Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli as a His-tagged fusion protein | Bacillus cereus |
Crystallization (Comment) | Organism |
---|---|
crystal structure of a DltA is determined at 2.0 A resolution in complex with the D-alanine adenylate intermediate of the first reaction. Despite the low level of sequence similarity, the DltA structure resembles known structures of adenylation domains such as the acetyl-CoA synthetase. The enantiomer selection appears to be enhanced by the medium-sized side chain of Cys-269 | Bacillus cereus |
Protein Variants | Comment | Organism |
---|---|---|
C269A | C269A mutation relaxes D-Ala preference. Km (mM): (D-Ala) 3.1, (L-Ala) 6.6, kcat (1/sec): (D-Ala) 0.103, (L-Ala) 0.12 | Bacillus cereus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.1 | - |
D-Ala | wild-tpye | Bacillus cereus | |
3.1 | - |
D-Ala | mutant C269A | Bacillus cereus | |
6.6 | - |
L-Ala | mutant C269A | Bacillus cereus | |
14.4 | - |
L-Ala | wild-tpye | Bacillus cereus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus cereus | Q81G39 | - |
- |
Purification (Comment) | Organism |
---|---|
using Ni-NTA chromatography | Bacillus cereus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + D-Ala + diphosphate | - |
Bacillus cereus | ? | - |
? | |
ATP + L-Ala + diphosphate | - |
Bacillus cereus | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
BcDltA | - |
Bacillus cereus |
D-alanyl carrier protein ligase | - |
Bacillus cereus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.025 | - |
D-Ala | wild-tpye | Bacillus cereus | |
0.103 | - |
D-Ala | mutant C269A | Bacillus cereus | |
0.11 | - |
L-Ala | wild-tpye | Bacillus cereus | |
0.12 | - |
L-Ala | mutant C269A | Bacillus cereus |