Cloned (Comment) | Organism |
---|---|
- |
Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Km-values of a number of site-specific mutant enzymes | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
wild-type and mutant enzymes, E317A, E317Q, T318A, Y319A, Y319F, D320A, V321A, T322A, T322S, T322V, T322Y, T323A, T323I, T323L, T323S, T323V, R325A, R325K, T328S | - |
Purification (Comment) | Organism |
---|---|
- |
Escherichia coli |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate | Arg325 is involved in stabilization of a pentacovalent intermediate leading to the formation of beta-aspartyl-AMP | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-Asp + L-Gln | - |
Escherichia coli | AMP + diphosphate + Asn + Glu | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | turnover-numbers of a number of site-specific AS-B mutant enzymes | Escherichia coli |