Crystallization (Comment) | Organism |
---|---|
analysis of the 2.6-A resolution crystal structure of Escherichia coli AspRS with bound aspartyl-adenylate, AspAMP, molecular dynamics simulations | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | ligand binding thermodynamics and kinetics, overview | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | the co-substrate ATP binds preferentially with three associated Mg2+ cations in an unusual, bent geometry, the Mg2+ cations play a structural role and also participate catalytically in the enzyme reaction, co-binding of the ATP-Mg3+ complex increases the Asp/Asn binding free energy difference | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P21889 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp | active site structure, ligand and substrate binding, and reaction mechanism | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the co-substrate ATP binds preferentially with three associated Mg2+ cations in an unusual, bent geometry, the Mg2+ cations play a structural role and also participate catalytically in the enzyme reaction, co-binding of the ATP-Mg3+ complex increases the Asp/Asn binding free energy difference, indicating that amino acid discrimination is substrate-assisted, molecular dynamics simulations, overview | Escherichia coli | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Aspartyl-tRNA synthetase | - |
Escherichia coli |
AspRS | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | the co-substrate ATP binds preferentially with three associated Mg2+ cations in an unusual, bent geometry, co-binding of the ATP-Mg3+ complex increases the Asp/Asn binding free energy difference | Escherichia coli |