EC 4.3.1.3 - Histidine ammonia-lyase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 4.3.1.3
Names
Accepted name:
histidine ammonia-lyase
Other
names:
histidase
histidinase
histidine α-deaminase
L-histidine ammonia-lyase
histidinase
histidine α-deaminase
L-histidine ammonia-lyase
Systematic name:
L-histidine ammonia-lyase (urocanate-forming)
Reaction
- L-histidine = urocanate + NH3
Comments:
This enzyme is a member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.23 (tyrosine ammonia-lyase), EC 4.3.1.24 (phenylalanine ammonia-lyase) and EC 4.3.1.25 (phenylalanine/tyrosine ammonia-lyase). The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO), which is common to this family [4]. This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine [5]. This enzyme catalyses the first step in the degradation of histidine and the product, urocanic acid, is further metabolized to glutamate [2,3].
Links to other databases
Enzymes and pathways:
NC-IUBMB
,
BRENDA
,
DIAGRAM
,
ExplorEnz
,
ENZYME@ExPASy
,
KEGG
,
MetaCyc
,
NIST 74
,
UniPathway
Protein domains and families:
PROSITE:PDOC00424
Gene Ontology:
GO:0004397
CAS Registry Number:
9013-75-6
References
-
Deamination of histidine to form urocanic acid in liver.J. Biol. Chem. 201 : 775-784 (1953). [PMID: 13061415]
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Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family.Chem. Biol. 13 : 1317-1326 (2006). [PMID: 17185227]
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Friedel-Crafts-type mechanism for the enzymatic elimination of ammonia from histidine and phenylalanine.Angew. Chem. Int. Ed. Engl. 44 : 3668-3688 (2005). [PMID: 15906398]
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Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases.Chem. Biol. 13 : 1327-1338 (2006). [PMID: 17185228]
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Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile.Biochemistry 38 : 5355-5361 (1999). [PMID: 10220322]
[EC 4.3.1.3 created 1961, modified 2008]