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Emergent mechanistic diversity of enzyme-catalysed beta-diketone cleavage

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Emergent mechanistic diversity of enzyme-catalysed beta-diketone cleavage. / Grogan, G .

In: Biochemical journal, Vol. 388, 15.06.2005, p. 721-730.

Research output: Contribution to journalLiterature reviewpeer-review

Harvard

Grogan, G 2005, 'Emergent mechanistic diversity of enzyme-catalysed beta-diketone cleavage', Biochemical journal, vol. 388, pp. 721-730. https://doi.org/10.1042/BJ20042038

APA

Grogan, G. (2005). Emergent mechanistic diversity of enzyme-catalysed beta-diketone cleavage. Biochemical journal, 388, 721-730. https://doi.org/10.1042/BJ20042038

Vancouver

Grogan G. Emergent mechanistic diversity of enzyme-catalysed beta-diketone cleavage. Biochemical journal. 2005 Jun 15;388:721-730. https://doi.org/10.1042/BJ20042038

Author

Grogan, G . / Emergent mechanistic diversity of enzyme-catalysed beta-diketone cleavage. In: Biochemical journal. 2005 ; Vol. 388. pp. 721-730.

Bibtex - Download

@article{f6c4db827bac4e7f80566840d28f5e44,
title = "Emergent mechanistic diversity of enzyme-catalysed beta-diketone cleavage",
abstract = "The enzymatic cleavage of C-C bonds in beta-diketones is, comparatively, a little studied biochemical process, but one that has important relevance to human metabolism, bioremediation and preparative biocatalysis. In recent studies, four types of enzymes have come to light that cleave C-C bonds in the beta-diketone functionality using different chemical mechanisms. OPH [oxidized poly(vinyl alcohol) hydrolase from Pseudomonas sp. strain VM15C], which cleaves nonane-4,6-dione to butyrate and pentan-2-one is a serine-triad hydrolase. Dke1 (diketone-cleaving enzyme from Acinetobacter johnsonii) is a dioxygenase, cleaving acetylacetone to methylglyoxal and acetate. Fumarylacetoacetate hydrolase cleaves fumarylacetoacetate to fumarate and acetoacetate using a water molecule, activated by a catalytic His/Asp dyad, aided by a calcium ion that both chelates the enol acid form of the substrate and indirectly positions the water for nucleophilic attack at a carbonyl group. 6-Oxocamphor hydrolase cleaves nonenolizable cyclic beta-diketones and is a homologue of the crotonase superfamily, employing a catalytic His/Asp dyad to activate a water molecule for nucleophilic attack at a carbonyl group on one prochiral face of the diketone substrate, effecting desymmetrizations of symmetrical substrates.",
keywords = "catalytic triad, crotonase, beta-diketone, dioxygenase, hydrolase, polyketide, POLYVINYL ALCOHOL)-DEGRADING ENZYME, RETRO-CLAISEN REACTION, CRYSTAL-STRUCTURE, CROTONASE SUPERFAMILY, PSEUDOMONAS SP, ANGSTROM RESOLUTION, ACINETOBACTER-JOHNSONII, SUBSTRATE-SPECIFICITY, DEGRADING ENZYME, CLEAVING ENZYME",
author = "G Grogan",
year = "2005",
month = jun,
day = "15",
doi = "10.1042/BJ20042038",
language = "English",
volume = "388",
pages = "721--730",
journal = "Biochemical journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Emergent mechanistic diversity of enzyme-catalysed beta-diketone cleavage

AU - Grogan, G

PY - 2005/6/15

Y1 - 2005/6/15

N2 - The enzymatic cleavage of C-C bonds in beta-diketones is, comparatively, a little studied biochemical process, but one that has important relevance to human metabolism, bioremediation and preparative biocatalysis. In recent studies, four types of enzymes have come to light that cleave C-C bonds in the beta-diketone functionality using different chemical mechanisms. OPH [oxidized poly(vinyl alcohol) hydrolase from Pseudomonas sp. strain VM15C], which cleaves nonane-4,6-dione to butyrate and pentan-2-one is a serine-triad hydrolase. Dke1 (diketone-cleaving enzyme from Acinetobacter johnsonii) is a dioxygenase, cleaving acetylacetone to methylglyoxal and acetate. Fumarylacetoacetate hydrolase cleaves fumarylacetoacetate to fumarate and acetoacetate using a water molecule, activated by a catalytic His/Asp dyad, aided by a calcium ion that both chelates the enol acid form of the substrate and indirectly positions the water for nucleophilic attack at a carbonyl group. 6-Oxocamphor hydrolase cleaves nonenolizable cyclic beta-diketones and is a homologue of the crotonase superfamily, employing a catalytic His/Asp dyad to activate a water molecule for nucleophilic attack at a carbonyl group on one prochiral face of the diketone substrate, effecting desymmetrizations of symmetrical substrates.

AB - The enzymatic cleavage of C-C bonds in beta-diketones is, comparatively, a little studied biochemical process, but one that has important relevance to human metabolism, bioremediation and preparative biocatalysis. In recent studies, four types of enzymes have come to light that cleave C-C bonds in the beta-diketone functionality using different chemical mechanisms. OPH [oxidized poly(vinyl alcohol) hydrolase from Pseudomonas sp. strain VM15C], which cleaves nonane-4,6-dione to butyrate and pentan-2-one is a serine-triad hydrolase. Dke1 (diketone-cleaving enzyme from Acinetobacter johnsonii) is a dioxygenase, cleaving acetylacetone to methylglyoxal and acetate. Fumarylacetoacetate hydrolase cleaves fumarylacetoacetate to fumarate and acetoacetate using a water molecule, activated by a catalytic His/Asp dyad, aided by a calcium ion that both chelates the enol acid form of the substrate and indirectly positions the water for nucleophilic attack at a carbonyl group. 6-Oxocamphor hydrolase cleaves nonenolizable cyclic beta-diketones and is a homologue of the crotonase superfamily, employing a catalytic His/Asp dyad to activate a water molecule for nucleophilic attack at a carbonyl group on one prochiral face of the diketone substrate, effecting desymmetrizations of symmetrical substrates.

KW - catalytic triad

KW - crotonase

KW - beta-diketone

KW - dioxygenase

KW - hydrolase

KW - polyketide

KW - POLYVINYL ALCOHOL)-DEGRADING ENZYME

KW - RETRO-CLAISEN REACTION

KW - CRYSTAL-STRUCTURE

KW - CROTONASE SUPERFAMILY

KW - PSEUDOMONAS SP

KW - ANGSTROM RESOLUTION

KW - ACINETOBACTER-JOHNSONII

KW - SUBSTRATE-SPECIFICITY

KW - DEGRADING ENZYME

KW - CLEAVING ENZYME

U2 - 10.1042/BJ20042038

DO - 10.1042/BJ20042038

M3 - Literature review

VL - 388

SP - 721

EP - 730

JO - Biochemical journal

JF - Biochemical journal

SN - 0264-6021

ER -