The Enzyme Database

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EC 1.1.3.2     
Accepted name: L-lactate oxidase
Reaction: (S)-lactate + O2 = pyruvate + H2O2
Other name(s): lctO (gene name); LOX
Systematic name: (S)-lactate:oxygen 2-oxidoreductase
Comments: Contains flavin mononucleotide (FMN). The best characterized enzyme is that from the bacterium Aerococcus viridans. The enzyme is widely used in biosensors to measure the lactate concentration in blood and other tissues.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Duncan, J.D., Wallis, J.O. and Azari, M.R. Purification and properties of Aerococcus viridans lactate oxidase. Biochem. Biophys. Res. Commun. 164 (1989) 919–926. [DOI] [PMID: 2818595]
2.  Maeda-Yorita, K., Aki, K., Sagai, H., Misaki, H. and Massey, V. L-lactate oxidase and L-lactate monooxygenase: mechanistic variations on a common structural theme. Biochimie 77 (1995) 631–642. [DOI] [PMID: 8589073]
3.  Gibello, A., Collins, M.D., Dominguez, L., Fernandez-Garayzabal, J.F. and Richardson, P.T. Cloning and analysis of the L-lactate utilization genes from Streptococcus iniae. Appl. Environ. Microbiol. 65 (1999) 4346–4350. [PMID: 10508058]
4.  Umena, Y., Yorita, K., Matsuoka, T., Kita, A., Fukui, K. and Morimoto, Y. The crystal structure of L-lactate oxidase from Aerococcus viridans at 2.1 Å resolution reveals the mechanism of strict substrate recognition. Biochem. Biophys. Res. Commun. 350 (2006) 249–256. [DOI] [PMID: 17007814]
5.  Furuichi, M., Suzuki, N., Dhakshnamoorhty, B., Minagawa, H., Yamagishi, R., Watanabe, Y., Goto, Y., Kaneko, H., Yoshida, Y., Yagi, H., Waga, I., Kumar, P.K. and Mizuno, H. X-ray structures of Aerococcus viridans lactate oxidase and its complex with D-lactate at pH 4.5 show an α-hydroxyacid oxidation mechanism. J. Mol. Biol. 378 (2008) 436–446. [DOI] [PMID: 18367206]
6.  Stoisser, T., Brunsteiner, M., Wilson, D.K. and Nidetzky, B. Conformational flexibility related to enzyme activity: evidence for a dynamic active-site gatekeeper function of Tyr215 in Aerococcus viridans lactate oxidase. Sci Rep 6:27892 (2016). [DOI] [PMID: 27302031]
[EC 1.1.3.2 created 1961, transferred 1972 to EC 1.13.12.4, reinstated 2018]
 
 
EC 1.1.3.20     
Accepted name: long-chain-alcohol oxidase
Reaction: a long-chain alcohol + O2 = a long-chain aldehyde + H2O2
Other name(s): long-chain fatty alcohol oxidase; fatty alcohol oxidase; fatty alcohol:oxygen oxidoreductase; long-chain fatty acid oxidase
Systematic name: long-chain-alcohol:oxygen oxidoreductase
Comments: Oxidizes long-chain fatty alcohols; best substrate is dodecyl alcohol.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 129430-50-8
References:
1.  Moreau, R.A. and Huang, A.H.C. Oxidation of fatty alcohol in the cotyledons of jojoba seedlings. Arch. Biochem. Biophys. 194 (1979) 422–430. [DOI] [PMID: 36040]
2.  Moreau, R.A. and Huang, A.H.C. Enzymes of wax ester catabolism in jojoba. Methods Enzymol. 71 (1981) 804–813.
3.  Cheng, Q., Liu, H.T., Bombelli, P., Smith, A. and Slabas, A.R. Functional identification of AtFao3, a membrane bound long chain alcohol oxidase in Arabidopsis thaliana. FEBS Lett. 574 (2004) 62–68. [DOI] [PMID: 15358540]
4.  Zhao, S., Lin, Z., Ma, W., Luo, D. and Cheng, Q. Cloning and characterization of long-chain fatty alcohol oxidase LjFAO1 in Lotus japonicus. Biotechnol. Prog. 24 (2008) 773–779. [DOI] [PMID: 18396913]
5.  Cheng, Q., Sanglard, D., Vanhanen, S., Liu, H.T., Bombelli, P., Smith, A. and Slabas, A.R. Candida yeast long chain fatty alcohol oxidase is a c-type haemoprotein and plays an important role in long chain fatty acid metabolism. Biochim. Biophys. Acta 1735 (2005) 192–203. [DOI] [PMID: 16046182]
[EC 1.1.3.20 created 1984, modified 2010]
 
 
EC 1.1.3.21     
Accepted name: glycerol-3-phosphate oxidase
Reaction: sn-glycerol 3-phosphate + O2 = glycerone phosphate + H2O2
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): glycerol phosphate oxidase; glycerol-1-phosphate oxidase; glycerol phosphate oxidase; L-α-glycerophosphate oxidase; α-glycerophosphate oxidase; L-α-glycerol-3-phosphate oxidase
Systematic name: sn-glycerol-3-phosphate:oxygen 2-oxidoreductase
Comments: A flavoprotein (FAD).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9046-28-0
References:
1.  Gancedo, C., Gancedo, J.M. and Sols, A. Glycerol metabolism in yeasts. Pathways of utilization and production. Eur. J. Biochem. 5 (1968) 165–172. [DOI] [PMID: 5667352]
2.  Koditschek, L.K. and Umbreit, W.W. α-Glycerophosphate oxidase in Streptococcus faecium F 24. J. Bacteriol. 93 (1969) 1063–1068. [PMID: 5788698]
[EC 1.1.3.21 created 1984]
 
 
EC 1.1.3.22      
Transferred entry: xanthine oxidase. Now EC 1.17.3.2, xanthine oxidase. The enzyme was incorrectly classified as acting on a CH-OH group
[EC 1.1.3.22 created 1961 as EC 1.2.3.2, transferred 1984 to EC 1.1.3.22, modified 1989, deleted 2004]
 
 
EC 1.1.3.23     
Accepted name: thiamine oxidase
Reaction: thiamine + 2 O2 + H2O = thiamine acetic acid + 2 H2O2
Other name(s): thiamin dehydrogenase; thiamine dehydrogenase; thiamin:oxygen 5-oxidoreductase
Systematic name: thiamine:oxygen 5-oxidoreductase
Comments: A flavoprotein (FAD). The product differs from thiamine in replacement of -CH2.CH2.OH by -CH2.COOH; the two-step oxidation proceeds without the release of the intermediate aldehyde from the enzyme.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 96779-44-1
References:
1.  Edmondson, D.E., Kenney, W.C. and Singer, T.P. Structural elucidation and properties of 8α-(N1-histidyl)riboflavin: the flavin component of thiamine dehydrogenase and β-cyclopiazonate oxidocyclase. Biochemistry 15 (1976) 2937–2945. [PMID: 8076]
2.  Gomez-Moreno, C. and Edmondson, D.E. Evidence for an aldehyde intermediate in the catalytic mechanism of thiamine oxidase. Arch. Biochem. Biophys. 239 (1985) 46–52. [DOI] [PMID: 2988447]
3.  Neal, R.A. Bacterial metabolism of thiamine. 3. Metabolism of thiamine to 3-(2′-methyl-4′-amino-5′-pyrimidylmethyl)-4-methyl-thiazole-5-acetic acid (thiamine acetic acid) by a flavoprotein isolated from a soil microorganism. J. Biol. Chem. 245 (1970) 2599–2604. [PMID: 4987737]
[EC 1.1.3.23 created 1984]
 
 
EC 1.1.3.24      
Transferred entry: L-galactonolactone oxidase. Now EC 1.3.3.12, L-galactonolactone oxidase. The enzyme had been incorrectly classified as acting upon a CH-OH donor rather than a CH-CH donor
[EC 1.1.3.24 created 1984, deleted 2006]
 
 
EC 1.1.3.25      
Transferred entry: cellobiose oxidase. Now included with EC 1.1.99.18, cellobiose dehydrogenase (acceptor)
[EC 1.1.3.25 created 1986, deleted 2005]
 
 
EC 1.1.3.26      
Transferred entry: columbamine oxidase. Now EC 1.21.3.2, columbamine oxidase
[EC 1.1.3.26 created 1989, deleted 2002]
 
 
EC 1.1.3.27     
Accepted name: hydroxyphytanate oxidase
Reaction: L-2-hydroxyphytanate + O2 = 2-oxophytanate + H2O2
Other name(s): L-2-hydroxyphytanate:oxygen 2-oxidoreductase
Systematic name: L-2-hydroxyphytanate:oxygen 2-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 114454-12-5
References:
1.  Vamecq, J. and Draye, J.P. The enzymatic and mass spectrometric identification of 2-oxophytanic acid, a product of the peroxisomal oxidation of l-2-hydroxyphytanic acid. Biomed. Environ. Mass Spectrom. 15 (1988) 345–351. [DOI] [PMID: 3288289]
[EC 1.1.3.27 created 1990]
 
 
EC 1.1.3.28     
Accepted name: nucleoside oxidase
Reaction: inosine + O2 = 9-riburonosylhypoxanthine + H2O
(1a) 2 inosine + O2 = 2 5′-dehydroinosine + 2 H2O
(1b) 2 5′-dehydroinosine + O2 = 2 9-riburonosylhypoxanthine
Systematic name: nucleoside:oxygen 5′-oxidoreductase
Comments: Other purine and pyrimidine nucleosides (as well as 2′-deoxyribonucleosides) are substrates, but ribose and nucleotides are not substrates. The overall reaction takes place in two separate steps, with the 5′-dehydro nucleoside being released from the enzyme to serve as substrate for the second reaction. This enzyme differs from EC 1.1.3.39, nucleoside oxidase (H2O2-forming), as it produces water rather than hydrogen peroxide.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 82599-71-1
References:
1.  Isono, Y., Sudo, T. and Hoshino, M. Purification and reaction of a new enzyme, nucleoside oxidase. Agric. Biol. Chem. 53 (1989) 1663–1669.
2.  Isono, Y., Sudo, T. and Hoshino, M. Properties of a new enzyme, nucleoside oxidase, from Pseudomonas maltophilia LB-86. Agric. Biol. Chem. 53 (1989) 1671–1677.
[EC 1.1.3.28 created 1992, modified 2001]
 
 
EC 1.1.3.29     
Accepted name: N-acylhexosamine oxidase
Reaction: N-acetyl-D-glucosamine + O2 = N-acetyl-D-glucosaminate + H2O2
Other name(s): N-acyl-D-hexosamine oxidase; N-acyl-β-D-hexosamine:oxygen 1-oxidoreductase
Systematic name: N-acyl-D-hexosamine:oxygen 1-oxidoreductase
Comments: Also acts on N-glycolylglucosamine, N-acetylgalactosamine and, more slowly, on N-acetylmannosamine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 121479-58-1
References:
1.  Horiuchi, T. Purification and properties of N-acyl-D-hexosamine oxidase from Pseudomonas sp 15-1. Agric. Biol. Chem. 53 (1989) 361–368.
[EC 1.1.3.29 created 1992]
 
 


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