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Literature summary 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

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.4.99.1 (2S)-Homocysteic acid
-
 Clostridium tetanomorphum
5.4.99.1 (2S,3R)-3-Methylglutamate
-
 Clostridium tetanomorphum
5.4.99.1 (2S,3S)-3-Methylglutamate
-
 Clostridium tetanomorphum
5.4.99.1 (2S,4S)-4-Fluoroglutamic acid
-
 Clostridium tetanomorphum
5.4.99.1 (S)-3-Methylitaconic acid
-
 Clostridium tetanomorphum
5.4.99.1 1-Bromo-cyclopropane-cis-1,2-diacidic acid
-
 Clostridium tetanomorphum
5.4.99.1 1-Bromo-cyclopropane-trans-1,2-diacidic acid
-
 Clostridium tetanomorphum
5.4.99.1 2-Bromo-2,3-Methanosuccinic acid
-
 Clostridium tetanomorphum
5.4.99.1 2-Methyleneglutaric acid
-
 Clostridium tetanomorphum
5.4.99.1 Itaconic acid
-
 Clostridium tetanomorphum

Organism

EC Number Organism UniProt Comment Textmining
5.4.99.1 Clostridium tetanomorphum
-
-
-

Reaction

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

Substrates and Products (Substrate)

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

Cofactor

EC Number Cofactor Comment Organism Structure
5.4.99.1 Cobalamin dependent on Clostridium tetanomorphum