Title : Two polymorphic forms of human histamine methyltransferase: structural, thermal, and kinetic comparisons.

Pub. Date : 2001 Sep

PMID : 11566133






1 Functional Relationships(s)
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1 CONCLUSIONS: HNMT has a 2 domain structure including a consensus AdoMet binding domain, where the residue 105 is located on the surface, consistent with the kinetic data that the polymorphism does not affect overall protein stability at physiological temperatures but lowers K(M) values for AdoMet and histamine. S-Adenosylmethionine histamine N-methyltransferase Homo sapiens