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Literature summary for 6.3.4.4 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
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Protein Variants

Protein Variants Comment Organism
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
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
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]

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

Organism

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

Reaction

Reaction Comment Organism Reaction ID
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)

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