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Histidine ammonia-lyase

From Wikipedia, the free encyclopedia

HAL
Identifiers
AliasesHAL, HIS, HSTD, histidine ammonia-lyase, Histidine ammonia-lyase
External IDsOMIM: 609457 MGI: 96010 HomoloGene: 68229 GeneCards: HAL
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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 MbChr 10: 93.32 – 93.36 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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).

YouTube Encyclopedic

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  • Histidine || Biochemistry
  • Synthesis of histamine in body | histidine to histamine formation | biosynthesis of histamine
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  • Histidinemia (Medical Condition)

Transcription

Function

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

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

Pathology

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

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000084110 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020017 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b "Entrez Gene: histidine ammonia-lyase".
  6. ^ 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.
  7. ^ 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.

Further reading

External links

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


This page was last edited on 22 December 2023, at 02:48
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