Histamine N-methyltransferase
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| histamine N-methyltransferase | |||||||
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| Crystallographic structure of human histamine N-methyltransferase | |||||||
| Identifiers | |||||||
| EC number | 2.1.1.8 | ||||||
| CAS number | 9029-80-5 | ||||||
| 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 / EGO | ||||||
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| Identifiers | |
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| Symbol | HNMT |
| Entrez | 3176 |
| HUGO | 5028 |
| OMIM | 605238 |
| RefSeq | NM_006895 |
| UniProt | P50135 |
| Other data | |
| Locus | Chr. 2 q22.1 |
Histamine N-methyltransferase (HMT, HNMT) is one of two enzymes involved in the metabolism of histamine. The other being diamine oxidase. Histamine N-methyltransferase catalyzes the methylation of histamine in the presence of S-adenosylmethionine (SAM) forming N-methylhistamine. HMT is present in most body tissues but is not present in fluid. Histamine N-methyltransferase is encoded by a single gene which has been mapped to chromosome 2.
[edit] References
- Brown DD, Tomchick R, Axelrod J (November 1959). "The distribution and properties of a histamine-methylating enzyme". J. Biol. Chem. 234: 2948–50. PMID 13804910.
[edit] External links
- MeSH Histamine+N-Methyltransferase
- PDB [1] Horton, J.R., Sawada, K., Nishibori, M., Zhang, X., Cheng, X. (August 2002) "Crystal Structure Analysis of Human Histamine Methyltransferase (Thr105 Polymorphic Variant) Complexed with AdoHcy and Histamine"
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