Crystallization (Comment) | Organism |
---|---|
mutants E383A, H361A and H243A in complex with substrate L-Val-L-Pro-L-Leu. Substrate interacts with one of the active site metal ions via its terminal amino group | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
E383A | crystallization data. One of the two metal sites is only partially occupied | Escherichia coli |
H243A | crystallization data. Mutant is capable of binding the substrate L-Val-L-Pro-L-Leu | Escherichia coli |
H361A | crystallization data. Mutant has residual catalytic activity | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P15034 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-Val-L-Pro-L-Leu + H2O | - |
Escherichia coli | L-Val + L-Pro-L-Leu | - |
? |