L-lactate oxidase
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| L-lactate oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.3.2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
L-lactate oxidase (EC 1.1.3.2) is an enzyme that catalyzes the chemical reaction:[1][2][3]
It belongs to the family of oxidoreductases (enzymes involved in redox reactions), specifically those acting on the CH−OH group of donors with oxygen as acceptor. The systematic name of this enzyme class is (S)-lactate:oxygen 2-oxidoreductase. It employs one cofactor, flavin mononucleotide.[4] The amino acid sequence of this enzyme is similar to that in lactate 2-monooxygenase, which converts lactate to acetate and carbon dioxide. The difference in the products formed has been ascribed to differences in the stability of an intermediate complex.[3]
The enzyme was first isolated and characterised from the bacterium Aerococcus viridans.[2] The relevant genes from Streptococcus iniae were subsequently cloned to allow further study.[5] These developments have allowed the enzyme to be used in biosensors which measure the concentration of lactic acid in blood.[1][6][7]
