Abstract

Enzymes containing flavin cofactors are predominantly involved in redox reactions in numerous cellular processes where the protein environment modulates the chemical reactivity of the flavin to either transfer one or two electrons. Some flavoenzymes catalyze reactions with no net redox change. In these reactions, the protein environment modulates the reactivity of the flavin to perform novel chemistries. Recent mechanistic and structural data supporting novel flavin functionalities in reactions catalyzed by chorismate synthase, type II isopentenyl diphosphate isomerase, UDP-galactopyranose mutase, and alkyl-dihydroxyacetone phosphate synthase are presented in this review. In these enzymes, the flavin plays either a direct role in acid/base reactions or as a nucleophile or electrophile. In addition, the flavin cofactor is proposed to function as a 'molecular scaffold' in the formation of UDP-galactofuranose and alkyl-dihydroxyacetone phosphate by forming a covalent adduct with reaction intermediates. © 2012 by the authors; licensee MDPI, Basel, Switzerland.

Department(s)

Chemistry

Publication Status

Open Access

Comments

National Institute of General Medical Sciences, Grant R01GM094469

Keywords and Phrases

Alkyl-dihydroxyacetonephosphate synthase; Chorismate synthase; Flavoenyzmes; Non-redox reaction; Novel function; Type II isopentenyl diphosphate/dimethylallyl diphosphate isomerase; UDP-galactopyranose mutase

International Standard Serial Number (ISSN)

1422-0067; 1661-6596

Document Type

Article - Journal

Document Version

Final Version

File Type

text

Language(s)

English

Rights

© 2024 The Authors, All rights reserved.

Creative Commons Licensing

Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.

Publication Date

01 Jan 2012

PubMed ID

23203060

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