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-dihydroxyacetonephosphate 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-dihydroxyacetonephosphate by forming a covalent adduct with reaction intermediates.
journal_name
Int J Mol Scijournal_title
International journal of molecular sciencesauthors
Sobrado Pdoi
10.3390/ijms131114219subject
Has Abstractpub_date
2012-11-05 00:00:00pages
14219-42issue
11issn
1422-0067pii
ijms131114219journal_volume
13pub_type
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journal_title：International journal of molecular sciences
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更新日期：2019-12-24 00:00:00
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更新日期：2008-11-01 00:00:00
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