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]
 
 


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