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Literature summary extracted from
- Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile (1999), Biochemistry, 38, 5355-5361.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.3.1.3 | Cys273A | - |
Pseudomonas putida |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.3.1.3 | Pseudomonas putida | P21310 | - |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 4.3.1.3 | L-histidine = urocanate + NH3 | mechanism | Pseudomonas putida |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.3.1.3 | L-histidine | natural substrate | Pseudomonas putida | urocanate + NH3 | - |
r |  |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.3.1.3 | tetramer | homotetramer with D2-symmetry, model building | Pseudomonas putida |
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Release 2023.1 (January 2023)
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