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Literature summary for 6.3.4.4 extracted from

  • Dong, Q.; Liu, F.; Myers, A.M.; Fromm, H.J.
    Evidence for an arginine residue as the substrate binding site of Escherichia coli adenylosuccinate synthetase as studied by chemical modification and site-directed mutagenesis (1991), J. Biol. Chem., 266, 12228-12233.
    View publication on PubMed
Search for more literature for 6.3.4.4

Protein Variants

Protein Variants Comment Organism
R147L mutant R147L shows increased Km for IMP and GTP relative to the wild-type enzyme, Km for Asp exhibits a modest decrease Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Phenylglyoxal GTP or IMP partially protect Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.022
-
 GTP wild-type Escherichia coli
0.024
-
 IMP wild-type Escherichia coli
0.115
-
 Asp mutant R147L Escherichia coli
0.118
-
 IMP mutant R147L Escherichia coli
0.133
-
 GTP mutant R147L Escherichia coli
0.191
-
 Asp wild-type Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 wild-type and mutant R147L
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + IMP + L-Asp
-
 Escherichia coli GDP + phosphate + adenylosuccinate
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Escherichia coli