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methylaspartate mutase

Known as: glutamate mutase 
National Institutes of Health

Related topics

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2 relations

Broader (2)

Amino Acid IsomerasesMutase

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2019
2019
Photolytic Cleavage of Co-C Bond in Coenzyme B12-Dependent Glutamate Mutase.
Glutamate mutase (GLM) is a coenzyme B12-dependent enzyme that catalyzes the conversion of S-glutamate to (2 S,3 S)-3-methyl… Expand
2015
2015
Production of mesaconate in Escherichia coli by engineered glutamate mutase pathway.
Mesaconate is an intermediate in the glutamate degradation pathway of microorganisms such as Clostridium tetanomorphum. However… Expand
2015
2015
Synthesis, solution and crystal structure of the coenzyme B(12) analogue Co(β)-2'-fluoro-2',5'-dideoxyadenosylcobalamin.
Crystal structure analyses have helped to decipher the mode of binding of coenzyme B12 (AdoCbl) in the active site of AdoCbl… Expand
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2010
2010
Theoretical analysis of the diradical nature of adenosylcobalamin cofactor-tyrosine complex in B12-dependent mutases: inspiring PCET-driven enzymatic catalysis.
Detailed theoretical and X-ray based structural analysis has been carried out in order to unmask the role of the tyrosine residue… Expand
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2009
2009
On the importance of ribose orientation in the substrate activation of the coenzyme B12-dependent mutases.
The degree to which the corrin ring portion of coenzyme B(12) can facilitate the H-atom-abstraction step in the glutamate mutase… Expand
Highly Cited
1999
Highly Cited
1999
Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme B12-dependent enzyme provides new mechanistic insights.
BACKGROUND Glutamate mutase (Glm) equilibrates (S)-glutamate with (2S,3S)-3-methylaspartate. Catalysis proceeds with the… Expand
1999
1999
Structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium cochlearium.
Glutamate mutase (Glm) is an adenosylcobamide-dependent enzyme that catalyzes the reversible rearrangement of (2S)-glutamate to… Expand
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