Work

Purification and kinetic properties of ox brain histamine N-methyltransferase

Year: 1986

Type: article

Abstract: Histamine N-methyltransferase (EC 2.1.1.8) was purified 1100-fold from ox brain. The native enzyme has an Mr of 34800 +/- 2400 as measured by gel filtration on Sephadex G-100. The enzyme is highly specific for histamine. It does not methylate noradrenaline, adrenaline, DL-3,4-dihydroxymandelic acid, 3,4-dihydroxyphenylacetic acid, 3-hydroxytyramine or imidazole-4-acetic acid. Unlike the enzyme from rat and mouse brain, ox brain histamine N-methyltransferase did not exhibit substrate inhibition by histamine. Initial rate and product inhibition studies were consistent with an ordered steady-state mechanism with S-adenosylmethionine being the first substrate to bind to the enzyme and N-methylhistamine being the first product to dissociate.

Source: Biochemical Journal

DOI: 10.1042/bj2330669

Authors: W L Gitomer, K F Tipton

Institutions: Trinity College Dublin, National Institute on Alcohol Abuse and Alcoholism

Language: English

Topic: Polyamine Metabolism and Applications

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funders: Medical Research Council, Corpus Christi College, University of Cambridge

OpenAlex ID: W613696394