HNMT transfers CH3 group from AdoMet to Hist

Stable Identifier
R-HSA-175993
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
Histamine is deactivated by N-methylation
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Histamine (Hist) plays important biological roles in cell-to-cell communication via by binding to histamine receptors and its local action is terminated primarily by methylation. Histamine is inactivated principally by two enzymes: histamine N-methyltransferase (HNMT) and diamine oxidase. HNMT uses the methyl donor AdoMet, methylates Hist to form methylhistamine (MetHist) (Yamauchi et al. 1994). The common polymorphism T105I correlates with high (T) or low (I) activity phenotypes (Horton et al. 2001, Rutherford et al. 2008).

Literature References
PubMed ID Title Journal Year
11566133 Two polymorphic forms of human histamine methyltransferase: structural, thermal, and kinetic comparisons

Horton, JR, Sawada, K, Nishibori, M, Zhang, X, Cheng, X

Structure 2001
18154359 The histamine N-methyltransferase T105I polymorphism affects active site structure and dynamics

Rutherford, K, Parson, WW, Daggett, V

Biochemistry 2008
7943261 Structure and function of human histamine N-methyltransferase: critical enzyme in histamine metabolism in airway

Yamauchi, K, Sekizawa, K, Suzuki, H, Nakazawa, H, Ohkawara, Y, Katayose, D, Ohtsu, H, Tamura, G, Shibahara, S, Takemura, M

Am. J. Physiol. 1994
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
histamine N-methyltransferase activity of HNMT [cytosol]
Physical Entity
Activity
Cross References
Rhea
Authored
Reviewed
Created