A Covalent Succinylcysteine-like Intermediate in the Enzyme-Catalyzed Transformation of Maleate to Fumarate by Maleate Isomerase

Florian Fisch; Carlos Martinez Fleites; Marie Delenne; Nina Baudendistel; Bernhard Hauer; Johan P. Turkenburg; Sam Hart; Neil C. Bruce; Gideon Grogan

doi:10.1021/ja1053576

A Covalent Succinylcysteine-like Intermediate in the Enzyme-Catalyzed Transformation of Maleate to Fumarate by Maleate Isomerase

Florian Fisch, Carlos Martinez Fleites, Marie Delenne, Nina Baudendistel, Bernhard Hauer, Johan P. Turkenburg, Sam Hart, Neil C. Bruce, Gideon Grogan

Research output: Contribution to journal › Article › peer-review

Abstract

Maleate isomerase (MI), a member of the Asp/Glu racemase superfamily, catalyzes cis-trans isomerization of the C2-C3 double bond in maleate to yield fumarate. Mutational studies, in conjunction with the structure of the C194A mutant of Nocardia farcinica MI cocrystallized with maleate, have revealed an unprecedented mode of catalysis for the superfamily in which the isomerization reaction is initiated by nucleophilic attack of cysteine at the double bond, yielding a covalent succinylcysteine-like intermediate.

Original language	English
Pages (from-to)	11455-11457
Number of pages	3
Journal	Journal of the American Chemical Society
Volume	132
Issue number	33
DOIs	https://doi.org/10.1021/ja1053576
Publication status	Published - 25 Aug 2010

Keywords

CIS-TRANS ISOMERASE
SUBTILIS GLUTAMATE RACEMASE
ARYLMALONATE DECARBOXYLASE
CRYSTAL-STRUCTURE
ESCHERICHIA-COLI
MECHANISM
EVOLUTION
CLONING
ACID

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http://pubs.acs.org/doi/abs/10.1021/ja1053576

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title = "A Covalent Succinylcysteine-like Intermediate in the Enzyme-Catalyzed Transformation of Maleate to Fumarate by Maleate Isomerase",

abstract = "Maleate isomerase (MI), a member of the Asp/Glu racemase superfamily, catalyzes cis-trans isomerization of the C2-C3 double bond in maleate to yield fumarate. Mutational studies, in conjunction with the structure of the C194A mutant of Nocardia farcinica MI cocrystallized with maleate, have revealed an unprecedented mode of catalysis for the superfamily in which the isomerization reaction is initiated by nucleophilic attack of cysteine at the double bond, yielding a covalent succinylcysteine-like intermediate.",

keywords = "CIS-TRANS ISOMERASE, SUBTILIS GLUTAMATE RACEMASE, ARYLMALONATE DECARBOXYLASE, CRYSTAL-STRUCTURE, ESCHERICHIA-COLI, MECHANISM, EVOLUTION, CLONING, ACID",

author = "Florian Fisch and Fleites, {Carlos Martinez} and Marie Delenne and Nina Baudendistel and Bernhard Hauer and Turkenburg, {Johan P.} and Sam Hart and Bruce, {Neil C.} and Gideon Grogan",

year = "2010",

month = aug,

day = "25",

doi = "10.1021/ja1053576",

language = "English",

volume = "132",

pages = "11455--11457",

journal = "Journal of the American Chemical Society",

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publisher = "American Chemical Society",

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T1 - A Covalent Succinylcysteine-like Intermediate in the Enzyme-Catalyzed Transformation of Maleate to Fumarate by Maleate Isomerase

AU - Fisch, Florian

AU - Fleites, Carlos Martinez

AU - Delenne, Marie

AU - Baudendistel, Nina

AU - Hauer, Bernhard

AU - Turkenburg, Johan P.

AU - Hart, Sam

AU - Bruce, Neil C.

AU - Grogan, Gideon

PY - 2010/8/25

Y1 - 2010/8/25

N2 - Maleate isomerase (MI), a member of the Asp/Glu racemase superfamily, catalyzes cis-trans isomerization of the C2-C3 double bond in maleate to yield fumarate. Mutational studies, in conjunction with the structure of the C194A mutant of Nocardia farcinica MI cocrystallized with maleate, have revealed an unprecedented mode of catalysis for the superfamily in which the isomerization reaction is initiated by nucleophilic attack of cysteine at the double bond, yielding a covalent succinylcysteine-like intermediate.

AB - Maleate isomerase (MI), a member of the Asp/Glu racemase superfamily, catalyzes cis-trans isomerization of the C2-C3 double bond in maleate to yield fumarate. Mutational studies, in conjunction with the structure of the C194A mutant of Nocardia farcinica MI cocrystallized with maleate, have revealed an unprecedented mode of catalysis for the superfamily in which the isomerization reaction is initiated by nucleophilic attack of cysteine at the double bond, yielding a covalent succinylcysteine-like intermediate.

KW - CIS-TRANS ISOMERASE

KW - SUBTILIS GLUTAMATE RACEMASE

KW - ARYLMALONATE DECARBOXYLASE

KW - CRYSTAL-STRUCTURE

KW - ESCHERICHIA-COLI

KW - MECHANISM

KW - EVOLUTION

KW - CLONING

KW - ACID

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U2 - 10.1021/ja1053576

DO - 10.1021/ja1053576

M3 - Article

SN - 0002-7863

VL - 132

SP - 11455

EP - 11457

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 33

ER -

A Covalent Succinylcysteine-like Intermediate in the Enzyme-Catalyzed Transformation of Maleate to Fumarate by Maleate Isomerase

Abstract

Keywords

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