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Literature summary for 6.3.4.4 extracted from

  • Wang, W.; Hou, Z.; Honzatko, R.B.; Fromm, H.J.
    Relationship of the conserved residues in the IMP binding site to substrate recognition and catalysis in Escherichia coli adenylosuccinate synthetase (1997), J. Biol. Chem., 272, 16911-16916.
    View publication on PubMed
Search for more literature for 6.3.4.4

Protein Variants

Protein Variants Comment Organism
L228A mutant enzymes L228A and S240A exhibit modest changes in their initial rate kinetics relative to the wild-type enzyme. The mutant enzymes Q224M and Q224E exhibit no significant change in Km values for GTP and Asp and modest change in Km values for IMP relative to the wild-type enzyme. The mutant Q224E shows an optimum pH at 6.2, which is 1.5 units lower than that of the wild-type enzyme. Mutant Q34E exhibits a 60fold decrease in turnover number compared with that of the wild-type enzyme Escherichia coli
Q224M mutant enzymes L228A and S240A exhibit modest changes in their initial rate kinetics relative to the wild-type enzyme. The mutant enzymes Q224M and Q224E exhibit no significant change in Km values for GTP and Asp and modest change in Km values for IMP relative to the wild-type enzyme. The mutant Q224E shows an optimum pH at 6.2, which is 1.5 units lower than that of the wild-type enzyme. Mutant Q34E exhibits a 60fold decrease in turnover number compared with that of the wild-type enzyme Escherichia coli
Q34E mutant enzymes L228A and S240A exhibit modest changes in their initial rate kinetics relative to the wild-type enzyme. The mutant enzymes Q224M and Q224E exhibit no significant change in Km values for GTP and Asp and modest change in Km values for IMP relative to the wild-type enzyme. The mutant Q224E shows an optimum pH at 6.2, which is 1.5 units lower than that of the wild-type enzyme. Mutant Q34E exhibits a 60fold decrease in turnover number compared with that of the wild-type enzyme Escherichia coli
S240A mutant enzymes L228A and S240A exhibit modest changes in their initial rate kinetics relative to the wild-type enzyme. The mutant enzymes Q224M and Q224E exhibit no significant change in Km values for GTP and Asp and modest change in Km values for IMP relative to the wild-type enzyme. The mutant Q224E shows an optimum pH at 6.2, which is 1.5 units lower than that of the wild-type enzyme. Mutant Q34E exhibits a 60fold decrease in turnover number compared with that of the wild-type enzyme Escherichia coli
S240E mutant enzymes L228A and S240A exhibit modest changes in their initial rate kinetics relative to the wild-type enzyme. The mutant enzymes Q224M and Q224E exhibit no significant change in Km values for GTP and Asp and modest change in Km values for IMP relative to the wild-type enzyme. The mutant Q224E shows an optimum pH at 6.2, which is 1.5 units lower than that of the wild-type enzyme. Mutant Q34E exhibits a 60fold decrease in turnover number compared with that of the wild-type enzyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Escherichia coli
0.0505
-
 IMP IMP, mutant Q224E Escherichia coli
0.0535
-
 GTP wild-type Escherichia coli
0.0605
-
 GTP mutant Q224M Escherichia coli
0.0689
-
 GTP mutant Q224E Escherichia coli
0.0798
-
 IMP mutant Q34E Escherichia coli
0.0825
-
 IMP mutant S240A Escherichia coli
0.0839
-
 GTP mutant L228A Escherichia coli
0.115
-
 Asp GTP, mutant S240A Escherichia coli
0.137
-
 IMP mutant L228A Escherichia coli
0.316
-
 IMP mutant Q224M Escherichia coli
0.32
-
 IMP Asp, mutant Q224E Escherichia coli
0.35
-
 Asp Asp, wild-type, and mutant Q224M Escherichia coli
0.38
-
 Asp mutant S240A Escherichia coli
0.52
-
 Asp mutant Q34E Escherichia coli
1.06
-
 Asp mutant L228A Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 wild-type and mutant enzymes L228A, S240A, and Q224E
-

Substrates and Products (Substrate)

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.2
-
 mutant Q224E Escherichia coli
7.7
-
 wild-type Escherichia coli