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4.3.1.3: histidine ammonia-lyase

This is an abbreviated version!
For detailed information about histidine ammonia-lyase, go to the full flat file.

Word Map on EC 4.3.1.3

Reaction

L-histidine
=
Urocanate
 +
NH3

Synonyms

ammonia-lyase, histidine, HAL, HAL1, Hal2, histidase, histidase, Hut, histidinase, histidinase-2, histidine alpha-deaminase, histidine ammonia lyase, histidine ammonia-lyase, histidine ammonia-lyase 2, histidine deaminase, L-HAL, L-histidase, L-histidine NH3-lyase

ECTree

     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.1 Ammonia-lyases
                4.3.1.3 histidine ammonia-lyase

Crystallization

Crystallization on EC 4.3.1.3 - histidine ammonia-lyase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
-
Achromobacter liquidum
-
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
-
crystal structure of C273A/D145A, C273A/F329A and C273A/F329G double mutants at 2.25 A, 2.0 A and 1.9 A resolution, respectively
crystal structure of native histidase inactivated with L-cystein at 1.0 A and Y280F mutant histidase at 1.7 A
structure solved to 1.8 A resolution
-
wild-type and mutant
-