Center for Bioinformatics
Oxidoreductases | Transferases | Hydrolases | Lyases | Isomerases | Ligases

Basic Information

Enzyme Number

4.3.1.3

Official Name

histidine ammonia-lyase

Name from literature

histidine ammonia lyase

Pathway from literature

L-histidine degradation

Pathway from KEGG

Amino Acid Metabolism; Histidine metabolism; map00340

Energy Metabolism; Nitrogen metabolism; map00910

Organisms

Rat (10116)

Genome localization

7q13[29301 ],

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].

Rate-limiting Description

"These findings demonstrate that histidine ammonia-lyase is the rate-limiting factor in L-histidine degradation in the rat." (8133)

Regulatory Information

Regulatory type

Detail

phosphorylation;

P21213:from_uniprot:631_Phosphoserine

phosphorylation;

P21213:from_uniprot:635_Phosphoserine

phosphorylation;

P21213:from_uniprot:648_Phosphoserine

Gene ontology

Gene ontology

GO:0006547 (P) histidine metabolic process [Q76N87, Q76N86 ];
GO:0004397 (F) histidine ammonia-lyase activity [Q76N87, Q76N86, P21213 ];
GO:0016211 (F) ammonia ligase activity [P21213 ];
GO:0009058 (P) biosynthetic process [P21213 ];
GO:0005829 (C) cytosol [Q76N87, Q76N86 ];
GO:0005737 (C) cytoplasm [P21213 ];
GO:0006548 (P) histidine catabolic process [P21213 ];

Links

SwissProt

P21213; Q76N86; Q76N87

Entrez Gene

29301



  Copyright 2009, Center for Bioinformatics 
  Last Modified: 2009-03-24  
  Design by Zhao Min