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Literature summary for 5.4.99.1 extracted from

  • Hoffmann, B.; Konrat, R.; Bothe, H.; Buckel, W.; Krautler, B.
    Structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium cochlearium (1999), Eur. J. Biochem., 263, 178-188.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Clostridium cochlearium
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate
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Clostridium cochlearium L-threo-3-methylaspartate
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?

Cofactor

Cofactor Comment Organism Structure
coenzyme B12 the alpha2beta2 tetramer consists of two subunits, subunit MutS of 53600 Da and subunit GlmS of 14800 Da, whose assembly is mediated by coenzyme B12. In GlnS and MutS the sequence motif, Asp-Xaa-His-Xaa-Xaa-Gly, which includes the cobalt-coordinating histidine residue, and a predicted alpha-helical region following the motif, are present as an unstructured and highly mobile loop. In the absence of coenzyme, the B12-binding site apparently is only partially formed. Important elements of the binding site only become structured upon binding B12, these include the cobalt-coordinating histidine residue, and an alpha helix that forms one side of the cleft accomodating the nucleotide tail of the coenzyme Clostridium cochlearium