EC Number   |
Protein Variants |
Reference |
|---|
    6.3.5.4 | A380S |
naturally occuring mutation, homozygous mutation, mutation of a polar residue in the hydrophobic region |
745375 |
| 6.3.5.4 | A6E |
naturally occuring mutation, compound heterozygous, mutation of a charged amino acid in hydrophobic region, causing steric clash with Phe8 |
745375 |
| 6.3.5.4 | C1A |
altering Cys-1 to either Ala or Ser eliminated the Gln-dependent activity, while only minimally affecting the kinetic properties of the NH4+-dependent reaction |
1695 |
| 6.3.5.4 | C1A |
replacement of Cys1 by either Ala or Ser results in a loss of glutaminase activity and Gln-dependent activity, without any significant effect upon NH4+-dependent Asn synthesis. Kinetic parameters of the NH4+-dependent activity of H29A and H80A are unchanged with respect to wild-type AS-B, the apparent Km for Gln is increased by a factor of 4.5 in Gln-dependent Asn synthesis |
1702 |
| 6.3.5.4 | C1S |
altering Cys-1 to either Ala or Ser eliminated the Gln-dependent activity, while only minimally affecting the kinetic properties of the NH4+-dependent reaction |
1695 |
| 6.3.5.4 | C1S |
replacement of Cys1 by either Ala or Ser results in a loss of glutaminase activity and Gln-dependent activity, without any significant effect upon NH4+-dependent Asn synthesis. Kinetic parameters of the NH4+-dependent activity of H29A and H80A are unchanged with respect to wild-type AS-B, the apparent Km for Gln is increased by a factor of 4.5 in Gln-dependent Asn synthesis |
1702 |
| 6.3.5.4 | E317A |
diminished glutaminase activity |
649262 |
| 6.3.5.4 | E348A |
mutant exhibits similar glutaminase activity to the wild-type enzyme in the absence of ATP, but is not capable of catalyzing asparagine formation when glutamine is employed as a nitrogen source |
714228 |
| 6.3.5.4 | E348A |
mutant shows similar glutaminase activity to the wild-type enzyme in the absence of ATP, mutant is not capable of catalyzing asparagine formation when glutamine is employed as a nitrogen source, mutant shows no synthetase activity, ATP-dependent stimulation of glutaminase activity is less than that of wild-type enzyme |
714228 |
| 6.3.5.4 | E348D |
mutant exhibits similar glutaminase activity to the wild-type enzyme in the absence of ATP and is capable of catalyzing asparagine formation when glutamine is employed as a nitrogen source. Formation of the beta-aspartyl-AMP intermediate, and therefore the eventual production of asparagine, is dependent on the presence of a carboxylate side chain at this position in the synthetase active site. In addition, E348 may also play a role in mediating the conformational changes needed to coordinate, albeit weakly, the glutaminase and synthetase activities of the enzyme and to establish the structural integrity of the intramolecular tunnel along which ammonia is translocated |
714228 |
