Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme B12-dependent enzyme provides new mechanistic insights (Q27619519)

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G Jogl

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U G Wagner

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H Bothe

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W Buckel

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C Kratky

Mechanisms of coenzyme B12-dependent rearrangements

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publication date

15 August 1999

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published in

Structure

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volume

7

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issue

8

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page(s)

891-902

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cites work

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The reactivity of B12 cofactors: the proteins make a difference

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Structure-based perspectives on B12-dependent enzymes

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How a protein binds B12: A 3.0 A X-ray structure of B12-binding domains of methionine synthase

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How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 A resolution

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Conformational changes on substrate binding to methylmalonyl CoA mutase and new insights into the free radical mechanism

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How a protein prepares for B12 binding: structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium tetanomorphum

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Glutamate mutase from Clostridium cochlearium. Purification, cobamide content and stereospecific inhibitors

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Characterization of the coenzyme-B12-dependent glutamate mutase from Clostridium cochlearium produced in Escherichia coli

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Coordination of a histidine residue of the protein‐component S to the cobalt atom in coenzyme B12‐dependent glutamate mutase from Clostridium cochlearium

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Cloning and sequencing of glutamate mutase component S from Clostridium tetanomorphum. Homologies with other cobalamin-dependent enzymes

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Crystallization and preliminary X-ray analysis of recombinant glutamate mutase and of the isolated component S from Clostridium cochlearium

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

10467146

1 reference

Consolidated OpenCitations Corpus – April 2017