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Literature summary extracted from

  • Kang, C.; Fromm, H.J.
    Characterization of the putative GTP-binding site residues of Escherichia coli adenylosuccinate synthetase by site-directed mutagenesis (1994), Arch. Biochem. Biophys., 310, 475-480.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
6.3.4.4 G15V the secondary structure of the G15V mutant is significantly altered by GTP and IMP, whereas that of the wild-type enzyme is not changed, however the two enzymes exhibit similar secondary structures in the absence of substrates. K331L mutant enzyme shows a 27fold increased Km for GTP, and the K331R mutant a 20fold increased Km for GTP Escherichia coli
6.3.4.4 K331l the secondary structure of the G15V mutant is significantly altered by GTP and IMP, whereas that of the wild-type enzyme is not changed, however the two enzymes exhibit similar secondary structures in the absence of substrates. K331L mutant enzyme shows a 27fold increased Km for GTP, and the K331R mutant a 20fold increased Km for GTP Escherichia coli
6.3.4.4 K331R the secondary structure of the G15V mutant is significantly altered by GTP and IMP, whereas that of the wild-type enzyme is not changed, however the two enzymes exhibit similar secondary structures in the absence of substrates. K331L mutant enzyme shows a 27fold increased Km for GTP, and the K331R mutant a 20fold increased Km for GTP Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.4.4 0.021
-
 IMP wild-type Escherichia coli
6.3.4.4 0.022
-
 GTP wild-type Escherichia coli
6.3.4.4 0.025
-
 GTP mutant G15V Escherichia coli
6.3.4.4 0.035
-
 GTP IMP, mutant G15V Escherichia coli
6.3.4.4 0.041
-
 IMP mutant K331L Escherichia coli
6.3.4.4 0.047
-
 IMP IMP, mutant K331R Escherichia coli
6.3.4.4 0.28
-
 Asp wild-type Escherichia coli
6.3.4.4 0.35
-
 Asp mutant G15V Escherichia coli
6.3.4.4 0.44
-
 Asp GTP, mutant K331R Escherichia coli
6.3.4.4 0.6
-
 GTP mutant K331L Escherichia coli
6.3.4.4 1.73
-
 IMP Asp, mutant K331R Escherichia coli
6.3.4.4 5.4
-
 Asp mutant K331L Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
6.3.4.4 Escherichia coli
-
 wild-type and mutant enzymes: G15V, K331L, and K331R
-

Reaction

EC Number Reaction Comment Organism Reaction ID
6.3.4.4 GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP phosphate-binding region of adenylosuccinate synthetase is involved in a conformational change induced by GTP and IMP binding. GTP and IMP binding depend on the presence of the other substrate at the active site of the enzyme Escherichia coli
a

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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