| EC |
4.3.1.3 |
| Accepted name: |
histidine ammonia-lyase |
| Reaction: |
L-histidine = urocanate + NH3 |
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| Glossary: |
urocanate = (E)-3-(imidazol-4-yl)propenoate |
| Other name(s): |
histidase; histidinase; histidine α-deaminase; L-histidine ammonia-lyase |
| Systematic name: |
L-histidine ammonia-lyase (urocanate-forming) |
| 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: |
BRENDA, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9013-75-6 |
| References: |
| 1. |
Mehler, A.H. and Tabor, H. Deamination of histidine to form urocanic acid in liver. J. Biol. Chem. 201 (1953) 775–784. [PMID: 13061415] |
| 2. |
Watts, K.T., Mijts, B.N., Lee, P.C., Manning, A.J. and Schmidt-Dannert, C. Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family. Chem. Biol. 13 (2006) 1317–1326. [DOI] [PMID: 17185227] |
| 3. |
Poppe, L. and Rétey, J. Friedel-Crafts-type mechanism for the enzymatic elimination of ammonia from histidine and phenylalanine. Angew. Chem. Int. Ed. Engl. 44 (2005) 3668–3688. [DOI] [PMID: 15906398] |
| 4. |
Louie, G.V., Bowman, M.E., Moffitt, M.C., Baiga, T.J., Moore, B.S. and Noel, J.P. Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases. Chem. Biol. 13 (2006) 1327–1338. [DOI] [PMID: 17185228] |
| 5. |
Schwede, T.F., Rétey, J. and Schulz, G.E. Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile. Biochemistry 38 (1999) 5355–5361. [DOI] [PMID: 10220322] |
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| [EC 4.3.1.3 created 1961, modified 2008] |
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