC 1.8.1.10, CoA-glutathione reductase
[EC 1.6.4.6 created 1972, deleted 2002]
 
 
EC 1.7.1.9     
Accepted name: nitroquinoline-N-oxide reductase
Reaction: 4-(hydroxyamino)quinoline N-oxide + 2 NAD(P)+ + H2O = 4-nitroquinoline N-oxide + 2 NAD(P)H + 2 H+
Other name(s): 4-nitroquinoline 1-oxide reductase; 4NQO reductase; NAD(P)H2:4-nitroquinoline-N-oxide oxidoreductase
Systematic name: 4-(hydroxyamino)quinoline N-oxide:NADP+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-35-2
References:
1.  Toriyama, N. [Metabolism of quinoline derivatives. On the reducing enzyme of 4-nitroquinoline-N-oxide] Nichidai Igaku Zasshi 24 (1965) 423–432. (in Japanese)
2.  Stanley, J.S., York, J.L. and Benson, A.M. Nitroreductases and glutathione transferases that act on 4-nitroquinoline 1-oxide and their differential induction by butylated hydroxyanisole in mice. Cancer Res. 52 (1992) 58–63. [PMID: 1370076]
[EC 1.7.1.9 created 1972 as EC 1.6.6.10, transferred 2002 to EC 1.7.1.9]
 
 
EC 1.8.1.7     
Accepted name: glutathione-disulfide reductase
Reaction: 2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
For diagram of glutathione biosynthesis, click here
Glossary: The term ’oxidized glutathione’ has been replaced by the term ’glutathione disulfide’ as the former is ambiguous. S,S′-Biglutathione may also be used to refer to this compound.
Other name(s): glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase
Systematic name: glutathione:NADP+ oxidoreductase
Comments: A dimeric flavoprotein (FAD); activity is dependent on a redox-active disulfide in each of the active centres.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-48-3
References:
1.  Pai, E.F., Schirmer, R.H. and Schulz, G.E. Structural studies on crystalline glutathione reductase from human erythrocytes. In: Singer, T.P. and Ondarza, R.N. (Ed.), Mechanisms of Oxidizing Enzymes, Mechanisms of Oxidizing Enzymes, New York, 1978, pp. 17–22.
2.  Pigiet, V.P. and Conley, R.R. Purification of thioredoxin, thioredoxin reductase, and glutathione reductase by affinity chromatography. J. Biol. Chem. 252 (1977) 6367–6372. [PMID: 330529]
3.  Racker, E. Glutathione reductase from bakers' yeast and beef liver. J. Biol. Chem. 217 (1955) 855–865. [PMID: 13271446]
4.  van Heyningen, R. and Pirie, A. Reduction of glutathione coupled with oxidative decarboxylation of malate in cattle lens. Biochem. J. 53 (1953) 436–444. [PMID: 13032091]
5.  Worthington, D.J. and Rosemeyer, M.A. Glutathione reductase from human erythrocytes. Catalytic properties and aggregation. Eur. J. Biochem. 67 (1976) 231–238. [DOI] [PMID: 9277]
6.  Böhmé, C.C., Arscott, L.D., Becker, K., Schirmer, R.H. and Williams, C.H., Jr. Kinetic characterization of glutathione reductase from the malarial parasite Plasmodium falciparum. Comparison with the human enzyme. J. Biol. Chem. 275 (2000) 37317–37323. [DOI] [PMID: 10969088]
7.  Libreros-Minotta, C.A., Pardo, J.P., Mendoza-Hernandez, G. and Rendon, J.L. Purification and characterization of glutathione reductase from Rhodospirillum rubrum. Arch. Biochem. Biophys. 298 (1992) 247–253. [DOI] [PMID: 1524433]
[EC 1.8.1.7 created 1961 as EC 1.6.4.2, modified 1989, transferred 2002 to EC 1.8.1.7]
 
 
EC 1.8.1.8     
Accepted name: protein-disulfide reductase
Reaction: protein-dithiol + NAD(P)+ = protein-disulfide + NAD(P)H + H+
Other name(s): protein disulphide reductase; insulin-glutathione transhydrogenase; disulfide reductase; NAD(P)H2:protein-disulfide oxidoreductase
Systematic name: protein-dithiol:NAD(P)+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9029-19-0
References:
1.  Hatch, M.D. and Turner, J.F. A protein disulphide reductase from pea seeds. Biochem. J. 76 (1960) 556–562. [PMID: 13712218]
[EC 1.8.1.8 created 1965 as EC 1.6.4.4, transferred 2002 to EC 1.8.1.8]
 
 
EC 1.8.1.10     
Accepted name: CoA-glutathione reductase
Reaction: CoA + glutathione + NADP+ = CoA-glutathione + NADPH + H+
Other name(s): coenzyme A glutathione disulfide reductase; NADPH-dependent coenzyme A-SS-glutathione reductase; coenzyme A disulfide-glutathione reductase; NADPH2:CoA-glutathione oxidoreductase
Systematic name: glutathione:NADP+ oxidoreductase (CoA-acylating)
Comments: A flavoprotein. The substrate is a mixed disulfide. May be identical to EC 1.8.1.9, thioredoxin-disulfide reductase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-33-0
References:
1.  Ondarza, R.N., Abney, R. and López-Colomé, A.M. Characterization of a NADPH-dependent coenzyme A-SS-glutathione reductase from yeast. Biochim. Biophys. Acta 191 (1969) 239–248. [DOI] [PMID: 4390951]
2.  Ondarza, R.N., Escamilla, E., Gutierrez, J. and De la Chica, G. CoAS-Sglutathione and GSSG reductases from rat liver. Two disulfide oxidoreductase activities in one protein entity. Biochim. Biophys. Acta 341 (1974) 162–171. [DOI] [PMID: 4151341]
3.  Carlberg, I. and Mannervik, B. Purification by affinity chromatography of yeast glutathione reductase, the enzyme responsible for the NADPH-dependent reduction of the mixed disulfide of coenzyme A and glutathione. Biochim. Biophys. Acta 484 (1977) 268–274. [DOI] [PMID: 334266]
[EC 1.8.1.10 created 1972 as EC 1.6.4.6, transferred 2002 to EC 1.8.1.10]
 
 
EC 1.8.1.12     
Accepted name: trypanothione-disulfide reductase
Reaction: trypanothione + NADP+ = trypanothione disulfide + NADPH + H+
For diagram of trypanothione biosynthesis, click here
Glossary: spermidine = N-(3-aminopropyl)butane-1,4-diamine
trypanothione = N1,N8-bis(glutathionyl)spermidine
Other name(s): trypanothione reductase; NADPH2:trypanothione oxidoreductase
Systematic name: trypanothione:NADP+ oxidoreductase
Comments: Trypanothione disulfide is the oxidized form of N1,N8-bis(glutathionyl)-spermidine from the insect-parasitic trypanosomatid Crithidia fasciculata. The enzyme from Crithidia fasciculata is a flavoprotein (FAD), whose activity is dependent on a redox-active cystine at the active centre. (cf. EC 1.8.1.7, glutathione-disulfide reductase)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 102210-35-5
References:
1.  Shames, S.L., Fairlamb, A.H., Cerami, A. and Walsh, C.T. Purification and characterization of trypanothione reductase from Crithidia fasciculata, a newly discovered member of the family of disulfide-containing flavoprotein reductases. Biochemistry 25 (1986) 3519–3526. [PMID: 3718941]
2.  Marsh, I.R. and Bradley, M. Substrate specificity of trypanothione reductase. Eur. J. Biochem. 243 (1977) 690–694. [DOI] [PMID: 9057833]
3.  Cunningham, M.L. and Fairlamb, A.H. Trypanothione reductase from Leishmania donovani. Purification, characterisation and inhibition by trivalent antimonials. Eur. J. Biochem. 230 (1995) 460–468. [DOI] [PMID: 7607216]
[EC 1.8.1.12 created 1989 as EC 1.6.4.8, transferred 2002 to EC 1.8.1.12]
 
 
EC 1.8.1.13     
Accepted name: bis-γ-glutamylcystine reductase
Reaction: 2 γ-glutamylcysteine + NADP+ = bis-γ-glutamylcystine + NADPH + H+
Other name(s): NADPH2:bis-γ-glutamylcysteine oxidoreductase; GSR
Systematic name: γ-glutamylcysteine:NADP+ oxidoreductase
Comments: Contains FAD. The enzyme, which is found only in halobacteria, maintains the concentration of γ-glutamylcysteine, the major low molecular weight thiol in halobacteria. Not identical with EC 1.8.1.7 (glutathione-disulfide reductase) or EC 1.8.1.14 (CoA-disulfide reductase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 117056-54-9
References:
1.  Sundquist, A.R. and Fahey, R.C. The novel disulfide reductase bis-γ-glutamylcystine reductase and dihydrolipoamide dehydrogenase from Halobacterium halobium: purification by immobilized-metal-ion affinity chromatography and properties of the enzymes. J. Bacteriol. 170 (1988) 3459–3467. [DOI] [PMID: 3136140]
2.  Sundquist, A.R. and Fahey, R.C. The function of γ-glutamylcysteine and bis-γ-glutamylcystine reductase in Halobacterium halobium. J. Biol. Chem. 264 (1989) 719–725. [PMID: 2910862]
3.  Kim, J. and Copley, S.D. The orphan protein bis-γ-glutamylcystine reductase joins the pyridine nucleotide disulfide reductase family. Biochemistry 52 (2013) 2905–2913. [DOI] [PMID: 23560638]
[EC 1.8.1.13 created 1992 as EC 1.6.4.9, transferred 2002 to EC 1.8.1.13, modified 2013]
 
 
EC 1.8.1.14     
Accepted name: CoA-disulfide reductase
Reaction: 2 CoA + NADP+ = CoA-disulfide + NADPH + H+
Other name(s): CoA-disulfide reductase (NADH2); NADH2:CoA-disulfide oxidoreductase; CoA:NAD+ oxidoreductase (misleading); CoADR; coenzyme A disulfide reductase
Systematic name: CoA:NADP+ oxidoreductase
Comments: A flavoprotein. Not identical with EC 1.8.1.6 (cystine reductase), EC 1.8.1.7 (glutathione-disulfide reductase) or EC 1.8.1.13 (bis-γ-glutamylcystine reductase). The enzyme from the bacterium Staphylococcus aureus has a strong preference for NADPH [3], while the bacterium Bacillus megaterium contains both NADH and NADPH-dependent enzymes [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 206770-55-0
References:
1.  Setlow, B. and Setlow, P. Levels of acetyl coenzyme A, reduced and oxidized coenzyme A, and coenzyme A in disulfide linkage to protein in dormant and germinated spores and growing and sporulating cells of Bacillus megaterium. J. Bacteriol. 132 (1977) 444–452. [PMID: 410791]
2.  delCardayré, S.B., Stock, K.P., Newton, G.L., Fahey, R.C. and Davies, J.E. Coenzyme A disulfide reductase, the primary low molecular weight disulfide reductase from Staphylococcus aureus. Purification and characterization of the native enzyme. J. Biol. Chem. 273 (1998) 5744–5751. [DOI] [PMID: 9488707]
3.  Luba, J., Charrier, V. and Claiborne, A. Coenzyme A-disulfide reductase from Staphylococcus aureus: evidence for asymmetric behavior on interaction with pyridine nucleotides. Biochemistry 38 (1999) 2725–2737. [DOI] [PMID: 10052943]
[EC 1.8.1.14 created 1992 as EC 1.6.4.10, transferred 2002 to EC 1.8.1.14, modified 2005, modified 2013]
 
 
EC 1.8.1.15     
Accepted name: mycothione reductase
Reaction: 2 mycothiol + NAD(P)+ = mycothione + NAD(P)H + H+
Glossary: mycothiol = 1-O-[2-(N2-acetyl-L-cysteinamido)-2-deoxy--D-glucopyranosyl]-1D-myo-inositol
mycothione = oxidized (disulfide) form of mycothiol
Other name(s): mycothiol-disulfide reductase
Systematic name: mycothiol:NAD(P)+ oxidoreductase
Comments: Contains FAD. No activity with glutathione, trypanothione or coenzyme A as substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 252212-92-3
References:
1.  Patel, M.P. and Blanchard, J.S. Expression, purification, and characterization of Mycobacterium tuberculosis mycothione reductase. Biochemistry 38 (1999) 11827–11833. [DOI] [PMID: 10512639]
2.  Patel, M.P. and Blanchard, J.S. Mycobacterium tuberculosis mycothione reductase: pH dependence of the kinetic parameters and kinetic isotope effects. Biochemistry 40 (2001) 5119–5126. [DOI] [PMID: 11318633]
[EC 1.8.1.15 created 2002]
 
 
EC 1.8.1.16     
Accepted name: glutathione amide reductase
Reaction: 2 glutathione amide + NAD+ = glutathione amide disulfide + NADH + H+
Other name(s): GAR
Systematic name: glutathione amide:NAD+ oxidoreductase
Comments: A dimeric flavoprotein (FAD). The enzyme restores glutathione amide disulfide, which is produced during the reduction of peroxide by EC 1.11.1.17 (glutathione amide-dependent peroxidase), back to glutathione amide (it catalyses the reaction in the opposite direction to that shown). The enzyme belongs to the family of flavoprotein disulfide oxidoreductases, but unlike other members of the family, which are specific for NADPH, it prefers NADH [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Vergauwen, B., Pauwels, F., Jacquemotte, F., Meyer, T.E., Cusanovich, M.A., Bartsch, R.G. and Van Beeumen, J.J. Characterization of glutathione amide reductase from Chromatium gracile. Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling. J. Biol. Chem. 276 (2001) 20890–20897. [DOI] [PMID: 11399772]
2.  Vergauwen, B., Van Petegem, F., Remaut, H., Pauwels, F. and Van Beeumen, J.J. Crystallization and preliminary X-ray crystallographic analysis of glutathione amide reductase from Chromatium gracile. Acta Crystallogr. D Biol. Crystallogr. 58 (2002) 339–340. [PMID: 11807270]
[EC 1.8.1.16 created 2010]
 
 
EC 1.8.3.3     
Accepted name: glutathione oxidase
Reaction: 2 glutathione + O2 = glutathione disulfide + H2O2
Systematic name: glutathione:oxygen oxidoreductase
Comments: A flavoprotein (FAD). Also acts, more slowly, on L-cysteine and several other thiols.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 55467-56-6
References:
1.  Kusakabe, H., Kuninaka, A. and Yoshino, H. Purification and properties of a new enzyme, glutathione oxidase from Penicillium sp.K-6-5. Agric. Biol. Chem. 46 (1982) 2057–2067.
[EC 1.8.3.3 created 1989]
 
 
EC 1.8.3.7     
Accepted name: formylglycine-generating enzyme
Reaction: a [sulfatase]-L-cysteine + O2 + 2 a thiol = a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
Glossary: 3-oxo-L-alanine = formylglycine = Cα-formylglycine = FGly
Other name(s): sulfatase-modifying factor 1; Cα-formylglycine-generating enzyme 1; SUMF1 (gene name)
Systematic name: [sulfatase]-L-cysteine:oxygen oxidoreductase (3-oxo-L-alanine-forming)
Comments: Requires a copper cofactor and Ca2+. The enzyme, which is found in both prokaryotes and eukaryotes, catalyses a modification of a conserved L-cysteine residue in the active site of sulfatases, generating a unique 3-oxo-L-alanine residue that is essential for sulfatase activity. The exact nature of the thiol involved is still not clear - dithiothreitol and cysteamine are the most efficiently used thiols in vitro. Glutathione alo acts in vitro, but it is not known whether it is used in vivo.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Dierks, T., Schmidt, B. and von Figura, K. Conversion of cysteine to formylglycine: a protein modification in the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 94 (1997) 11963–11968. [DOI] [PMID: 9342345]
2.  Dierks, T., Miech, C., Hummerjohann, J., Schmidt, B., Kertesz, M.A. and von Figura, K. Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine. J. Biol. Chem. 273 (1998) 25560–25564. [DOI] [PMID: 9748219]
3.  Preusser-Kunze, A., Mariappan, M., Schmidt, B., Gande, S.L., Mutenda, K., Wenzel, D., von Figura, K. and Dierks, T. Molecular characterization of the human Cα-formylglycine-generating enzyme. J. Biol. Chem. 280 (2005) 14900–14910. [DOI] [PMID: 15657036]
4.  Roeser, D., Preusser-Kunze, A., Schmidt, B., Gasow, K., Wittmann, J.G., Dierks, T., von Figura, K. and Rudolph, M.G. A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme. Proc. Natl. Acad. Sci. USA 103 (2006) 81–86. [DOI] [PMID: 16368756]
5.  Carlson, B.L., Ballister, E.R., Skordalakes, E., King, D.S., Breidenbach, M.A., Gilmore, S.A., Berger, J.M. and Bertozzi, C.R. Function and structure of a prokaryotic formylglycine-generating enzyme. J. Biol. Chem. 283 (2008) 20117–20125. [DOI] [PMID: 18390551]
6.  Holder, P.G., Jones, L.C., Drake, P.M., Barfield, R.M., Banas, S., de Hart, G.W., Baker, J. and Rabuka, D. Reconstitution of formylglycine-generating enzyme with copper(II) for aldehyde tag conversion. J. Biol. Chem. 290 (2015) 15730–15745. [DOI] [PMID: 25931126]
7.  Knop, M., Engi, P., Lemnaru, R. and Seebeck, F.P. In vitro reconstitution of formylglycine-generating enzymes requires copper(I). ChemBioChem 16 (2015) 2147–2150. [DOI] [PMID: 26403223]
8.  Knop, M., Dang, T.Q., Jeschke, G. and Seebeck, F.P. Copper is a cofactor of the formylglycine-generating enzyme. ChemBioChem 18 (2017) 161–165. [DOI] [PMID: 27862795]
9.  Meury, M., Knop, M. and Seebeck, F.P. Structural basis for copper-oxygen mediated C-H bond activation by the formylglycine-generating enzyme. Angew. Chem. Int. Ed. Engl. (2017) . [DOI] [PMID: 28544744]
[EC 1.8.3.7 created 2014]
 
 
EC 1.8.4.1     
Accepted name: glutathione—homocystine transhydrogenase
Reaction: 2 glutathione + homocystine = glutathione disulfide + 2 homocysteine
Systematic name: glutathione:homocystine oxidoreductase
Comments: The reactions catalysed by this enzyme and by others in this subclass may be similar to those catalysed by EC 2.5.1.18 glutathione transferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9029-40-7
References:
1.  Racker, E. Glutathione-homocystine transhydrogenase. J. Biol. Chem. 217 (1955) 867–874. [PMID: 13271447]
[EC 1.8.4.1 created 1961]
 
 
EC 1.8.4.2     
Accepted name: protein-disulfide reductase (glutathione)
Reaction: 2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol
Other name(s): glutathione-insulin transhydrogenase; insulin reductase; reductase, protein disulfide (glutathione); protein disulfide transhydrogenase; glutathione-protein disulfide oxidoreductase; protein disulfide reductase (glutathione); GSH-insulin transhydrogenase; protein-disulfide interchange enzyme; protein-disulfide isomerase/oxidoreductase; thiol:protein-disulfide oxidoreductase; thiol-protein disulphide oxidoreductase
Systematic name: glutathione:protein-disulfide oxidoreductase
Comments: Reduces insulin and some other proteins.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9082-53-5
References:
1.  Katzen, H.M., Tietze, F. and Stetten, D. Further studies on the properties of hepatic glutathione-insulin transhydrogenase. J. Biol. Chem. 238 (1963) 1006–1011. [PMID: 14031343]
2.  Kohnert, K.-D., Hahn, H.-J., Zühlke, H., Schmidt, S. and Fiedler, H. Breakdown of exogenous insulin by Langerhans islets of the pancreas in vitro. Biochim. Biophys. Acta 338 (1974) 68–77.
[EC 1.8.4.2 created 1965]
 
 
EC 1.8.4.3     
Accepted name: glutathione—CoA-glutathione transhydrogenase
Reaction: CoA + glutathione disulfide = CoA-glutathione + glutathione
Other name(s): glutathione-coenzyme A glutathione disulfide transhydrogenase; glutathione-coenzyme A glutathione disulfide transhydrogenase; glutathione coenzyme A-glutathione transhydrogenase; glutathione:coenzyme A-glutathione transhydrogenase; coenzyme A:oxidized-glutathione oxidoreductase; coenzyme A:glutathione-disulfide oxidoreductase
Systematic name: CoA:glutathione-disulfide oxidoreductase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 37256-48-7
References:
1.  Chang, S.H. and Wilken, D.R. Participation of the unsymmetrical disulfide of coenzyme A and glutathione in an enzymatic sulfhydryl-disulfide interchange. I. Partial purification and properties of the bovine kidney enzyme. J. Biol. Chem. 241 (1966) 4251–4260. [PMID: 5924646]
[EC 1.8.4.3 created 1972]
 
 
EC 1.8.4.4     
Accepted name: glutathione—cystine transhydrogenase
Reaction: 2 glutathione + cystine = glutathione disulfide + 2 cysteine
Other name(s): GSH-cystine transhydrogenase; NADPH-dependent GSH-cystine transhydrogenase
Systematic name: glutathione:cystine oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-49-8
References:
1.  Nagai, S. and Black, S. A thiol-disulfide transhydrogenase from yeast. J. Biol. Chem. 243 (1968) 1942–1947. [PMID: 5646485]
[EC 1.8.4.4 created 1972]
 
 
EC 1.8.4.7     
Accepted name: enzyme-thiol transhydrogenase (glutathione-disulfide)
Reaction: [xanthine dehydrogenase] + glutathione disulfide = [xanthine oxidase] + 2 glutathione
Other name(s): [xanthine-dehydrogenase]:oxidized-glutathione S-oxidoreductase; enzyme-thiol transhydrogenase (oxidized-glutathione); glutathione-dependent thiol:disulfide oxidoreductase; thiol:disulphide oxidoreductase
Systematic name: [xanthine-dehydrogenase]:glutathione-disulfide S-oxidoreductase
Comments: Converts EC 1.17.1.4 xanthine dehydrogenase into EC 1.17.3.2 xanthine oxidase in the presence of glutathione disulfide; also reduces the disulfide bond of ricin. Not inhibited by Cu2+ or thiol reagents.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 85030-79-1
References:
1.  Battelli, M.G. and Lorenzoni, E. Purification and properties of a new glutathione-dependent thiol:disulphide oxidoreductase from rat liver. Biochem. J. 207 (1982) 133–138. [PMID: 6960894]
[EC 1.8.4.7 created 1989, modified 2002]
 
 
EC 1.8.4.9     
Accepted name: adenylyl-sulfate reductase (glutathione)
Reaction: AMP + sulfite + glutathione disulfide = adenylyl sulfate + 2 glutathione
Other name(s): 5′-adenylylsulfate reductase (also used for EC 1.8.99.2); AMP,sulfite:oxidized-glutathione oxidoreductase (adenosine-5′-phosphosulfate-forming); plant-type 5′-adenylylsulfate reductase
Systematic name: AMP,sulfite:glutathione-disulfide oxidoreductase (adenosine-5′-phosphosulfate-forming)
Comments: This enzyme differs from EC 1.8.99.2, adenylyl-sulfate reductase, in using glutathione as the reductant. Glutathione can be replaced by γ-glutamylcysteine or dithiothreitol, but not by thioredoxin, glutaredoxin or 2-sulfanylethan-1-ol (2-mercaptoethanol). The enzyme from the mouseear cress, Arabidopsis thaliana, contains a glutaredoxin-like domain. The enzyme is also found in other photosynthetic eukaryotes, e.g., the Madagascar periwinkle, Catharanthus roseus and the hollow green seaweed, Ulva intestinalis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 355840-27-6
References:
1.  Gutierrez-Marcos, J.F., Roberts, M.A., Campbell, E.I. and Wray, J.L. Three members of a novel small gene-family from Arabidopsis thaliana able to complement functionally an Escherichia coli mutant defective in PAPS reductase activity encode proteins with a thioredoxin-like domain and 'APS reductase' activity. Proc. Natl. Acad. Sci. USA 93 (1996) 13377–13382. [DOI] [PMID: 8917599]
2.  Setya, A., Murillo, M. and Leustek, T. Sulfate reduction in higher plants: Molecular evidence for a novel 5-adenylylphosphosulfate (APS) reductase. Proc. Natl. Acad. Sci. USA 93 (1996) 13383–13388. [DOI] [PMID: 8917600]
3.  Bick, J.A., Aslund, F., Cen, Y. and Leustek, T. Glutaredoxin function for the carboxyl-terminal domain of the plant-type 5′-adenylylsulfate reductase. Proc. Natl. Acad. Sci. USA 95 (1998) 8404–8409. [DOI] [PMID: 9653199]
[EC 1.8.4.9 created 2000, modified 2002]
 
 
EC 1.8.4.10     
Accepted name: adenylyl-sulfate reductase (thioredoxin)
Reaction: AMP + sulfite + thioredoxin disulfide = 5′-adenylyl sulfate + thioredoxin
Other name(s): thioredoxin-dependent 5′-adenylylsulfate reductase
Systematic name: AMP,sulfite:thioredoxin-disulfide oxidoreductase (adenosine-5′-phosphosulfate-forming)
Comments: Uses adenylyl sulfate, not phosphoadenylyl sulfate, distinguishing this enzyme from EC 1.8.4.8, phosphoadenylyl-sulfate reductase (thioredoxin). Uses thioredoxin as electron donor, not glutathione or other donors, distinguishing it from EC 1.8.4.9 [adenylyl-sulfate reductase (glutathione)] and EC 1.8.99.2 (adenylyl-sulfate reductase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bick, J.A., Dennis, J.J., Zylstra, G.J., Nowack, J. and Leustek, T. Identification of a new class of 5-adenylylsulfate (APS) reductase from sulfate-assimilating bacteria. J. Bacteriol. 182 (2000) 135–142. [DOI] [PMID: 10613872]
2.  Abola, A.P., Willits, M.G., Wang, R.C. and Long, S.R. Reduction of adenosine-5′-phosphosulfate instead of 3′-phosphoadenosine-5′-phosphosulfate in cysteine biosynthesis by Rhizobium meliloti and other members of the family Rhizobiaceae. J. Bacteriol. 181 (1999) 5280–5287. [PMID: 10464198]
3.  Williams, S.J., Senaratne, R.H., Mougous, J.D., Riley, L.W. and Bertozzi, C.R. 5′-Adenosinephosphosulfate lies at a metabolic branchpoint in mycobacteria. J. Biol. Chem. 277 (2002) 32606–32615. [DOI] [PMID: 12072441]
4.  Neumann, S., Wynen, A., Truper, H.G. and Dahl, C. Characterization of the cys gene locus from Allochromatium vinosum indicates an unusual sulfate assimilation pathway. Mol. Biol. Rep. 27 (2000) 27–33. [PMID: 10939523]
[EC 1.8.4.10 created 2003]
 
 
EC 1.8.5.1     
Accepted name: glutathione dehydrogenase (ascorbate)
Reaction: 2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
Other name(s): dehydroascorbic reductase; dehydroascorbic acid reductase; glutathione dehydroascorbate reductase; DHA reductase ; dehydroascorbate reductase; GDOR; glutathione:dehydroascorbic acid oxidoreductase
Systematic name: glutathione:dehydroascorbate oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9026-38-4
References:
1.  Crook, E.M. The system dehydroascorbic acid-glutathione. Biochem. J. 35 (1941) 226–236. [PMID: 16747320]
[EC 1.8.5.1 created 1961]
 
 
EC 1.8.5.7     
Accepted name: glutathionyl-hydroquinone reductase
Reaction: glutathione + 2-(glutathione-S-yl)-hydroquinone = glutathione disulfide + hydroquinone
Other name(s): pcpF (gene name); yqjG (gene name)
Systematic name: 2-(glutathione-S-yl)-hydroquinone:glutathione oxidoreductase
Comments: This type of enzymes, which are found in bacteria, halobacteria, fungi, and plants, catalyse the glutathione-dependent reduction of glutathionyl-hydroquinones. The enzyme from the bacterium Sphingobium chlorophenolicum can act on halogenated substrates such as 2,6-dichloro-3-(glutathione-S-yl)-hydroquinone and 2,3,5-trichloro-6-(glutathione-S-yl)-hydroquinone. Substrates for these enzymes are often formed spontaneously by interaction of benzoquinones with glutathione.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Huang, Y., Xun, R., Chen, G. and Xun, L. Maintenance role of a glutathionyl-hydroquinone lyase (PcpF) in pentachlorophenol degradation by Sphingobium chlorophenolicum ATCC 39723. J. Bacteriol. 190 (2008) 7595–7600. [DOI] [PMID: 18820023]
2.  Xun, L., Belchik, S.M., Xun, R., Huang, Y., Zhou, H., Sanchez, E., Kang, C. and Board, P.G. S-Glutathionyl-(chloro)hydroquinone reductases: a novel class of glutathione transferases. Biochem. J. 428 (2010) 419–427. [DOI] [PMID: 20388120]
3.  Lam, L.K., Zhang, Z., Board, P.G. and Xun, L. Reduction of benzoquinones to hydroquinones via spontaneous reaction with glutathione and enzymatic reaction by S-glutathionyl-hydroquinone reductases. Biochemistry 51 (2012) 5014–5021. [DOI] [PMID: 22686328]
4.  Green, A.R., Hayes, R.P., Xun, L. and Kang, C. Structural understanding of the glutathione-dependent reduction mechanism of glutathionyl-hydroquinone reductases. J. Biol. Chem. 287 (2012) 35838–35848. [DOI] [PMID: 22955277]
[EC 1.8.5.7 created 2017]
 
 
EC 1.8.5.8     
Accepted name: eukaryotic sulfide quinone oxidoreductase
Reaction: hydrogen sulfide + glutathione + a quinone = S-sulfanylglutathione + a quinol
Other name(s): SQR; SQOR; SQRDL (gene name)
Systematic name: sulfide:glutathione,quinone oxidoreductase
Comments: Contains FAD. This eukaryotic enzyme, located at the inner mitochondrial membrane, catalyses the first step in the metabolism of sulfide. While both sulfite and glutathione have been shown to act as sulfane sulfur acceptors in vitro, it is thought that the latter acts as the main acceptor in vivo. The electrons are transferred via FAD and quinones to the electron transfer chain. Unlike the bacterial homolog (EC 1.8.5.4, bacterial sulfide:quinone reductase), which repeats the catalytic cycle without releasing the product, producing a polysulfide, the eukaryotic enzyme transfers the persulfide to an acceptor at the end of each catalytic cycle.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Vande Weghe, J.G. and Ow, D.W. A fission yeast gene for mitochondrial sulfide oxidation. J. Biol. Chem. 274 (1999) 13250–13257. [DOI] [PMID: 10224084]
2.  Hildebrandt, T.M. and Grieshaber, M.K. Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria. FEBS J. 275 (2008) 3352–3361. [DOI] [PMID: 18494801]
3.  Jackson, M.R., Melideo, S.L. and Jorns, M.S. Human sulfide:quinone oxidoreductase catalyzes the first step in hydrogen sulfide metabolism and produces a sulfane sulfur metabolite. Biochemistry 51 (2012) 6804–6815. [DOI] [PMID: 22852582]
4.  Libiad, M., Yadav, P.K., Vitvitsky, V., Martinov, M. and Banerjee, R. Organization of the human mitochondrial hydrogen sulfide oxidation pathway. J. Biol. Chem. 289 (2014) 30901–30910. [DOI] [PMID: 25225291]
[EC 1.8.5.8 created 2017]
 
 
EC 1.8.6.1      
Deleted entry:  Nitrate-ester reductase. Now included with EC 2.5.1.18 glutathione transferase
[EC 1.8.6.1 created 1961, deleted 1976]
 
 
EC 1.11.1.9     
Accepted name: glutathione peroxidase
Reaction: 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
Other name(s): GSH peroxidase; selenium-glutathione peroxidase; reduced glutathione peroxidase
Systematic name: glutathione:hydrogen-peroxide oxidoreductase
Comments: A protein containing a selenocysteine residue. Steroid and lipid hydroperoxides, but not the product of reaction of EC 1.13.11.12 lipoxygenase on phospholipids, can act as acceptor, but more slowly than H2O2 (cf. EC 1.11.1.12 phospholipid-hydroperoxide glutathione peroxidase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9013-66-5
References:
1.  Chaudiere, J. and Tappel, A.L. Purification and characterization of selenium-glutathione peroxidase from hamster liver. Arch. Biochem. Biophys. 226 (1983) 448–457. [DOI] [PMID: 6227287]
2.  Grossmann, A. and Wendel, A. Non-reactivity of the selenoenzyme glutathione peroxidase with enzymatically hydroperoxidized phospholipids. Eur. J. Biochem. 135 (1983) 549–552. [DOI] [PMID: 6413205]
3.  Nakamura, W., Hosoda, S. and Hayashi, K. Purification and properties of rat liver glutathione peroxidase. Biochim. Biophys. Acta 358 (1974) 251–261.
[EC 1.11.1.9 created 1965, modified 1989]
 
 
EC 1.11.1.12     
Accepted name: phospholipid-hydroperoxide glutathione peroxidase
Reaction: 2 glutathione + a hydroperoxy-fatty-acyl-[lipid] = glutathione disulfide + a hydroxy-fatty-acyl-[lipid] + H2O
Other name(s): peroxidation-inhibiting protein; PHGPX; peroxidation-inhibiting protein:peroxidase,glutathione (phospholipid hydroperoxide-reducing); phospholipid hydroperoxide glutathione peroxidase; hydroperoxide glutathione peroxidase
Systematic name: glutathione:lipid-hydroperoxide oxidoreductase
Comments: A protein containing a selenocysteine residue. The products of action of EC 1.13.11.12 lipoxygenase on phospholipids can act as acceptors; H2O2 can also act, but much more slowly (cf. EC 1.11.1.9 glutathione peroxidase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 97089-70-8
References:
1.  Ursini, F., Maiorino, M. and Gregolin, C. The selenoenzyme phospholipid hydroperoxide glutathione peroxidase. Biochim. Biophys. Acta 839 (1985) 62–70. [DOI] [PMID: 3978121]
2.  Schnurr, K., Belkner, J., Ursini, F., Schewe, T. and Kuhn, H. The selenoenzyme phospholipid hydroperoxide glutathione peroxidase controls the activity of the 15-lipoxygenase with complex substrates and preserves the specificity of the oxygenation products. J. Biol. Chem. 271 (1996) 4653–4658. [DOI] [PMID: 8617728]
[EC 1.11.1.12 created 1989, modified 2015]
 
 
EC 1.11.1.15      
Transferred entry: peroxiredoxin. Now described by EC 1.11.1.24, thioredoxin-dependent peroxiredoxin; EC 1.11.1.25, glutaredoxin-dependent peroxiredoxin; EC 1.11.1.26, NADH-dependent peroxiredoxin; EC 1.11.1.27, glutathione-dependent peroxiredoxin; EC 1.11.1.28, lipoyl-dependent peroxiredoxin; and EC 1.11.1.29, mycoredoxin-dependent peroxiredoxin.
[EC 1.11.1.15 created 2004, deleted 2020]
 
 
EC 1.11.1.17     
Accepted name: glutathione amide-dependent peroxidase
Reaction: 2 glutathione amide + H2O2 = glutathione amide disulfide + 2 H2O
Systematic name: glutathione amide:hydrogen-peroxide oxidoreductase
Comments: This enzyme, which has been characterized from the proteobacterium Marichromatium gracile, is a chimeric protein, containing a peroxiredoxin-like N-terminus and a glutaredoxin-like C terminus. The enzyme has peroxidase activity towards hydrogen peroxide and several small alkyl hydroperoxides, and is thought to represent an early adaptation for fighting oxidative stress [1]. The glutathione amide disulfide produced by this enzyme can be restored to glutathione amide by EC 1.8.1.16 (glutathione amide reductase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Vergauwen, B., Pauwels, F., Jacquemotte, F., Meyer, T.E., Cusanovich, M.A., Bartsch, R.G. and Van Beeumen, J.J. Characterization of glutathione amide reductase from Chromatium gracile. Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling. J. Biol. Chem. 276 (2001) 20890–20897. [DOI] [PMID: 11399772]
[EC 1.11.1.17 created 2010]
 
 
EC 1.11.1.22     
Accepted name: hydroperoxy fatty acid reductase
Reaction: a hydroperoxy fatty acid + NADPH + H+ = a hydroxy fatty acid + NADP+ + H2O
Other name(s): slr1171 (gene name); slr1992 (gene name); hydroperoxy fatty acid:NADPH oxidoreductase
Systematic name: NADPH:hydroperoxy fatty acid oxidoreductase
Comments: The enzyme, characterized from the cyanobacterium Synechocystis PCC 6803, can reduce unsaturated fatty acid hydroperoxides and alkyl hydroperoxides. The enzyme, which utilizes NADPH generated by the photosynthetic electron transfer system, protects the cells from lipid peroxidation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Gaber, A., Tamoi, M., Takeda, T., Nakano, Y. and Shigeoka, S. NADPH-dependent glutathione peroxidase-like proteins (Gpx-1, Gpx-2) reduce unsaturated fatty acid hydroperoxides in Synechocystis PCC 6803. FEBS Lett. 499 (2001) 32–36. [DOI] [PMID: 11418106]
2.  Gaber, A., Yoshimura, K., Tamoi, M., Takeda, T., Nakano, Y. and Shigeoka, S. Induction and functional analysis of two reduced nicotinamide adenine dinucleotide phosphate-dependent glutathione peroxidase-like proteins in Synechocystis PCC 6803 during the progression of oxidative stress. Plant Physiol. 136 (2004) 2855–2861. [DOI] [PMID: 15347790]
[EC 1.11.1.22 created 2013]
 
 
EC 1.11.1.25     
Accepted name: glutaredoxin-dependent peroxiredoxin
Reaction: glutaredoxin + ROOH = glutaredoxin disulfide + H2O + ROH
For diagram of reaction, click here and for mechanism, click here
Other name(s): PRXIIB (gene name)
Systematic name: glutaredoxin:hydroperoxide oxidoreductase
Comments: Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins [2]. The peroxidase reaction comprises two steps centred around a redox-active cysteine called the peroxidatic cysteine. All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid) (see mechanism). The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the ‘resolving’ cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants completing the catalytic cycle. In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor. The 1-Cys Prxs conserve only the peroxidatic cysteine, so its regeneration involves direct interaction with a reductant molecule. Glutaredoxin-dependent peroxiredoxins have been reported from bacteria, fungi, plants, and animals. These enzymes are often able to use an alternative reductant such as thioredoxin or glutathione.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 207137-51-7
References:
1.  Rouhier, N., Gelhaye, E. and Jacquot, J.P. Glutaredoxin-dependent peroxiredoxin from poplar: protein-protein interaction and catalytic mechanism. J. Biol. Chem. 277 (2002) 13609–13614. [PMID: 11832487]
2.  Wood, Z.A., Schröder, E., Harris, J.R. and Poole, L.B. Structure, mechanism and regulation of peroxiredoxins. Trends Biochem. Sci. 28 (2003) 32–40. [DOI] [PMID: 12517450]
3.  Pedrajas, J.R., Padilla, C.A., McDonagh, B. and Barcena, J.A. Glutaredoxin participates in the reduction of peroxides by the mitochondrial 1-CYS peroxiredoxin in Saccharomyces cerevisiae. Antioxid Redox Signal 13 (2010) 249–258. [PMID: 20059400]
4.  Hanschmann, E.M., Lonn, M.E., Schutte, L.D., Funke, M., Godoy, J.R., Eitner, S., Hudemann, C. and Lillig, C.H. Both thioredoxin 2 and glutaredoxin 2 contribute to the reduction of the mitochondrial 2-Cys peroxiredoxin Prx3. J. Biol. Chem. 285 (2010) 40699–40705. [PMID: 20929858]
5.  Lim, J.G., Bang, Y.J. and Choi, S.H. Characterization of the Vibrio vulnificus 1-Cys peroxiredoxin Prx3 and regulation of its expression by the Fe-S cluster regulator IscR in response to oxidative stress and iron starvation. J. Biol. Chem. 289 (2014) 36263–36274. [PMID: 25398878]
6.  Couturier, J., Prosper, P., Winger, A.M., Hecker, A., Hirasawa, M., Knaff, D.B., Gans, P., Jacquot, J.P., Navaza, A., Haouz, A. and Rouhier, N. In the absence of thioredoxins, what are the reductants for peroxiredoxins in Thermotoga maritima. Antioxid Redox Signal 18 (2013) 1613–1622. [PMID: 22866991]
[EC 1.11.1.25 created 1983 as EC 1.11.1.15, part transferred 2020 to EC 1.11.1.25]
 
 
EC 1.11.1.27     
Accepted name: glutathione-dependent peroxiredoxin
Reaction: 2 glutathione + ROOH = glutathione disulfide + H2O + ROH
For diagram of reaction, click here and for mechanism, click here
Other name(s): PRDX6 (gene name); prx3 (gene name)
Systematic name: glutathione:hydroperoxide oxidoreductase
Comments: Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins [1]. The peroxidase reaction comprises two steps centred around a redox-active cysteine called the peroxidatic cysteine. All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid) (see mechanism). The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the ‘resolving’ cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants completing the catalytic cycle. In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. The 1-Cys Prxs conserve only the peroxidatic cysteine, so its regeneration involves direct interaction with a reductant molecule. Glutathione-dependent peroxiredoxins have been reported from bacteria and animals, and appear to be 1-Cys enzymes. The mechanism for the mammalian PRDX6 enzyme involves heterodimerization of the enzyme with π-glutathione S-transferase, followed by glutathionylation of the oxidized cysteine residue. Subsequent dissociation of the heterodimer yields glutathionylated peroxiredoxin, which is restored to the active form via spontaneous reduction by a second glutathione molecule.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 207137-51-7
References:
1.  Wood, Z.A., Schröder, E., Harris, J.R. and Poole, L.B. Structure, mechanism and regulation of peroxiredoxins. Trends Biochem. Sci. 28 (2003) 32–40. [DOI] [PMID: 12517450]
2.  Pauwels, F., Vergauwen, B., Vanrobaeys, F., Devreese, B. and Van Beeumen, J.J. Purification and characterization of a chimeric enzyme from Haemophilus influenzae Rd that exhibits glutathione-dependent peroxidase activity. J. Biol. Chem. 278 (2003) 16658–16666. [PMID: 12606554]
3.  Manevich, Y., Feinstein, S.I. and Fisher, A.B. Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with π GST. Proc. Natl. Acad. Sci. USA 101 (2004) 3780–3785. [PMID: 15004285]
4.  Greetham, D. and Grant, C.M. Antioxidant activity of the yeast mitochondrial one-Cys peroxiredoxin is dependent on thioredoxin reductase and glutathione in vivo. Mol. Cell Biol. 29 (2009) 3229–3240. [PMID: 19332553]
5.  Lim, J.G., Bang, Y.J. and Choi, S.H. Characterization of the Vibrio vulnificus 1-Cys peroxiredoxin Prx3 and regulation of its expression by the Fe-S cluster regulator IscR in response to oxidative stress and iron starvation. J. Biol. Chem. 289 (2014) 36263–36274. [PMID: 25398878]
[EC 1.11.1.27 created 1983 as EC 1.11.1.15, part transferred 2020 to EC 1.11.1.27]
 
 
EC 1.13.11.18     
Accepted name: persulfide dioxygenase
Reaction: S-sulfanylglutathione + O2 + H2O = glutathione + sulfite + 2 H+ (overall reaction)
(1a) S-sulfanylglutathione + O2 = S-sulfinatoglutathione + H+
(1b) S-sulfinatoglutathione + H2O = glutathione + sulfite + H+ (spontaneous)
Other name(s): sulfur oxygenase (incorrect); sulfur:oxygen oxidoreductase (incorrect); sulfur dioxygenase (incorrect)
Systematic name: S-sulfanylglutathione:oxygen oxidoreductase
Comments: An iron protein. Perthiols, formed spontaneously by interactions between thiols and elemental sulfur or sulfide, are the only acceptable substrate to the enzyme. The sulfite that is formed by the enzyme can be further converted into sulfate, thiosulfate or S-sulfoglutathione (GSSO3-) non-enzymically [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-58-9
References:
1.  Suzuki, I. and Silver, M. The initial product and properties of the sulfur-oxidizing enzyme of thiobacilli. Biochim. Biophys. Acta 122 (1966) 22–33. [PMID: 5968172]
2.  Rohwerder, T. and Sand, W. The sulfane sulfur of persulfides is the actual substrate of the sulfur-oxidizing enzymes from Acidithiobacillus and Acidiphilium spp. Microbiology 149 (2003) 1699–1710. [DOI] [PMID: 12855721]
3.  Liu, H., Xin, Y. and Xun, L. Distribution, diversity, and activities of sulfur dioxygenases in heterotrophic bacteria. Appl. Environ. Microbiol. 80 (2014) 1799–1806. [DOI] [PMID: 24389926]
4.  Holdorf, M.M., Owen, H.A., Lieber, S.R., Yuan, L., Adams, N., Dabney-Smith, C. and Makaroff, C.A. Arabidopsis ETHE1 encodes a sulfur dioxygenase that is essential for embryo and endosperm development. Plant Physiol. 160 (2012) 226–236. [DOI] [PMID: 22786886]
5.  Pettinati, I., Brem, J., McDonough, M.A. and Schofield, C.J. Crystal structure of human persulfide dioxygenase: structural basis of ethylmalonic encephalopathy. Hum. Mol. Genet. 24 (2015) 2458–2469. [DOI] [PMID: 25596185]
[EC 1.13.11.18 created 1972, modified 2015]
 
 
EC 1.13.11.19     
Accepted name: cysteamine dioxygenase
Reaction: cysteamine + O2 = hypotaurine
For diagram of taurine biosynthesis, click here
Glossary: cysteamine = 2-aminoethanethiol
Other name(s): ADO (gene name); persulfurase; cysteamine oxygenase; cysteamine:oxygen oxidoreductase
Systematic name: 2-aminoethanethiol:oxygen oxidoreductase
Comments: A non-heme iron protein that is involved in the biosynthesis of taurine. 3-Aminopropanethiol (homocysteamine) and 2-sulfanylethan-1-ol (2-mercaptoethanol) can also act as substrates, but glutathione, cysteine, and cysteine ethyl- and methyl esters are not good substrates [1,3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9033-41-4
References:
1.  Cavallini, D., de Marco, C., Scandurra, R., Duprè, S. and Graziani, M.T. The enzymatic oxidation of cysteamine to hypotaurine. Purification and properties of the enzyme. J. Biol. Chem. 241 (1966) 3189–3196. [PMID: 5912113]
2.  Wood, J.L. and Cavallini, D. Enzymic oxidation of cysteamine to hypotaurine in the absence of a cofactor. Arch. Biochem. Biophys. 119 (1967) 368–372. [DOI] [PMID: 6052430]
3.  Cavallini, D., Federici, G., Ricci, G., Duprè, S. and Antonucci, A. The specificity of cysteamine oxygenase. FEBS Lett. 56 (1975) 348–351. [DOI] [PMID: 1157952]
4.  Richerson, R.B. and Ziegler, D.M. Cysteamine dioxygenase. Methods Enzymol. 143 (1987) 410–415. [DOI] [PMID: 3657558]
5.  Dominy, J.E., Jr., Simmons, C.R., Hirschberger, L.L., Hwang, J., Coloso, R.M. and Stipanuk, M.H. Discovery and characterization of a second mammalian thiol dioxygenase, cysteamine dioxygenase. J. Biol. Chem. 282 (2007) 25189–25198. [PMID: 17581819]
[EC 1.13.11.19 created 1972, modified 2006]
 
 
EC 1.14.14.43     
Accepted name: (methylsulfanyl)alkanaldoxime N-monooxygenase
Reaction: an (E)-ω-(methylsulfanyl)alkanal oxime + [reduced NADPH—hemoprotein reductase] + glutathione + O2 = an S-[(1E)-1-(hydroxyimino)-ω-(methylsulfanyl)alkyl]-L-glutathione + [oxidized NADPH—hemoprotein reductase] + 2 H2O (overall reaction)
(1a) an (E)-ω-(methylsulfanyl)alkanal oxime + [reduced NADPH—hemoprotein reductase] + O2 = a 1-(methylsulfanyl)-4-aci-nitroalkane + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) a 1-(methylsulfanyl)-4-aci-nitroalkane + glutathione = an S-[(1E)-1-(hydroxyimino)-ω-(methylsulfanyl)alkyl]-L-glutathione + H2O
Glossary: a 1-(methylsulfanyl)-4-aci-nitroalkane = a hydroxyoxo-λ5-azanylidene-ω-(methylsulfanyl)alkane
Other name(s): CYP83A1 (gene name); (methylthio)alkanaldoxime N-monooxygenase; (E)-ω-(methylthio)alkananaldoxime,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)
Systematic name: (E)-ω-(methylsulfanyl)alkananal oxime,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)
Comments: This cytochrome P-450 (heme thiolate) enzyme is involved in the biosynthesis of glucosinolates in plants. The enzyme catalyses an N-hydroxylation of the E isomer of ω-(methylsulfanyl)alkanal oximes, forming an aci-nitro intermediate that reacts non-enzymically with glutathione to produce an N-alkyl-thiohydroximate adduct, the committed precursor of glucosinolates. In the absence of a thiol compound, the enzyme is suicidal, probably due to interaction of the reactive aci-nitro intermediate with active site residues.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bak, S., Tax, F.E., Feldmann, K.A., Galbraith, D.W. and Feyereisen, R. CYP83B1, a cytochrome P450 at the metabolic branch point in auxin and indole glucosinolate biosynthesis in Arabidopsis. Plant Cell 13 (2001) 101–111. [PMID: 11158532]
2.  Naur, P., Petersen, B.L., Mikkelsen, M.D., Bak, S., Rasmussen, H., Olsen, C.E. and Halkier, B.A. CYP83A1 and CYP83B1, two nonredundant cytochrome P450 enzymes metabolizing oximes in the biosynthesis of glucosinolates in Arabidopsis. Plant Physiol. 133 (2003) 63–72. [DOI] [PMID: 12970475]
3.  Clausen, M., Kannangara, R.M., Olsen, C.E., Blomstedt, C.K., Gleadow, R.M., Jørgensen, K., Bak, S., Motawie, M.S. and Møller, B.L. The bifurcation of the cyanogenic glucoside and glucosinolate biosynthetic pathways. Plant J. 84 (2015) 558–573. [DOI] [PMID: 26361733]
[EC 1.14.14.43 created 2017]
 
 
EC 1.14.14.45     
Accepted name: aromatic aldoxime N-monooxygenase
Reaction: (1) (E)-indol-3-ylacetaldehyde oxime + [reduced NADPH—hemoprotein reductase] + glutathione + O2 = S-[(E)-N-hydroxy(indol-3-yl)acetimidoyl]-L-glutathione + [oxidized NADPH—hemoprotein reductase] + 2 H2O (overall reaction)
(1a) (E)-indol-3-ylacetaldehyde oxime + [reduced NADPH—hemoprotein reductase] + O2 = 1-(1H-indol-3-yl)-2-aci-nitroethane + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) 1-(1H-indol-3-yl)-2-aci-nitroethane + glutathione = S-[(E)-N-hydroxy(indol-3-yl)acetimidoyl]-L-glutathione + H2O (spontaneous)
(2) (E)-phenylacetaldehyde oxime + [reduced NADPH—hemoprotein reductase] + glutathione + O2 = S-[(Z)-N-hydroxy(phenyl)acetimidoyl]-L-glutathione + [oxidized NADPH—hemoprotein reductase] + 2 H2O (overall reaction)
(2a) (E)-phenylacetaldehyde oxime + [reduced NADPH—hemoprotein reductase] + O2 = 1-aci-nitro-2-phenylethane + [oxidized NADPH—hemoprotein reductase] + H2O
(2b) 1-aci-nitro-2-phenylethane + glutathione = S-[(Z)-N-hydroxy(phenyl)acetimidoyl]-L-glutathione + H2O (spontaneous)
Other name(s): CYP83B1 (gene name)
Systematic name: (E)-indol-3-ylacetaldoxime,[reduced NADPH—hemoprotein reductase],glutathione:oxygen oxidoreductase (oxime-hydroxylating)
Comments: This cytochrome P-450 (heme thiolate) enzyme is involved in the biosynthesis of glucosinolates in plants. The enzyme catalyses the N-hydroxylation of aromatic aldoximes derived from L-tryptophan, L-phenylalanine, and L-tyrosine, forming an aci-nitro intermediate that reacts non-enzymically with glutathione to produce an N-alkyl-thiohydroximate adduct, the committed precursor of glucosinolates. In the absence of glutathione, the enzyme is suicidal, probably due to interaction of the reactive aci-nitro compound with catalytic residues in the active site.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bak, S., Tax, F.E., Feldmann, K.A., Galbraith, D.W. and Feyereisen, R. CYP83B1, a cytochrome P450 at the metabolic branch point in auxin and indole glucosinolate biosynthesis in Arabidopsis. Plant Cell 13 (2001) 101–111. [PMID: 11158532]
2.  Naur, P., Petersen, B.L., Mikkelsen, M.D., Bak, S., Rasmussen, H., Olsen, C.E. and Halkier, B.A. CYP83A1 and CYP83B1, two nonredundant cytochrome P450 enzymes metabolizing oximes in the biosynthesis of glucosinolates in Arabidopsis. Plant Physiol. 133 (2003) 63–72. [DOI] [PMID: 12970475]
3.  Geu-Flores, F., Møldrup, M.E., Böttcher, C., Olsen, C.E., Scheel, D. and Halkier, B.A. Cytosolic γ-glutamyl peptidases process glutathione conjugates in the biosynthesis of glucosinolates and camalexin in Arabidopsis. Plant Cell 23 (2011) 2456–2469. [DOI] [PMID: 21712415]
[EC 1.14.14.45 created 2017]
 
 
EC 1.14.16.5     
Accepted name: alkylglycerol monooxygenase
Reaction: 1-O-alkyl-sn-glycerol + a 5,6,7,8-tetrahydropteridine + O2 = 1-O-(1-hydroxyalkyl)-sn-glycerol + a 4a-hydroxy-5,6,7,8-tetrahydropteridine
Other name(s): glyceryl-ether monooxygenase; glyceryl-ether cleaving enzyme; glyceryl ether oxygenase; glyceryl etherase; O-alkylglycerol monooxygenase
Systematic name: 1-alkyl-sn-glycerol,tetrahydrobiopteridine:oxygen oxidoreductase
Comments: The enzyme cleaves alkylglycerols, but does not cleave alkenylglycerols (plasmalogens). Requires non-heme iron [7], reduced glutathione and phospholipids for full activity. The product spontaneously breaks down to form a fatty aldehyde and glycerol. The co-product, 4a-hydroxytetrahydropteridine, is rapidly dehydrated to 6,7-dihydropteridine, either spontaneously or by EC 4.2.1.96, 4a-hydroxytetrahydrobiopterin dehydratase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-82-9
References:
1.  Ishibashi, T. and Imai, Y. Solubilization and partial characterization of alkylglycerol monooxygenase from rat liver microsomes. Eur. J. Biochem. 132 (1983) 23–27. [DOI] [PMID: 6840084]
2.  Pfleger, E.C., Piantadosi, C. and Snyder, F. The biocleavage of isomeric glyceryl ethers by soluble liver enzymes in a variety of species. Biochim. Biophys. Acta 144 (1967) 633–648. [DOI] [PMID: 4383918]
3.  Snyder, F., Malone, B. and Piantadosi, C. Tetrahydropteridine-dependent cleavage enzyme for O-alkyl lipids: substrate specificity. Biochim. Biophys. Acta 316 (1973) 259–265. [DOI] [PMID: 4355017]
4.  Soodsma, J.F., Piantadosi, C. and Snyder, F. Partial characterization of the alkylglycerol cleavage enzyme system of rat liver. J. Biol. Chem. 247 (1972) 3923–3929. [PMID: 4402391]
5.  Tietz, A., Lindberg, M. and Kennedy, E.P. A new pteridine-requiring enzyme system for the oxidation of glyceryl ethers. J. Biol. Chem. 239 (1964) 4081–4090. [PMID: 14247652]
6.  Taguchi, H. and Armarego, W.L. Glyceryl-ether monooxygenase [EC 1.14.16.5]. A microsomal enzyme of ether lipid metabolism. Med. Res. Rev. 18 (1998) 43–89. [DOI] [PMID: 9436181]
7.  Watschinger, K., Keller, M.A., Hermetter, A., Golderer, G., Werner-Felmayer, G. and Werner, E.R. Glyceryl ether monooxygenase resembles aromatic amino acid hydroxylases in metal ion and tetrahydrobiopterin dependence. Biol. Chem. 390 (2009) 3–10. [DOI] [PMID: 19007315]
8.  Werner, E.R., Hermetter, A., Prast, H., Golderer, G. and Werner-Felmayer, G. Widespread occurrence of glyceryl ether monooxygenase activity in rat tissues detected by a novel assay. J. Lipid Res. 48 (2007) 1422–1427. [DOI] [PMID: 17303893]
[EC 1.14.16.5 created 1972 as EC 1.14.99.17, transferred 1976 to EC 1.14.16.5, modified 2010, modified 2020]
 
 
EC 1.16.1.1     
Accepted name: mercury(II) reductase
Reaction: Hg + NADP+ + H+ = Hg2+ + NADPH
Other name(s): mercuric reductase; mercurate(II) reductase; mercuric ion reductase; mercury reductase; reduced NADP:mercuric ion oxidoreductase; mer A
Systematic name: Hg:NADP+ oxidoreductase
Comments: A dithiol enzyme.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 67880-93-7
References:
1.  Fox, B.S. and Walsh, C.T. Mercuric reductase. Purification and characterization of a transposon-encoded flavoprotein containing an oxidation-reduction-active disulfide. J. Biol. Chem. 257 (1982) 2498–2503. [PMID: 6277900]
2.  Fox, B.S. and Walsh, C.T. Mercuric reductase - homology to glutathione-reductase and lipoamide dehydrogenase - iodoacetamide alkylation and sequence of the active-site peptide. Biochemistry 22 (1983) 4082–4088. [PMID: 6412751]
[EC 1.16.1.1 created 1984]
 
 
EC 1.16.1.6     
Accepted name: cyanocobalamin reductase
Reaction: 2 cob(II)alamin-[cyanocobalamin reductase] + 2 hydrogen cyanide + NADP+ = 2 cyanocob(III)alamin + 2 [cyanocobalamin reductase] + NADPH + H+
Other name(s): MMACHC (gene name); CblC; cyanocobalamin reductase (NADPH, cyanide-eliminating); cyanocobalamin reductase (NADPH, CN-eliminating); NADPH:cyanocob(III)alamin oxidoreductase (cyanide-eliminating); cob(I)alamin, cyanide:NADP+ oxidoreductase; cyanocobalamin reductase (cyanide-eliminating)
Systematic name: cob(II)alamin, hydrogen cyanide:NADP+ oxidoreductase
Comments: The mammalian enzyme, which is cytosolic, can bind internalized cyanocobalamin and process it to cob(II)alamin by removing the upper axial ligand. The product remains bound to the protein, which, together with its interacting partner MMADHC, transfers it directly to downstream enzymes involved in adenosylcobalamin and methylcobalamin biosynthesis. In addition to its decyanase function, the mammalian enzyme also catalyses an entirely different chemical reaction with alkylcobalamins, using the thiolate of glutathione for nucleophilic displacement, generating cob(I)alamin and the corresponding glutathione thioether (cf. EC 2.5.1.151, alkylcobalamin dealkylase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 131145-00-1
References:
1.  Watanabe, F., Oki, Y., Nakano, Y. and Kitaoka, S. Occurrence and characterization of cyanocobalamin reductase (NADPH; CN-eliminating) involved in decyanation of cyanocobalamin in Euglena gracilis. J. Nutr. Sci. Vitaminol. 34 (1988) 1–10. [PMID: 3134526]
2.  Kim, J., Gherasim, C. and Banerjee, R. Decyanation of vitamin B12 by a trafficking chaperone. Proc. Natl. Acad. Sci. USA 105 (2008) 14551–14554. [PMID: 18779575]
3.  Koutmos, M., Gherasim, C., Smith, J.L. and Banerjee, R. Structural basis of multifunctionality in a vitamin B12-processing enzyme. J. Biol. Chem. 286 (2011) 29780–29787. [PMID: 21697092]
4.  Mah, W., Deme, J.C., Watkins, D., Fung, S., Janer, A., Shoubridge, E.A., Rosenblatt, D.S. and Coulton, J.W. Subcellular location of MMACHC and MMADHC, two human proteins central to intracellular vitamin B12 metabolism. Mol Genet Metab 108 (2013) 112–118. [PMID: 23270877]
[EC 1.16.1.6 created 1989 as EC 1.6.99.12, transferred 2002 to EC 1.16.1.6, modified 2018, modified 2021]
 
 
EC 1.17.1.4     
Accepted name: xanthine dehydrogenase
Reaction: xanthine + NAD+ + H2O = urate + NADH + H+
For diagram of reaction, click here
Glossary: 4-mercuribenzoate = (4-carboxylatophenyl)mercury
Other name(s): NAD+-xanthine dehydrogenase; xanthine-NAD+ oxidoreductase; xanthine/NAD+ oxidoreductase; xanthine oxidoreductase
Systematic name: xanthine:NAD+ oxidoreductase
Comments: Acts on a variety of purines and aldehydes, including hypoxanthine. The mammalian enzyme can also convert all-trans retinol to all-trans-retinoate, while the substrate is bound to a retinoid-binding protein [14]. The enzyme from eukaryotes contains [2Fe-2S], FAD and a molybdenum centre. The mammalian enzyme predominantly exists as the NAD-dependent dehydrogenase (EC 1.17.1.4). During purification the enzyme is largely converted to an O2-dependent form, xanthine oxidase (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [2,6,8,15] [which can be catalysed by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide] or limited proteolysis, which results in irreversible conversion. The conversion can also occur in vivo [2,7,15].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9054-84-6
References:
1.  Battelli, M.G. and Lorenzoni, E. Purification and properties of a new glutathione-dependent thiol:disulphide oxidoreductase from rat liver. Biochem. J. 207 (1982) 133–138. [PMID: 6960894]
2.  Della Corte, E. and Stirpe, F. The regulation of rat liver xanthine oxidase. Involvement of thiol groups in the conversion of the enzyme activity from dehydrogenase (type D) into oxidase (type O) and purification of the enzyme. Biochem. J. 126 (1972) 739–745. [PMID: 4342395]
3.  Parzen, S.D. and Fox, A.S. Purification of xanthine dehydrogenase from Drosophila melanogaster. Biochim. Biophys. Acta 92 (1964) 465–471. [PMID: 14264879]
4.  Rajagopalan, K.V. and Handler, P. Purification and properties of chicken liver xanthine dehydrogenase. J. Biol. Chem. 242 (1967) 4097–4107. [PMID: 4294045]
5.  Smith, S.T., Rajagopalan, K.V. and Handler, P. Purification and properties of xanthine dehydroganase from Micrococcus lactilyticus. J. Biol. Chem. 242 (1967) 4108–4117. [PMID: 6061702]
6.  Ikegami, T. and Nishino, T. The presence of desulfo xanthine dehydrogenase in purified and crude enzyme preparations from rat liver. Arch. Biochem. Biophys. 247 (1986) 254–260. [DOI] [PMID: 3459393]
7.  Engerson, T.D., McKelvey, T.G., Rhyne, D.B., Boggio, E.B., Snyder, S.J. and Jones, H.P. Conversion of xanthine dehydrogenase to oxidase in ischemic rat tissues. J. Clin. Invest. 79 (1987) 1564–1570. [DOI] [PMID: 3294898]
8.  Saito, T., Nishino, T. and Tsushima, K. Interconversion between NAD-dependent and O2-dependent types of rat liver xanthine dehydrogenase and difference in kinetic and redox properties between them. Adv. Exp. Med. Biol. 253B (1989) 179–183. [PMID: 2610112]
9.  Parschat, K., Canne, C., Hüttermann, J., Kappl, R. and Fetzner, S. Xanthine dehydrogenase from Pseudomonas putida 86: specificity, oxidation-reduction potentials of its redox-active centers, and first EPR characterization. Biochim. Biophys. Acta 1544 (2001) 151–165. [DOI] [PMID: 11341925]
10.  Ichida, K., Amaya, Y., Noda, K., Minoshima, S., Hosoya, T., Sakai, O., Shimizu, N. and Nishino, T. Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene. Gene 133 (1993) 279–284. [DOI] [PMID: 8224915]
11.  Enroth, C., Eger, B.T., Okamoto, K., Nishino, T., Nishino, T. and Pai, E.F. Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion. Proc. Natl. Acad. Sci. USA 97 (2000) 10723–10728. [DOI] [PMID: 11005854]
12.  Truglio, J.J., Theis, K., Leimkuhler, S., Rappa, R., Rajagopalan, K.V. and Kisker, C. Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus. Structure 10 (2002) 115–125. [DOI] [PMID: 11796116]
13.  Hille, R. The mononuclear molybdenum enzymes. Chem. Rev. 96 (1996) 2757–2816. [DOI] [PMID: 11848841]
14.  Taibi, G., Di Gaudio, F. and Nicotra, C.M. Xanthine dehydrogenase processes retinol to retinoic acid in human mammary epithelial cells. J. Enzyme Inhib. Med. Chem. 23 (2008) 317–327. [DOI] [PMID: 18569334]
15.  Nishino, T., Okamoto, K., Eger, B.T., Pai, E.F. and Nishino, T. Mammalian xanthine oxidoreductase - mechanism of transition from xanthine dehydrogenase to xanthine oxidase. FEBS J. 275 (2008) 3278–3289. [DOI] [PMID: 18513323]
[EC 1.17.1.4 created 1972 as EC 1.2.1.37, transferred 1984 to EC 1.1.1.204, modified 1989, transferred 2004 to EC 1.17.1.4, modified 2011]
 
 
EC 1.17.3.2     
Accepted name: xanthine oxidase
Reaction: xanthine + H2O + O2 = urate + H2O2
For diagram of AMP catabolism, click here
Glossary: 4-mercuribenzoate = (4-carboxylatophenyl)mercury
Other name(s): hypoxanthine oxidase; hypoxanthine:oxygen oxidoreductase; Schardinger enzyme; xanthine oxidoreductase; hypoxanthine-xanthine oxidase; xanthine:O2 oxidoreductase; xanthine:xanthine oxidase
Systematic name: xanthine:oxygen oxidoreductase
Comments: An iron-molybdenum flavoprotein (FAD) containing [2Fe-2S] centres. Also oxidizes hypoxanthine, some other purines and pterins, and aldehydes, but is distinct from EC 1.2.3.1, aldehyde oxidase. Under some conditions the product is mainly superoxide rather than peroxide: RH + H2O + 2 O2 = ROH + 2 O2.- + 2 H+. The mammalian enzyme predominantly exists as an NAD-dependent dehydrogenase (EC 1.17.1.4, xanthine dehydrogenase). During purification the enzyme is largely converted to the O2-dependent xanthine oxidase form (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [4,5,7,10] [which can be catalysed by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide] or limited proteolysis, which results in irreversible conversion. The conversion can also occur in vivo [4,6,10].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 9002-17-9
References:
1.  Avis, P.G., Bergel, F. and Bray, R.C. Cellular constituents. The chemistry of xanthine oxidase. Part I. The preparation of a crystalline xanthine oxidase from cow's milk. J. Chem. Soc. (Lond.) (1955) 1100–1105.
2.  Battelli, M.G. and Lorenzoni, E. Purification and properties of a new glutathione-dependent thiol:disulphide oxidoreductase from rat liver. Biochem. J. 207 (1982) 133–138. [PMID: 6960894]
3.  Bray, R.C. Xanthine oxidase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 533–556.
4.  Della Corte, E. and Stirpe, F. The regulation of rat liver xanthine oxidase. Involvement of thiol groups in the conversion of the enzyme activity from dehydrogenase (type D) into oxidase (type O) and purification of the enzyme. Biochem. J. 126 (1972) 739–745. [PMID: 4342395]
5.  Ikegami, T. and Nishino, T. The presence of desulfo xanthine dehydrogenase in purified and crude enzyme preparations from rat liver. Arch. Biochem. Biophys. 247 (1986) 254–260. [DOI] [PMID: 3459393]
6.  Engerson, T.D., McKelvey, T.G., Rhyne, D.B., Boggio, E.B., Snyder, S.J. and Jones, H.P. Conversion of xanthine dehydrogenase to oxidase in ischemic rat tissues. J. Clin. Invest. 79 (1987) 1564–1570. [DOI] [PMID: 3294898]
7.  Saito, T., Nishino, T. and Tsushima, K. Interconversion between NAD-dependent and O2-dependent types of rat liver xanthine dehydrogenase and difference in kinetic and redox properties between them. Adv. Exp. Med. Biol. 253B (1989) 179–183. [PMID: 2610112]
8.  Carpani, G., Racchi, M., Ghezzi, P., Terao, M. and Garattini, E. Purification and characterization of mouse liver xanthine oxidase. Arch. Biochem. Biophys. 279 (1990) 237–241. [DOI] [PMID: 2350174]
9.  Eger, B.T., Okamoto, K., Enroth, C., Sato, M., Nishino, T., Pai, E.F. and Nishino, T. Purification, crystallization and preliminary X-ray diffraction studies of xanthine dehydrogenase and xanthine oxidase isolated from bovine milk. Acta Crystallogr. D Biol. Crystallogr. 56 (2000) 1656–1658. [PMID: 11092937]
10.  Nishino, T., Okamoto, K., Eger, B.T., Pai, E.F. and Nishino, T. Mammalian xanthine oxidoreductase - mechanism of transition from xanthine dehydrogenase to xanthine oxidase. FEBS J. 275 (2008) 3278–3289. [DOI] [PMID: 18513323]
[EC 1.17.3.2 created 1961 as EC 1.2.3.2, transferred 1984 to EC 1.1.3.22, modified 1989, transferred 2004 to EC 1.17.3.2, modified 2011]
 
 
EC 1.20.4.1     
Accepted name: arsenate reductase (glutathione/glutaredoxin)
Reaction: arsenate + glutathione + glutaredoxin = arsenite + a glutaredoxin-glutathione disulfide + H2O
For diagram of arsenate catabolism, click here
Other name(s): ArsC (ambiguous); arsenate:glutaredoxin oxidoreductase; arsenate reductase (glutaredoxin)
Systematic name: arsenate:glutathione/glutaredoxin oxidoreductase
Comments: The enzyme is part of a system for detoxifying arsenate. The substrate binds to a catalytic cysteine residue, forming a covalent thiolate—As(V) intermediate. A tertiary intermediate is then formed between the arsenic, the enzyme’s cysteine, and a glutathione cysteine. This intermediate is reduced by glutaredoxin, which forms a dithiol with the glutathione, leading to the dissociation of arsenite. Thus reduction of As(V) is mediated by three cysteine residues: one in ArsC, one in glutathione, and one in glutaredoxin. Although the arsenite formed is more toxic than arsenate, it can be extruded from some bacteria by EC 7.3.2.7, arsenite-transporting ATPase; in other organisms, arsenite can be methylated by EC 2.1.1.137, arsenite methyltransferase, in a pathway that produces non-toxic organoarsenical compounds. cf. EC 1.20.4.4, arsenate reductase (thioredoxin).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 146907-46-2
References:
1.  Gladysheva, T., Liu, J.Y. and Rosen, B.P. His-8 lowers the pKa of the essential Cys-12 residue of the ArsC arsenate reductase of plasmid R773. J. Biol. Chem. 271 (1996) 33256–33260. [DOI] [PMID: 8969183]
2.  Gladysheva, T.B., Oden, K.L. and Rosen, B.P. Properties of the arsenate reductase of plasmid R773. Biochemistry 33 (1994) 7288–7293. [PMID: 8003492]
3.  Holmgren, A. and Aslund, F. Glutaredoxin. Methods Enzymol. 252 (1995) 283–292. [DOI] [PMID: 7476363]
4.  Krafft, T. and Macy, J.M. Purification and characterization of the respiratory arsenate reductase of Chrysiogenes arsenatis. Eur. J. Biochem. 255 (1998) 647–653. [DOI] [PMID: 9738904]
5.  Martin, J.L. Thioredoxin - a fold for all reasons. Structure 3 (1995) 245–250. [DOI] [PMID: 7788290]
6.  Radabaugh, T.R. and Aposhian, H.V. Enzymatic reduction of arsenic compounds in mammalian systems: reduction of arsenate to arsenite by human liver arsenate reductase. Chem. Res. Toxicol. 13 (2000) 26–30. [DOI] [PMID: 10649963]
7.  Sato, T. and Kobayashi, Y. The ars operon in the skin element of Bacillus subtilis confers resistance to arsenate and arsenite. J. Bacteriol. 180 (1998) 1655–1661. [PMID: 9537360]
8.  Shi, J., Vlamis-Gardikas, V., Aslund, F., Holmgren, A. and Rosen, B.P. Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction. J. Biol. Chem. 274 (1999) 36039–36042. [DOI] [PMID: 10593884]
9.  Mukhopadhyay, R. and Rosen, B.P. Arsenate reductases in prokaryotes and eukaryotes. Environ Health Perspect 110 Suppl 5 (2002) 745–748. [PMID: 12426124]
10.  Messens, J. and Silver, S. Arsenate reduction: thiol cascade chemistry with convergent evolution. J. Mol. Biol. 362 (2006) 1–17. [PMID: 16905151]
[EC 1.20.4.1 created 2000 as EC 1.97.1.5, transferred 2001 to EC 1.20.4.1, modified 2015, modified 2019, modified 2020]
 
 
EC 1.20.4.2     
Accepted name: methylarsonate reductase
Reaction: methylarsonate + 2 glutathione = methylarsonite + glutathione disulfide + H2O
For diagram of arsenate catabolism, click here
Glossary: methylarsonite = methylarsonous acid
cacodylic acid = dimethylarsinic acid
Other name(s): MMA(V) reductase
Systematic name: methylarsonate:glutathione oxidoreductase
Comments: The product, methylarsonite, is biologically methylated by EC 2.1.1.137, arsenite methyltransferase, to form cacodylic acid.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 254889-62-8
References:
1.  Zakharyan, R.A. and Aposhian, H.V. Enzymatic reduction of arsenic compounds in mammalian systems: the rate-limiting enzyme of rabbit liver arsenic biotransformation is MMA(V) reductase. Chem. Res. Toxicol. 12 (1999) 1278–1283. [DOI] [PMID: 10604879]
[EC 1.20.4.2 created 2000 as EC 1.97.1.7, transferred 2001 to EC 1.20.4.2, modified 2003]
 
 
EC 1.21.4.5     
Accepted name: tetrachlorohydroquinone reductive dehalogenase
Reaction: (1) 2,6-dichlorohydroquinone + Cl- + glutathione disulfide = 2,3,6-trichlorohydroquinone + 2 glutathione
(2) 2,3,6-trichlorohydroquinone + Cl- + glutathione disulfide = 2,3,5,6-tetrachlorohydroquinone + 2 glutathione
Other name(s): pcpC (gene name)
Systematic name: glutathione disulfide:2,6-dichlorohydroquinone (chlorinating)
Comments: The enzyme, characterized from the bacterium Sphingobium chlorophenolicum, converts tetrachlorohydroquinone to 2,6-dichlorohydroquinone in two steps, via 2,3,6-trichlorohydroquinone, using glutathione as the reducing agent. The enzyme is sensitive to oxidation - when an internal L-cysteine residue is oxidized, the enzyme produces 2,3,5-trichloro-6-(glutathion-S-yl)-hydroquinone and 2,6-dichloro-3-(glutathion-S-yl)-hydroquinone instead of its normal products.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Xun, L., Topp, E. and Orser, C.S. Purification and characterization of a tetrachloro-p-hydroquinone reductive dehalogenase from a Flavobacterium sp. J. Bacteriol. 174 (1992) 8003–8007. [PMID: 1459949]
2.  McCarthy, D.L., Navarrete, S., Willett, W.S., Babbitt, P.C. and Copley, S.D. Exploration of the relationship between tetrachlorohydroquinone dehalogenase and the glutathione S-transferase superfamily. Biochemistry 35 (1996) 14634–14642. [PMID: 8931562]
[EC 1.21.4.5 created 2018]
 
 


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