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(Top) 1 Function 2 Pathology 3 See also 4 References 5 Further reading 6 External links

Histidine ammonia-lyase

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HAL

Identifiers

Aliases

HAL, HIS, HSTD, histidine ammonia-lyase, Histidine ammonia-lyase

External IDs

OMIM: 609457; MGI: 96010; HomoloGene: 68229; GeneCards: HAL; OMA:HAL - orthologs

Gene location (Human)

Chr.	Chromosome 12 (human)^[1]

Band	12q23.1	Start	95,972,662 bp^[1]
Band	12q23.1	End	95,996,365 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 10 (mouse)^[2]

Band	10 C2\|10 48.49 cM	Start	93,324,630 bp^[2]
Band	10 C2\|10 48.49 cM	End	93,355,166 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

right lobe of liver

human penis

skin of thigh

vulva

blood

oocyte

skin of arm

monocyte

secondary oocyte

skin of abdomen

Top expressed in

morula

skin of external ear

left lobe of liver

lip

skin of back

lumbar spinal ganglion

calvaria

belly cord

spermatid

granulocyte

More reference expression data

BioGPS

n/a

Gene ontology
Molecular function	catalytic activity lyase activity ammonia-lyase activity histidine ammonia-lyase activity
Cellular component	cytosol cytoplasm
Biological process	histidine metabolic process histidine catabolic process to glutamate and formate histidine catabolic process to glutamate and formamide histidine catabolic process
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


3034


15109

Ensembl


ENSG00000084110


ENSMUSG00000020017

UniProt


P42357


P35492

RefSeq (mRNA)


NM_001258333 NM_001258334 NM_002108


NM_010401

RefSeq (protein)


NP_001245262 NP_001245263 NP_002099


NP_034531

Location (UCSC)

Chr 12: 95.97 – 96 Mb

Chr 10: 93.32 – 93.36 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

histidine ammonia-lyase

Histidine ammonia-lyase homotetramer, Pseudomonas putida

Identifiers

Databases

PDB structures

Search
PMC	articles
PubMed	articles
NCBI	proteins

Histidine ammonia-lyase (EC 4.3.1.3, histidase, histidinase) is an enzyme that in humans is encoded by the HAL gene.^[5]^[6] It converts histidine into ammonia and urocanic acid. Its systematic name is L-histidine ammonia-lyase (urocanate-forming).

Function[edit]

Histidine ammonia-lyase is a cytosolic enzyme catalyzing the first reaction in histidine catabolism, the nonoxidative deaminationofL-histidine to trans-urocanic acid.^[5] The reaction is catalyzed by 3,5-dihydro-5-methyldiene-4H-imidazol-4-one (MIO), an electrophilic cofactor which is formed autocatalytically by cyclization of the protein backbone of the enzyme.^[7]

Proposed autocatalytic formation of MIO cofactor in another enzyme, phenylalanine ammonia-lyase, from the tripeptide Ala-Ser-Gly by two water elimination steps.

Pathology[edit]

Mutations in the gene for histidase are associated with histidinemia and urocanic aciduria.

References[edit]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000084110 – Ensembl, May 2017

^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000020017 – Ensembl, May 2017

^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

^ ^a ^b "Entrez Gene: histidine ammonia-lyase".

^ Suchi M, Sano H, Mizuno H, Wada Y (September 1995). "Molecular cloning and structural characterization of the human histidase gene (HAL)". Genomics. 29 (1): 98–104. doi:10.1006/geno.1995.1219. PMID 8530107.

^ Schwede TF, Rétey J, Schulz GE (Apr 27, 1999). "Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile". Biochemistry. 38 (17): 5355–5361. doi:10.1021/bi982929q. PMID 10220322.

External links[edit]

Histidine+Ammonia-Lyase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

This lyase article is a stub. You can help Wikipedia by expanding it.

Metabolism: Protein metabolism, synthesis and catabolism enzymes

Essential amino acids are in Capitals

K→acetyl-CoA

LYSINE→	Saccharopine dehydrogenase Glutaryl-CoA dehydrogenase
LEUCINE→	3-Hydroxybutyryl-CoA dehydrogenase Branched-chain amino acid aminotransferase Branched-chain alpha-keto acid dehydrogenase complex Enoyl-CoA hydratase HMG-CoA lyase HMG-CoA reductase Isovaleryl coenzyme A dehydrogenase α-Ketoisocaproate dioxygenase Leucine 2,3-aminomutase Methylcrotonyl-CoA carboxylase Methylglutaconyl-CoA hydratase (See Template:Leucine metabolism in humans – this diagram does not include the pathway for β-leucine synthesis via leucine 2,3-aminomutase)
TRYPTOPHAN→	Indoleamine 2,3-dioxygenase/Tryptophan 2,3-dioxygenase Arylformamidase Kynureninase 3-hydroxyanthranilate oxidase Aminocarboxymuconate-semialdehyde decarboxylase Aminomuconate-semialdehyde dehydrogenase
PHENYLALANINE→tyrosine→	(see below)

G→pyruvate
→citrate

glycine→serine→	Serine hydroxymethyltransferase Serine dehydratase glycine→creatine: Guanidinoacetate N-methyltransferase Creatine kinase
alanine→	Alanine transaminase
cysteine→	D-cysteine desulfhydrase
threonine→	L-threonine dehydrogenase

G→glutamate→
α-ketoglutarate

HISTIDINE→	Histidine ammonia-lyase Urocanate hydratase Formiminotransferase cyclodeaminase
proline→	Proline oxidase Pyrroline-5-carboxylate reductase 1-Pyrroline-5-carboxylate dehydrogenase/ALDH4A1 PYCR1
arginine→	Ornithine aminotransferase Ornithine decarboxylase Agmatinase
→alpha-ketoglutarate→TCA	Glutamate dehydrogenase
Other	cysteine+glutamate→glutathione: Gamma-glutamylcysteine synthetase Glutathione synthetase Gamma-glutamyl transpeptidase glutamate→glutamine: Glutamine synthetase Glutaminase

G→propionyl-CoA→
succinyl-CoA

VALINE→	Branched-chain amino acid aminotransferase Branched-chain alpha-keto acid dehydrogenase complex Enoyl-CoA hydratase 3-hydroxyisobutyryl-CoA hydrolase 3-hydroxyisobutyrate dehydrogenase Methylmalonate semialdehyde dehydrogenase
ISOLEUCINE→	Branched-chain amino acid aminotransferase Branched-chain alpha-keto acid dehydrogenase complex 3-hydroxy-2-methylbutyryl-CoA dehydrogenase
METHIONINE→	generation of homocysteine: Methionine adenosyltransferase Adenosylhomocysteinase regeneration of methionine: Methionine synthase/Homocysteine methyltransferase Betaine-homocysteine methyltransferase conversion to cysteine: Cystathionine beta synthase Cystathionine gamma-lyase
THREONINE→	Threonine aldolase
→succinyl-CoA→TCA	Propionyl-CoA carboxylase Methylmalonyl CoA epimerase Methylmalonyl-CoA mutase

G→fumarate

PHENYLALANINE→tyrosine→

tyrosine→melanin: Tyrosinase

G→oxaloacetate

asparagine→aspartate→

Carbon–nitrogen lyases (EC 4.3)

4.3.1: ammonia-lyases

4.3.2: amidine-lyases

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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