Source:http://linkedlifedata.com/resource/pubmed/id/18805424
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2008-11-25
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pubmed:databankReference | |
pubmed:abstractText |
The hydrolysis of 1,4,5,6-tetrahydro-6-oxonicotinate to 2-formylglutarate is a central step in the catabolism of nicotinate in several Clostridia and Proteobacteria. This reaction is catalyzed by the novel enzyme enamidase, a new member of the amidohydrolase superfamily as indicated by its unique reaction, sequence relationship, and the stoichiometric binding of iron and zinc. A hallmark of enamidase is its capability to catalyze a two-step reaction: the initial decyclization of 1,4,5,6-tetrahydro-6-oxonicotinate leading to 2-(enamine)glutarate followed by an additional hydrolysis step yielding (S)-2-formylglutarate. Here, we present the crystal structure of enamidase from Eubacterium barkeri at 1.9 A resolution, providing a structural basis for catalysis and suggesting a mechanism for its exceptional activity and enantioselectivity. The enzyme forms a 222-symmetric tetramer built up by a dimer of dimers. Each enamidase monomer consists of a composite beta-sandwich domain and an (alpha/beta)(8)-TIM-barrel domain harboring the active site. With its catalytic binuclear metal center comprising both zinc and iron ions, enamidase represents a special case of subtype II amidohydrolases.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1089-8638
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
26
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pubmed:volume |
384
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
837-47
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pubmed:meshHeading |
pubmed-meshheading:18805424-Amino Acid Sequence,
pubmed-meshheading:18805424-Aminohydrolases,
pubmed-meshheading:18805424-Binding Sites,
pubmed-meshheading:18805424-Catalytic Domain,
pubmed-meshheading:18805424-Crystallography, X-Ray,
pubmed-meshheading:18805424-Dimerization,
pubmed-meshheading:18805424-Eubacterium,
pubmed-meshheading:18805424-Metabolic Networks and Pathways,
pubmed-meshheading:18805424-Models, Molecular,
pubmed-meshheading:18805424-Molecular Sequence Data,
pubmed-meshheading:18805424-Niacin,
pubmed-meshheading:18805424-Protein Structure, Tertiary,
pubmed-meshheading:18805424-Sequence Alignment
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pubmed:year |
2008
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pubmed:articleTitle |
The crystal structure of enamidase: a bifunctional enzyme of the nicotinate catabolism.
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pubmed:affiliation |
Philipps-Universität Marburg, Fachbereich Chemie, Marburg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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