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Literature summary for 6.3.4.4 extracted from

  • Moe, O.A.; Baker-Malcolm, J.F.; Wang, W.; Kang, C.; Fromm, H.J.; Colman, R.F.
    Involvement of arginine 143 in nucleotide substrate binding at the active site of adenylosuccinate synthetase from Escherichia coli (1996), Biochemistry, 35, 9024-9033.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
R143L mutant enzyme R143L with no change in catalytic constant or Km for Asp, but significantly impaired nucleotide binding, 60fold increased Km for IMP and 10fold increased Km for GTP Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Guanosine 5'-O-[S-(4-bromo-2,3-dioxobutyl)thio]phosphate
-
Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.026
-
GTP wild-type Escherichia coli
0.03
-
Asp IMP, wild-type Escherichia coli
0.23
-
Asp Asp, wild-type Escherichia coli
0.269
-
GTP mutant R143L Escherichia coli
0.34
-
allopurinol ribonucleotide Asp, mutant R143L Escherichia coli
1.73
-
IMP mutant R143L Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
wild-type and mutant R143L
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + 4-hydroxypyrazolo[3,4-d]pyrimidine ribonucleotide + L-Asp
-
Escherichia coli GDP + phosphate + 4-aminopyrazolo[3,4-d]pyrimidine ribonucleotide
-
?
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