Catalytic Determinants of Alkene Production by the Cytochrome P450 Peroxygenase OleTJE.
Sarah Matthews,James Belcher,Kang Lan Tee,Hazel M. Girvan,Kirsty J. McLean,Stephen E. J. Rigby,Colin Levy,David Leys,David A. Parker,Richard T. Blankley,Andrew W. Munro +10 more
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TLDR
Key roles are identified for the active site amino acid trio in determining OleTJE catalytic efficiency in alkene production and in regulating protein stability, heme iron coordination, and spin state.About:
This article is published in Journal of Biological Chemistry.The article was published on 2017-03-24 and is currently open access. It has received 66 citations till now. The article focuses on the topics: Decarboxylation & Oxidative decarboxylation.read more
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Microbial and Enzymatic Degradation of Synthetic Plastics
TL;DR: The objective of this review is to outline the advances made in the microbial degradation of synthetic plastics and, overview the enzymes involved in biodegradation.
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Unrivalled diversity: the many roles and reactions of bacterial cytochromes P450 in secondary metabolism.
TL;DR: An overview of the range of chemical transformations that P 450 enzymes can catalyse within bacterial secondary metabolism is provided to provide an important resource to aid in understanding of the potential roles of P450 enzymes within newly identified bacterial biosynthetic pathways.
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Structure and function of the cytochrome P450 peroxygenase enzymes.
TL;DR: The biochemical properties of the P450 peroxygenases are focused on and on their biotechnological applications with respect to production of volatile alkenes as biofuels, as well as other fine chemicals.
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Kinetics of H 2 O 2 -driven degradation of chitin by a bacterial lytic polysaccharide monooxygenase
Silja Kuusk,Bastien Bissaro,Piret Kuusk,Zarah Forsberg,Vincent G. H. Eijsink,Morten Sørlie,Priit Väljamäe +6 more
TL;DR: itin degradation by the bacterial LPMO chitin-binding protein CBP21 using H2O2 as cosubstrate is provided, indicating that LPMOs have catalytic efficiencies similar to those of peroxygenases.
Journal ArticleDOI
Lytic Polysaccharide Monooxygenases in Enzymatic Processing of Lignocellulosic Biomass
Piotr Chylenski,Bastien Bissaro,Morten Sørlie,Åsmund K. Røhr,Anikó Várnai,Svein Jarle Horn,Vincent G. H. Eijsink +6 more
TL;DR: The discovery of lytic polysaccharide monooxygenases (LPMOs) has revolutionized enzymatic processing ofpolysaccharides, in particular, recalcitrant insoluble polysacchides, such as cellulose.
References
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Structure and Chemistry of Cytochrome P450
TL;DR: This review will concentrate on findings with P-450cam of the Pseudomonas putida camphor-5-exo-hydroxylase, and attention will be drawn to parallel and contrasting examples from other P- 450s as appropriate.
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Cytochrome P450 Compound I: Capture, Characterization, and C-H Bond Activation Kinetics
Jonathan Rittle,Michael Green +1 more
TL;DR: The spectroscopic and kinetic characterization of the long-sought principal intermediate involved in this process, P450 compound I (P450-I), which was prepared in approximately 75% yield by reacting ferric CYP119 with m-chloroperbenzoic acid is reported.
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Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency.
Rachel B. Kapust,József Tözsér,Jeffrey D. Fox,D. Eric Anderson,Scott Cherry,Terry D. Copeland,David S. Waugh +6 more
TL;DR: Results suggest that autoinactivation of TEV protease may be an intramolecular reaction that is facilitated by an allosteric interaction between protease molecules.
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Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors
TL;DR: A general rate equation has been derived and shown to be quadratic with square and linear terms in v which represents that true initial steady-state velocity of enzymic reactions that are reversibly inhibited by a substrate analogue at concentrations comparable to that of the enzyme.
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High-valent iron in chemical and biological oxidations.
TL;DR: Accumulated evidence shows that the ferryl species [Fe(IV)O](2+) can be formed under a variety of conditions including those related to the ferrous ion-hydrogen peroxide system known as Fenton's reagent, indicating that the oxygen rebound pathway is a ubiquitous mechanism for hydrocarbon oxygenation by both heme and non-heme iron enzymes.