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Literature summary 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

EC Number Protein Variants Comment Organism
6.3.4.4 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

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.4.4 0.026
-
GTP wild-type Escherichia coli
6.3.4.4 0.03
-
Asp IMP, wild-type Escherichia coli
6.3.4.4 0.23
-
Asp Asp, wild-type Escherichia coli
6.3.4.4 0.269
-
GTP mutant R143L Escherichia coli
6.3.4.4 0.34
-
allopurinol ribonucleotide Asp, mutant R143L Escherichia coli
6.3.4.4 1.73
-
IMP mutant R143L Escherichia coli

Organism

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

Substrates and Products (Substrate)

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