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Literature summary for 6.3.4.4 extracted from

  • Wang, W.; Poland, B.W.; Honzatko, R.B.; Fromm, H.J.
    Identification of arginine residues in the putative L-aspartate binding site of Escherichia coli adenylosuccinate synthetase (1995), J. Biol. Chem., 270, 13160-13168.
    View publication on PubMed
Search for more literature for 6.3.4.4

Protein Variants

Protein Variants Comment Organism
R303L mutant enzymes R303L, R304L, and R305L exhibit a 50-200fold increase in their Km values for Asp relative to the wild-type enzyme. The Km values for GTP and IMP are comparable Escherichia coli
R304L mutant enzymes R303L, R304L, and R305L exhibit a 50-200fold increase in their Km values for Asp relative to the wild-type enzyme. The Km values for GTP and IMP are comparable Escherichia coli
R305L mutant enzymes R303L, R304L, and R305L exhibit a 50-200fold increase in their Km values for Asp relative to the wild-type enzyme. The Km values for GTP and IMP are comparable Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.01
-
 GTP Asp, mutant R305L Escherichia coli
0.0201
-
 GTP mutant R303L Escherichia coli
0.026
-
 GTP wild-type Escherichia coli
0.0265
-
 GTP mutant R304L Escherichia coli
0.0278
-
 IMP wild-type Escherichia coli
0.0296
-
 IMP mutant R304L Escherichia coli
0.0305
-
 IMP mutant R305L Escherichia coli
0.0306
-
 GTP mutant R305L Escherichia coli
0.0352
-
 IMP mutant R303L Escherichia coli
0.057
-
 Asp mutant R303L Escherichia coli
0.0657
-
 Asp mutant R303L Escherichia coli
0.23
-
 Asp Asp, wild-type Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 wild-type and mutant enzymes R303L, R304L, and R305L
-

Purification (Commentary)

Purification (Comment) Organism
mutant enzymes R303L, R304L, and R305L Escherichia coli

Substrates and Products (Substrate)

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