EC Number | Crystallization (Comment) | Organism |
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4.3.1.3 | construction of enzyme structure with a closed active site by modifying the HAL structure including the L-cysteine inhibitor by replacement of the 39-80 loop containing the catalytically essential Tyr53, in every subunit of the homotetrameric enzyme. The most plausible reaction pathway involves the N-3,5-dihydro-5-methylidene-4H-imidazol-4-one intermediate structure in which the L-histidine substrate is covalently bound to the N-3,5-dihydro-5-methylidene-4H-imidazol-4-one prosthetic group of the apoenzyme via the amino group. Zn-complex formation plays a role in the reactivity and substrate specificity | Pseudomonas putida |
EC Number | Organism | UniProt | Comment | Textmining |
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4.3.1.3 | Pseudomonas putida | - |
- |
- |