Work

Inactivation of a Flavoprotein, Lactate Oxidase, by an Acetylenic Substrate

Year: 1972

Type: article

Abstract: The acetylenic substrate, 2-hydroxy-3-butynoic acid, inactivates lactate oxidase from Mycobacterium smegmatis. When inactivated lactate oxidase is separated into flavin and apoprotein components, the apoprotein is reactivatable by exogenous FMN while the flavin has been converted to a fluorescent, reduced species stable to autoxidation. Incubation of enzyme with 2-OH-3-[4-3H]butynoate produces a 3H-labeled covalent adduct with the flavin coenzyme upon inactivation. When 2-OH[2-3H]butynoate is used, no 3H is incorporated on inactivation into either the flavocoenzyme or the apoprotein, indicating that the C2-hydrogen must be lost in the inactivation process which involves adduct formation between substrate and flavin.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(19)44857-6

Authors: Christopher T. Walsh, Agnes Schonbrunn, Oksana Lockridge, Vincent Massey, Robert H. Abeles

Institutions: University of Michigan, Brandeis University

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

OpenAlex ID: W1526638050

FWCI: 14.3

Cites: 11

Cited by: 79

Related to: 10