From Wikipedia, the free encyclopedia
(Redirected from Histidase)
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
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 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
EC no. 4.3.1.3
CAS no. 9013-75-6
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
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

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-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

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

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000084110Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020017Ensembl, 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.

From Wikipedia, the free encyclopedia
(Redirected from Histidase)
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
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 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
EC no. 4.3.1.3
CAS no. 9013-75-6
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
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

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-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

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

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000084110Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020017Ensembl, 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.


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