The Enzyme Database

Displaying entries 51-72 of 72.

<< Previous | Next >>    printer_iconPrintable version

EC 4.1.3.30     
Accepted name: methylisocitrate lyase
Reaction: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = succinate + pyruvate
Glossary: (2S,3R)-2-methylisocitrate = (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = threo-Ds-2-methylisocitrate
Other name(s): 2-methylisocitrate lyase; MICL; (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate pyruvate-lyase
Systematic name: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate pyruvate-lyase (succinate-forming)
Comments: The enzyme acts on threo-Ds-2-methylisocitrate, but not on threo-Ds-isocitrate, threo-DL-isocitrate or erythro-Ls-isocitrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 57827-77-7
References:
1.  Tabuchi, T. and Satoh, T. Distinction between isocitrate lyase and methylisocitrate lyase in Candida lipolytica. Agric. Biol. Chem. 40 (1976) 1863–1869.
2.  Tabuchi, T. and Satoh, T. Purification and properties of methylisocitrate lyase, a key enzyme in propionate metabolism, from Candida lipolytica. Agric. Biol. Chem. 41 (1977) 169–174.
[EC 4.1.3.30 created 1978]
 
 
EC 4.1.3.31      
Transferred entry: 2-methylcitrate synthase. Now EC 2.3.3.5, 2-methylcitrate synthase
[EC 4.1.3.31 created 1978, deleted 2002]
 
 
EC 4.1.3.34     
Accepted name: citryl-CoA lyase
Reaction: (3S)-citryl-CoA = acetyl-CoA + oxaloacetate
Other name(s): (3S)-citryl-CoA oxaloacetate-lyase
Systematic name: (3S)-citryl-CoA oxaloacetate-lyase (acetyl-CoA-forming)
Comments: The enzyme is a component of EC 4.1.3.6 {[citrate (pro-3S)-lyase]}and EC 2.3.3.8 [ATP citrate synthase]. Also acts on (3S)-citryl thioacyl-carrier protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 131095-35-7
References:
1.  Dimroth, P., Loyal, R. and Eggerer, H. Characterization of the isolated transferase subunit of citrate lyase as a CoA-transferase. Evidence against a covalent enzyme-substrate intermediate. Eur. J. Biochem. 80 (1977) 479–488. [DOI] [PMID: 336371]
2.  Lill, U., Schreil, A. and Eggerer, H. Isolation of enzymically active fragments formed by limited proteolysis of ATP citrate lyase. Eur. J. Biochem. 125 (1982) 645–650. [DOI] [PMID: 6749502]
[EC 4.1.3.34 created 1984, modified 1986]
 
 
EC 4.2.1.3     
Accepted name: aconitate hydratase
Reaction: citrate = isocitrate (overall reaction)
(1a) citrate = cis-aconitate + H2O
(1b) cis-aconitate + H2O = isocitrate
For diagram of the citric acid cycle, click here and for diagram of the glyoxylate cycle, click here
Glossary: isocitrate = (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate (previously known as threo-Ds-isocitrate)
cis-aconitate = (Z)-prop-1-ene-1,2,3-tricarboxylate
Other name(s): cis-aconitase; aconitase; AcnB; 2-methylaconitate hydratase; citrate(isocitrate) hydro-lyase
Systematic name: citrate(isocitrate) hydro-lyase (cis-aconitate-forming)
Comments: Besides interconverting citrate and cis-aconitate, it also interconverts cis-aconitate with isocitrate and, hence, interconverts citrate and isocitrate. The equilibrium mixture is 91% citrate, 6% isocitrate and 3% aconitate. cis-Aconitate is used to designate the isomer (Z)-prop-1-ene-1,2,3-tricarboxylate. An iron-sulfur protein, containing a [4Fe-4S] cluster to which the substrate binds.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9024-25-3
References:
1.  Dickman, S.R. Aconitase. In: Boyer, P.D., Lardy, H. and Myrbäck, K (Ed.), The Enzymes, 2nd edn, vol. 5, Academic Press, New York, 1961, pp. 495–510.
2.  Morrison, J.F. The purification of aconitase. Biochem. J. 56 (1954) 99–105. [PMID: 13126098]
3.  Lauble, H., Kennedy, M.C., Beinert, H. and Stout, C.D. Crystal structures of aconitase with trans-aconitate and nitrocitrate bound. J. Mol. Biol. 237 (1994) 437–451. [DOI] [PMID: 8151704]
[EC 4.2.1.3 created 1961, modified 2003]
 
 
EC 4.2.1.4      
Deleted entry: citrate dehydratase. Now known to be a partial reaction catalysed by EC 4.2.1.3, aconitate hydratase.
[EC 4.2.1.4 created 1961, deleted 2013]
 
 
EC 4.2.1.36     
Accepted name: homoaconitate hydratase
Reaction: (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate = (Z)-but-1-ene-1,2,4-tricarboxylate + H2O
For diagram of l-lysine synthesis, click here
Glossary: cis-homoaconitate = (Z)-but-1-ene-1,2,4-tricarboxylate
(R)-homocitrate = (2R)-2-hydroxybutane-1,2,4-tricarboxylate
homoisocitrate = (-)-threo-homoisocitrate = (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
Other name(s): homoaconitase; cis-homoaconitase; HACN; Lys4; LysF; 2-hydroxybutane-1,2,4-tricarboxylate hydro-lyase (incorrect)
Systematic name: (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate hydro-lyase [(Z)-but-1-ene-1,2,4-tricarboxylate-forming]
Comments: Requires a [4Fe-4S] cluster for activity. The enzyme from the hyperthermophilic eubacterium Thermus thermophilus can catalyse the reaction shown above but cannot catalyse the previously described reaction, i.e. formation of (R)-homocitrate by hydration of cis-homoaconitate. The enzyme responsible for the conversion of cis-homoaconitate into (R)-homocitrate in T. thermophilus is unknown at present but the reaction can be catalysed in vitro using aconitate hydratase from pig (EC 4.2.1.3) [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9030-68-6
References:
1.  Strassman, M. and Ceci, L.N. Enzymatic formation of cis-homoaconitic acid, an intermediate in lysine biosynthesis in yeast. J. Biol. Chem. 241 (1966) 5401–5407. [PMID: 5954805]
2.  Jia, Y., Tomita, T., Yamauchi, K., Nishiyama, M. and Palmer, D.R. Kinetics and product analysis of the reaction catalysed by recombinant homoaconitase from Thermus thermophilus. Biochem. J. 396 (2006) 479–485. [DOI] [PMID: 16524361]
3.  Zabriskie, T.M. and Jackson, M.D. Lysine biosynthesis and metabolism in fungi. Nat. Prod. Rep. 17 (2000) 85–97. [PMID: 10714900]
[EC 4.2.1.36 created 1972, modified 2007]
 
 
EC 4.2.1.79     
Accepted name: 2-methylcitrate dehydratase
Reaction: (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate = (Z)-but-2-ene-1,2,3-tricarboxylate + H2O
Glossary: (2S,3S)-2-methylcitrate = (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate
cis-2-methylaconitate = (Z)-but-2-ene-1,2,3-tricarboxylate
Other name(s): 2-methylcitrate hydro-lyase; PrpD; 2-hydroxybutane-1,2,3-tricarboxylate hydro-lyase
Systematic name: (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate hydro-lyase [(Z)-but-2-ene-1,2,3-tricarboxylate-forming]
Comments: The enzyme is specific for (2S,3S)-methylcitrate, showing no activity with (2R,3S)-methylcitrate [2]. The enzyme can also use cis-aconitate as a substrate but more slowly [2]. Both this enzyme and EC 4.2.1.3, aconitate hydratase, are required to complete the isomerization of (2S,3S)-methylcitrate to (2R,3S)-2-methylisocitrate [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 80891-26-5
References:
1.  Aoki, H. and Tabuchi, T. Purification and properties of 2-methylcitrate dehydratase from Yarrowia lipolytica. Agric. Biol. Chem. 45 (1981) 2831–2837.
2.  Brock, M., Maerker, C., Schütz, A., Völker, U. and Buckel, W. Oxidation of propionate to pyruvate in Escherichia coli. Involvement of methylcitrate dehydratase and aconitase. Eur. J. Biochem. 269 (2002) 6184–6194. [DOI] [PMID: 12473114]
[EC 4.2.1.79 created 1984]
 
 
EC 4.2.1.99     
Accepted name: 2-methylisocitrate dehydratase
Reaction: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = (Z)-but-2-ene-1,2,3-tricarboxylate + H2O
Glossary: cis-2-methylaconitate = (Z)-but-2-ene-1,2,3-tricarboxylate
(2S,3R)-2-methylisocitrate = (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = threo-Ds-2-methylisocitrate
Other name(s): (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate hydro-lyase
Systematic name: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate hydro-lyase [(Z)-but-2-ene-1,2,3-tricarboxylate-forming]
Comments: The enzyme from the fungus Yarrowia lipolytica (Saccharomycopsis) does not act on isocitrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 170780-51-5
References:
1.  Aoki, H., Uchiyama, H., Umetsu, H., Tabuchi, T. Isolation of 2-methylisocitrate dehydratase, a new enzyme serving in the methylcitric acid cycle for propionate metabolism, from Yarrowia lipolytica. Biosci. Biotechnol. Biochem. 59 (1995) 1825–1828.
2.  Tabuchi, T., Umetsu, H., Aoki, H., Uchiyama, H. Characteristics of 2-methylisocitrate dehydratase, isolated from Yarrowia lipolytica, in comparison to aconitase. Biosci. Biotechnol. Biochem. 59 (1995) 2013–2017.
[EC 4.2.1.99 created 1999]
 
 
EC 4.2.1.114     
Accepted name: methanogen homoaconitase
Reaction: (R)-2-hydroxybutane-1,2,4-tricarboxylate = (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate (overall reaction)
(1a) (R)-2-hydroxybutane-1,2,4-tricarboxylate = (Z)-but-1-ene-1,2,4-tricarboxylate + H2O
(1b) (Z)-but-1-ene-1,2,4-tricarboxylate + H2O = (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
For diagram of the 2-aminoadipate pathway of L-lysine synthesis, click here
Glossary: cis-homoaconitate = (Z)-but-1-ene-1,2,4-tricarboxylate
(R)-homocitrate = (R)-2-hydroxybutane-1,2,4-tricarboxylate
homoisocitrate = (–)-threo-homoisocitrate = (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
Other name(s): methanogen HACN
Systematic name: (R)-2-hydroxybutane-1,2,4-tricarboxylate hydro-lyase [(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate-forming]
Comments: This enzyme catalyses several reactions in the pathway of coenzyme-B biosynthesis in methanogenic archaea. Requires a [4Fe-4S] cluster for activity. In contrast to EC 4.2.1.36, homoaconitate hydratase, this enzyme can catalyse both the dehydration of (R)-homocitrate to form cis-homoaconitate and the subsequent hydration reaction that forms homoisocitrate. In addition to cis-homoaconitate, the enzyme can also catalyse the hydration of the physiological substrates dihomoaconitate and trihomoaconitate as well as the non-physiological substrate tetrahomoaconitate. cis-Aconitate and threo-DL-isocitrate cannot act as substrates, and (S)-homocitrate and trans-homoaconitate act as inhibitors of the enzyme.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Drevland, R.M., Jia, Y., Palmer, D.R. and Graham, D.E. Methanogen homoaconitase catalyzes both hydrolyase reactions in coenzyme B biosynthesis. J. Biol. Chem. 283 (2008) 28888–28896. [DOI] [PMID: 18765671]
[EC 4.2.1.114 created 2009]
 
 
EC 4.2.1.117     
Accepted name: 2-methylcitrate dehydratase (2-methyl-trans-aconitate forming)
Reaction: (2S,3S)-2-methylcitrate = 2-methyl-trans-aconitate + H2O
Glossary: (2S,3S)-2-methylcitrate = (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate
2-methyl-trans-aconitate = (2E)-but-2-ene-1,2,3-tricarboxylate
Systematic name: (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate hydro-lyase (2-methyl-trans-aconitate-forming)
Comments: Catalyses the dehydration of (2S,3S)-2-methylcitrate, forming the trans isomer of 2-methyl-aconitate (unlike EC 4.2.1.79, which forms only the cis isomer). Part of a propionate degradation pathway. The enzyme from Shewanella oneidensis can also accept citrate and cis-aconitate, but activity with (2S,3S)-2-methylcitrate was approximately 2.5-fold higher. 2-methylisocitrate and isocitrate were not substrates [1]. An iron-sulfur protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Grimek, T.L. and Escalante-Semerena, J.C. The acnD genes of Shewenella oneidensis and Vibrio cholerae encode a new Fe/S-dependent 2-methylcitrate dehydratase enzyme that requires prpF function in vivo. J. Bacteriol. 186 (2004) 454–462. [DOI] [PMID: 14702315]
[EC 4.2.1.117 created 2009]
 
 
EC 5.1.2.6     
Accepted name: isocitrate epimerase
Reaction: (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate = (1S,2S)-1-hydroxypropane-1,2,3-tricarboxylate
For diagram of reaction, click here
Glossary: isocitrate = (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate = threo-Ds-isocitrate
allocitrate = (1S,2S)-1-hydroxypropane-1,2,3-tricarboxylate = D-erythro-isocitrate
Systematic name: (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate 1-epimerase
Comments: (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate is the commonly occurring isomer of isocitrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81210-68-6
References:
1.  Hoshiko, S., Kunimoto, Y., Arima, K. and Beppu, T. Mechanism of L-alloisocitric acid fermentation: isocitrate epimerase activity in the cell-free-extract of Penicillium purpurogenum. Agric. Biol. Chem. 46 (1982) 143–151.
[EC 5.1.2.6 created 1984]
 
 
EC 6.2.1.18     
Accepted name: citrate—CoA ligase
Reaction: ATP + citrate + CoA = ADP + phosphate + (3S)-citryl-CoA
Glossary: citrate = 2-hydroxypropane-1,2,3-tricarboxylate
Other name(s): citryl-CoA synthetase; citrate:CoA ligase; citrate thiokinase
Systematic name: citrate:CoA ligase (ADP-forming)
Comments: The enzyme is a component of EC 2.3.3.8 ATP citrate synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 856428-87-0
References:
1.  Lill, U., Schreil, A. and Eggerer, H. Isolation of enzymically active fragments formed by limited proteolysis of ATP citrate lyase. Eur. J. Biochem. 125 (1982) 645–650. [DOI] [PMID: 6749502]
2.  Aoshima, M., Ishii, M. and Igarashi, Y. A novel enzyme, citryl-CoA synthetase, catalysing the first step of the citrate cleavage reaction in Hydrogenobacter thermophilus TK-6. Mol. Microbiol. 52 (2004) 751–761. [DOI] [PMID: 15101981]
[EC 6.2.1.18 created 1986]
 
 
EC 6.2.1.22     
Accepted name: [citrate (pro-3S)-lyase] ligase
Reaction: ATP + acetate + holo-[citrate (pro-3S)-lyase] = AMP + diphosphate + acetyl-[citrate (pro-3S)-lyase]
Glossary: citrate = 2-hydroxypropane-1,2,3-tricarboxylate
Other name(s): citrate lyase ligase; citrate lyase synthetase; acetate: SH-[acyl-carrier-protein] enzyme ligase (AMP); acetate:HS-citrate lyase ligase; acetate:citrate-(pro-3S)-lyase(thiol-form) ligase (AMP-forming); acetate:[citrate-(pro-3S)-lyase](thiol-form) ligase (AMP-forming)
Systematic name: acetate:holo-[citrate-(pro-3S)-lyase] ligase (AMP-forming)
Comments: Both this enzyme and EC 2.3.1.49,deacetyl-[citrate-(pro-3S)-lyase] S-acetyltransferase, acetylate and activate EC 4.1.3.6, citrate (pro-3S)-lyase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 52660-22-7
References:
1.  Antranikian, G. and Gottschalk, G. Copurification of citrate lyase and citrate lyase ligase from Rhodopseudomonas gelatinosa and subsequent separation of the two enzymes. Eur. J. Biochem. 126 (1982) 43–47. [DOI] [PMID: 7128585]
2.  Antranikian, G., Herzberg, C. and Gottschalk, G. Covalent modification of citrate lyase ligase from Clostridium sphenoides by phosphorylation/dephosphorylation. Eur. J. Biochem. 153 (1985) 413–420. [DOI] [PMID: 3935436]
3.  Quentmeier, A. and Antranikian, G. Characterization of citrate lyase from Clostridium sporosphaeroides. Arch. Microbiol. 141 (1985) 85–90. [PMID: 3994485]
4.  Schmellenkamp, H. and Eggerer, H. Mechanism of enzymic acetylation of des-acetyl citrate lyase. Proc. Natl. Acad. Sci. USA 71 (1974) 1987–1991. [DOI] [PMID: 4365579]
[EC 6.2.1.22 created 1989]
 
 
EC 6.3.1.17     
Accepted name: β-citrylglutamate synthase
Reaction: ATP + citrate + L-glutamate = ADP + phosphate + β-citryl-L-glutamate
Other name(s): NAAG synthetase I; NAAGS-I; RIMKLB (gene name) (ambiguous)
Systematic name: citrate:L-glutamate ligase (ADP-forming)
Comments: The enzyme, found in animals, also has the activity of EC 6.3.2.41, N-acetylaspartylglutamate synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Collard, F., Stroobant, V., Lamosa, P., Kapanda, C.N., Lambert, D.M., Muccioli, G.G., Poupaert, J.H., Opperdoes, F. and Van Schaftingen, E. Molecular identification of N-acetylaspartylglutamate synthase and β-citrylglutamate synthase. J. Biol. Chem. 285 (2010) 29826–29833. [DOI] [PMID: 20657015]
[EC 6.3.1.17 created 2014]
 
 
EC 6.3.2.27      
Deleted entry: The activity is covered by two independent enzymes, EC 6.3.2.38 N2-citryl-N6-acetyl-N6-hydroxylysine synthase, and EC 6.3.2.39, aerobactin synthase
[EC 6.3.2.27 created 2002, modified 2006, deleted 2012]
 
 
EC 6.3.2.38     
Accepted name: N2-citryl-N6-acetyl-N6-hydroxylysine synthase
Reaction: 2 ATP + citrate + N6-acetyl-N6-hydroxy-L-lysine + H2O = 2 ADP + 2 phosphate + N6-acetyl-N2-citryl-N6-hydroxy-L-lysine
For diagram of aerobactin biosynthesis, click here
Glossary: citryl = 3-hydroxy-3,4-dicarboxybutanoyl
Other name(s): Nα-citryl-Nε-acetyl-Nε-hydroxylysine synthase; iucA (gene name)
Systematic name: citrate:N6-acetyl-N6-hydroxy-L-lysine ligase (AMP-forming)
Comments: Requires Mg2+. The enzyme is involved in the biosynthesis of aerobactin, a dihydroxamate siderophore. It belongs to a class of siderophore synthases known as type A nonribosomal peptide synthase-independent synthases (NIS). Type A enzymes are responsible for the formation of amide or ester bonds between polyamines or amino alcohols and a prochiral carboxyl group of citrate. The enzyme is believed to form an adenylate intermediate prior to ligation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Gibson, F. and Magrath, D.I. The isolation and characterization of a hydroxamic acid (aerobactin) formed by Aerobacter aerogenes 62-I. Biochim. Biophys. Acta 192 (1969) 175–184. [DOI] [PMID: 4313071]
2.  Maurer, P.J. and Miller, M. Microbial iron chelators: total synthesis of aerobactin and its constituent amino acid, N6-acetyl-N6-hydroxylysine. J. Am. Chem. Soc. 104 (1982) 3096–3101.
3.  de Lorenzo, V., Bindereif, A., Paw, B.H. and Neilands, J.B. Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in Escherichia coli K-12. J. Bacteriol. 165 (1986) 570–578. [DOI] [PMID: 2935523]
4.  Appanna, D.L., Grundy, B.J., Szczepan, E.W. and Viswanatha, T. Aerobactin synthesis in a cell-free system of Aerobacter aerogenes 62-1. Biochim. Biophys. Acta 801 (1984) 437–443.
5.  Challis, G.L. A widely distributed bacterial pathway for siderophore biosynthesis independent of nonribosomal peptide synthetases. ChemBioChem 6 (2005) 601–611. [DOI] [PMID: 15719346]
6.  Oves-Costales, D., Kadi, N. and Challis, G.L. The long-overlooked enzymology of a nonribosomal peptide synthetase-independent pathway for virulence-conferring siderophore biosynthesis. Chem. Commun. (Camb.) (2009) 6530–6541. [PMID: 19865642]
[EC 6.3.2.38 created 2012, modified 2019]
 
 
EC 6.3.2.39     
Accepted name: aerobactin synthase
Reaction: ATP + N2-citryl-N6-acetyl-N6-hydroxy-L-lysine + N6-acetyl-N6-hydroxy-L-lysine = AMP + diphosphate + aerobactin
For diagram of aerobactin biosynthesis, click here
Other name(s): iucC (gene name)
Systematic name: N2-citryl-N6-acetyl-N6-hydroxy-L-lysine:N6-acetyl-N6-hydroxy-L-lysine ligase (AMP-forming)
Comments: Requires Mg2+. The enzyme is involved in the biosynthesis of aerobactin, a dihydroxamate siderophore. It belongs to a class of siderophore synthases known as type C nonribosomal peptide synthase-independent synthases (NIS). Type C enzymes are responsible for the formation of amide or ester bonds between a variety of substrates and a prochiral carboxyl group of a citrate molecule that is already linked to a different moiety at its other prochiral carboxyl group. The enzyme is believed to form an adenylate intermediate prior to ligation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Gibson, F. and Magrath, D.I. The isolation and characterization of a hydroxamic acid (aerobactin) formed by Aerobacter aerogenes 62-I. Biochim. Biophys. Acta 192 (1969) 175–184. [DOI] [PMID: 4313071]
2.  Maurer, P.J. and Miller, M. Microbial iron chelators: total synthesis of aerobactin and its constituent amino acid, N6-acetyl-N6-hydroxylysine. J. Am. Chem. Soc. 104 (1982) 3096–3101.
3.  Appanna, D.L., Grundy, B.J., Szczepan, E.W. and Viswanatha, T. Aerobactin synthesis in a cell-free system of Aerobacter aerogenes 62-1. Biochim. Biophys. Acta 801 (1984) 437–443.
4.  de Lorenzo, V., Bindereif, A., Paw, B.H. and Neilands, J.B. Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in Escherichia coli K-12. J. Bacteriol. 165 (1986) 570–578. [DOI] [PMID: 2935523]
5.  de Lorenzo, V. and Neilands, J.B. Characterization of iucA and iucC genes of the aerobactin system of plasmid ColV-K30 in Escherichia coli. J. Bacteriol. 167 (1986) 350–355. [DOI] [PMID: 3087960]
6.  Challis, G.L. A widely distributed bacterial pathway for siderophore biosynthesis independent of nonribosomal peptide synthetases. ChemBioChem 6 (2005) 601–611. [DOI] [PMID: 15719346]
7.  Oves-Costales, D., Kadi, N. and Challis, G.L. The long-overlooked enzymology of a nonribosomal peptide synthetase-independent pathway for virulence-conferring siderophore biosynthesis. Chem. Commun. (Camb.) (2009) 6530–6541. [PMID: 19865642]
[EC 6.3.2.39 created 2012, modified 2019]
 
 
EC 6.3.2.54     
Accepted name: L-2,3-diaminopropanoate—citrate ligase
Reaction: ATP + L-2,3-diaminopropanoate + citrate = AMP + diphosphate + 2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate
Glossary: staphyloferrin B = 5-[(2-{[(3S)-5-{[(2S)-2-amino-2-carboxyethyl]amino}-3-carboxy-3-hydroxy-5-oxopentanoyl]amino}ethyl)amino]-2,5-dioxopentanoate
Other name(s): sbnE (gene name); 2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate synthtase
Systematic name: L-2,3-diaminopropanoate:citrate ligase (2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate-forming)
Comments: Requires Mg2+. The enzyme, characterized from the bacterium Staphylococcus aureus, is involved in the biosynthesis of the siderophore staphyloferrin B. It belongs to a class of siderophore synthases known as type A nonribosomal peptide synthase-independent synthases (NIS). Type A NIS enzymes are responsible for the formation of amide or ester bonds between polyamines or amino alcohols and a prochiral carboxyl group of citrate. The enzyme forms a citrate adenylate intermediate prior to ligation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Dale, S.E., Doherty-Kirby, A., Lajoie, G. and Heinrichs, D.E. Role of siderophore biosynthesis in virulence of Staphylococcus aureus: identification and characterization of genes involved in production of a siderophore. Infect. Immun. 72 (2004) 29–37. [PMID: 14688077]
2.  Cheung, J., Beasley, F.C., Liu, S., Lajoie, G.A. and Heinrichs, D.E. Molecular characterization of staphyloferrin B biosynthesis in Staphylococcus aureus. Mol. Microbiol. 74 (2009) 594–608. [PMID: 19775248]
[EC 6.3.2.54 created 2019]
 
 
EC 6.3.2.57     
Accepted name: staphyloferrin A synthase
Reaction: ATP + N5-[(S)-citryl]-D-ornithine + citrate = AMP + diphosphate + staphyloferrin A
For diagram of staphyloferrin A biosynthesis, click here
Glossary: staphyloferrin A = N2-[(R)-citryl],N5-[(S)-citryl]-D-ornithine
citryl = 3-hydroxy-3,4-dicarboxybutanoyl
Other name(s): sfnaB (gene name)
Systematic name: N5-[(S)-citryl]-D-ornithine:citrate ligase (staphyloferrin A-forming)
Comments: Requires Mg2+. The enzyme, characterized from the bacterium Staphylococcus aureus, catalyses the last step in the biosynthesis of the siderophore staphyloferrin A. It belongs to a class of siderophore synthases known as type A nonribosomal peptide synthase-independent synthases (NIS). Type A NIS enzymes are responsible for the formation of amide or ester bonds between polyamines or amino alcohols and a prochiral carboxyl group of citrate. The enzyme forms a citrate adenylate intermediate prior to ligation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Cotton, J.L., Tao, J. and Balibar, C.J. Identification and characterization of the Staphylococcus aureus gene cluster coding for staphyloferrin A. Biochemistry 48 (2009) 1025–1035. [PMID: 19138128]
[EC 6.3.2.57 created 2019]
 
 
EC 6.3.2.58     
Accepted name: D-ornithine—citrate ligase
Reaction: ATP + D-ornithine + citrate = AMP + diphosphate + N5-[(S)-citryl]-D-ornithine
For diagram of staphyloferrin A biosynthesis, click here
Glossary: staphyloferrin A = N2-[(R)-citryl],N5-[(S)-citryl]-D-ornithine
Other name(s): sfnaD (gene name)
Systematic name: D-ornithine:citrate ligase {3-[(2-aminopentan-5-oylcarbamoyl)methyl]-3-hydroxybutanoate-forming}
Comments: Requires Mg2+. The enzyme, characterized from the bacterium Staphylococcus aureus, is involved in the biosynthesis of the siderophore staphyloferrin A. It belongs to a class of siderophore synthases known as type A nonribosomal peptide synthase-independent synthases (NIS). Type A NIS enzymes are responsible for the formation of amide or ester bonds between polyamines or amino alcohols and a prochiral carboxyl group of citrate. The enzyme forms a citrate adenylate intermediate prior to ligation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Cotton, J.L., Tao, J. and Balibar, C.J. Identification and characterization of the Staphylococcus aureus gene cluster coding for staphyloferrin A. Biochemistry 48 (2009) 1025–1035. [PMID: 19138128]
[EC 6.3.2.58 created 2019]
 
 
EC 6.4.1.7     
Accepted name: 2-oxoglutarate carboxylase
Reaction: ATP + 2-oxoglutarate + HCO3- = ADP + phosphate + oxalosuccinate
For diagram of reaction, click here
Glossary: oxalosuccinate = 1-oxopropane-1,2,3-tricarboxylate
Other name(s): oxalosuccinate synthetase; carboxylating factor for ICDH (incorrect); CFI; OGC
Comments: A biotin-containing enzyme that requires Mg2+ for activity. It was originally thought [1] that this enzyme was a promoting factor for the carboxylation of 2-oxoglutarate by EC 1.1.1.41, isocitrate dehydrogenase (NAD+), but this has since been disproved [2]. The product of the reaction is unstable and is quickly converted into isocitrate by the action of EC 1.1.1.41 [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 60382-75-4
References:
1.  Aoshima, M., Ishii, M. and Igarashi, Y. A novel biotin protein required for reductive carboxylation of 2-oxoglutarate by isocitrate dehydrogenase in Hydrogenobacter thermophilus TK-6. Mol. Microbiol. 51 (2004) 791–798. [DOI] [PMID: 14731279]
2.  Aoshima, M. and Igarashi, Y. A novel oxalosuccinate-forming enzyme involved in the reductive carboxylation of 2-oxoglutarate in Hydrogenobacter thermophilus TK-6. Mol. Microbiol. 62 (2006) 748–759. [DOI] [PMID: 17076668]
[EC 6.4.1.7 created 2006]
 
 
EC 7.2.2.18     
Accepted name: ABC-type ferric citrate transporter
Reaction: ATP + H2O + Fe3+-dicitrate-[dicitrate-binding protein][side 1] = ADP + phosphate + Fe3+-dicitrate[side 2] + [dicitrate-binding protein][side 1]
Other name(s): ferric citrate transporting ATPase; ferric citrate ABC transporter; fecBCDE (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, iron(III) dicitrate-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme from Escherichia coli interacts with a periplasmic substrate binding protein and mediates the high affinity uptake of Fe3+-citrate in the form of a mononuclear (containing one iron(III) ion and two citrate molecules) or dinuclear (containing 2 iron(III) ions) complexes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Staudenmaier, H., Van Hove, B., Yaraghi, Z. and Braun, V. Nucleotide sequences of the fecBCDE genes and locations of the proteins suggest a periplasmic-binding-protein-dependent transport mechanism for iron(III) dicitrate in Escherichia coli. J. Bacteriol. 171 (1989) 2626–2633. [PMID: 2651410]
2.  Banerjee, S., Paul, S., Nguyen, L.T., Chu, B.C. and Vogel, H.J. FecB, a periplasmic ferric-citrate transporter from E. coli, can bind different forms of ferric-citrate as well as a wide variety of metal-free and metal-loaded tricarboxylic acids. Metallomics 8 (2016) 125–133. [PMID: 26600288]
[EC 7.2.2.18 created 2000 as EC 3.6.3.34, part transferred 2018 to EC 7.2.2.18]
 
 


Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald