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Literature summary for 5.4.99.1 extracted from

  • Patwardhan, A.; Marsh, E.N.
    Changes in the free energy profile of glutamate mutase imparted by the mutation of an active site arginine residue to lysine (2007), Arch. Biochem. Biophys., 461, 194-199.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.4.99.1

Cloned(Commentary)

Cloned (Comment) Organism
-
 Clostridium cochlearium

Protein Variants

Protein Variants Comment Organism
R100K mutation significantly impairs the ability of enzyme to catalyze the rearrangement of substrate radical to product radical Clostridium cochlearium

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.14
-
 L-threo-3-methylaspartate wild-type, pH 7.0 Clostridium cochlearium
9.5
-
 L-threo-3-methylaspartate mutant R100K, pH 7.0 Clostridium cochlearium

Organism

Organism UniProt Comment Textmining
Clostridium cochlearium
-
-
-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.073
-
 L-threo-3-methylaspartate mutant R100K, pH 7.0 Clostridium cochlearium
5.4
-
 L-threo-3-methylaspartate wild-type, pH 7.0 Clostridium cochlearium