BRENDA - Enzyme Database

Mechanism of action of coenzyme B12. Hydrogen transfer in the isomerization of beta-methylaspartate to glutamate

Eagar, R.G.; Baltimore, B.G.; Herbst, M.M.; Barker, H.A.; Richards, J.H.; Biochemistry 11, 253-264 (1972)

Data extracted from this reference:

Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
5.4.99.1
Clostridium tetanomorphum
-
-
-
Reaction
EC Number
Reaction
Commentary
Organism
5.4.99.1
L-threo-3-methylaspartate = L-glutamate
mechanism
Clostridium tetanomorphum
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5.4.99.1
L-Glu
-
3448
Clostridium tetanomorphum
threo-3-Methylaspartate
-
3448
Clostridium tetanomorphum
-
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
5.4.99.1
Cobalamin
dependent on
Clostridium tetanomorphum
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
5.4.99.1
Cobalamin
dependent on
Clostridium tetanomorphum
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5.4.99.1
L-Glu
-
3448
Clostridium tetanomorphum
threo-3-Methylaspartate
-
3448
Clostridium tetanomorphum
-