Structure and role for active site lid of lactate monooxygenase from Mycobacterium smegmatis.

ABSTRACT: Lactate monooxygenase (LMO) catalyzes the FMN-dependent "coupled" oxidation of lactate and O₂ to acetate, carbon dioxide, and water, involving pyruvate and hydrogen peroxide as enzyme-bound intermediates. Other α-hydroxy acid oxidase family members follow an "uncoupled pathway," wherein the α-keto acid product quickly dissociates before the reduced flavin reacts with oxygen. Here, we report the structures of Mycobacterium smegmatis wild-type LMO and a wild-type-like C203A variant at 2.1 Å and 1.7 Å resolution, respectively. The overall LMO fold and active site organization, including a bound sulfate mimicking substrate, resemble those of other α-hydroxy acid oxidases. Based on structural similarity, LMO is similarly distant from lactate oxidase, glycolate oxidase, mandelate dehy

SUBMITTER: Kean KM 

PROVIDER: S-EPMC6295902 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature