Literature summary for 5.4.99.1 extracted from

Hartzoulakis, B.; Gani, D.
The mechanism of glutamate mutase: an unusually substrate-specific enzyme (1994), Proc. Indian Acad. Sci. Chem. Sci., 106, 1165-1176.

No PubMed abstract available

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Inhibitors

Inhibitors	Comment	Organism	Structure
(2S)-Homocysteic acid	-	Clostridium tetanomorphum
(2S,3R)-3-Methylglutamate	-	Clostridium tetanomorphum
(2S,3S)-3-Methylglutamate	-	Clostridium tetanomorphum
(2S,4S)-4-Fluoroglutamic acid	-	Clostridium tetanomorphum
(S)-3-Methylitaconic acid	-	Clostridium tetanomorphum
1-Bromo-cyclopropane-cis-1,2-diacidic acid	-	Clostridium tetanomorphum
1-Bromo-cyclopropane-trans-1,2-diacidic acid	-	Clostridium tetanomorphum
2-Bromo-2,3-Methanosuccinic acid	-	Clostridium tetanomorphum
2-Methyleneglutaric acid	-	Clostridium tetanomorphum
Itaconic acid	-	Clostridium tetanomorphum

Organism

Organism	UniProt	Comment	Textmining
Clostridium tetanomorphum	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
L-threo-3-methylaspartate = L-glutamate	mechanism	Clostridium tetanomorphum	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-Glu	-	Clostridium tetanomorphum	threo-3-Methylaspartate	(2S,3S)-3-methylaspartate	?

Cofactor

Cofactor	Comment	Organism	Structure
Cobalamin	dependent on	Clostridium tetanomorphum

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Release 2023.1 (January 2023)