Flavoenzymes: diverse catalysts with recurrent features
Marco W. Fraaije,Andrea Mattevi +1 more
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TLDR
Modulation of substrate and cofactor reactivity and exact positioning of the substrate are key elements in the mode of action of these enzymes.About:
This article is published in Trends in Biochemical Sciences.The article was published on 2000-03-01 and is currently open access. It has received 475 citations till now. The article focuses on the topics: Flavoprotein & Flavin group.read more
Figures
Figure 4 Schematic view of different mechanisms for flavin-catalysed substrate-dehydrogenation reactions – direct hydride transfer (1), the carbanion mechanism (2,3) and the radical mechanism (4,5). R1 and R2 indicate unspecific substituents of the CH atom undergoing oxidation, and X is the activating group. 
Table 1. Binding features of the isoalloxazine ring in flavin-dependent enzymes 
Table 2. Stereochemistry of substrate binding in flavoenzyme structures
Citations
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Structure and function of xanthine oxidoreductase: where are we now?
TL;DR: Of special interest has been the finding that XOR can catalyze the reduction of nitrates and nitrites to nitric oxide (NO), acting as a source of both NO and peroxynitrite.
Journal ArticleDOI
Evolution of function in protein superfamilies, from a structural perspective.
TL;DR: The functional variation of homologous enzyme superfamilies containing two or more enzymes, as defined by the CATH protein structure classification, is assessed by way of the Enzyme Commission (EC) scheme.
Journal ArticleDOI
Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion
TL;DR: The crystal structure of the dimeric bovine milk XDH is presented and the major changes that occur on the proteolytic transformation of XDH to the XO form are described, reflecting the switch of substrate specificity observed for the two forms of this enzyme.
Journal ArticleDOI
Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders
TL;DR: The structure provides a framework for probing the catalytic mechanism, understanding the differences between the B- and A-monoamine oxidase isoforms and designing specific inhibitors.
Journal ArticleDOI
Type II polyketide synthases: gaining a deeper insight into enzymatic teamwork
TL;DR: This review covers advances in understanding of the biosynthesis of polyketides produced by type II PKS systems at the genetic, biochemical and structural levels.
References
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Journal ArticleDOI
The Protein Data Bank: a computer-based archival file for macromolecular structures.
Frances C. Bernstein,Thomas F. Koetzle,Graheme J. B. Williams,Edgar F. Meyer,Michael D. Brice,John R. Rodgers,O. Kennard,Takehiko Shimanouchi,Mitsuo Tasumi +8 more
TL;DR: The Protein Data Bank is a computer-based archival file for macromolecular structures that stores in a uniform format atomic co-ordinates and partial bond connectivities, as derived from crystallographic studies.
Journal ArticleDOI
Catalytic triads and their relatives
Guy Dodson,Alexander Wlodawer +1 more
TL;DR: Review of these enzymes shows that the acid-base-ser/thr pattern of catalytic residues is generally conserved, although the individual acids and bases can vary.
Journal ArticleDOI
Mechanisms of flavoprotein-catalyzed reactions.
Sandro Ghisla,Vincent Massey +1 more
TL;DR: This review describes the best studied of Flavoproteins mechanisms and discusses factors possibly governing reactivity and specificity.
Journal ArticleDOI
Structure of the Escherichia coli fumarate reductase respiratory complex.
TL;DR: The crystal structure of intact fumarate reductase has been solved at 3.3 angstrom resolution and demonstrates that the cofactors are arranged in a nearly linear manner from the membrane-bound quinone to the active site flavin.
Journal ArticleDOI
The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction.
TL;DR: The crystallographic structures of two FAD-containing enzyme complexes suggest that direct hydride transfers from NAD(P)H to FAD and from FADH2 to the quinone provide a simple rationale for the obligatory two-electron reductions involving a ping-pong mechanism.
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