Publication: Substrate specificity and heterogeneity of N-methyltransferases
Issued Date
1972-04-28
Resource Type
ISSN
10902104
0006291X
0006291X
Other identifier(s)
2-s2.0-0015526796
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Mahidol University
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SCOPUS
Bibliographic Citation
Biochemical and Biophysical Research Communications. Vol.47, No.2 (1972), 301-308
Suggested Citation
Amnuay Thithapandha Substrate specificity and heterogeneity of N-methyltransferases. Biochemical and Biophysical Research Communications. Vol.47, No.2 (1972), 301-308. doi:10.1016/0006-291X(72)90712-7 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/10000
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Title
Substrate specificity and heterogeneity of N-methyltransferases
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Abstract
Histamine N-methyltransferase ( EC. 2.1.1.8 ) from cat intestine and guinea pig brain was compared with indoleamine N-methyltransferase from rabbit lung and chick brain. Histamine N-methyltransferase, regardless of its source, methylated specifically histamine and not other imidazoles or aromatic amines. In contrast, indoleamine N-methyltransferase from rabbit lung had different substrate specificity from that of chick brain enzyme. The best substrate for lung indoleamine N-methyltransferase was N-methyltryptamine whereas serotonin was the best substrate for the chick brain enzyme. Both histamine N-methyltransferase and indoleamine N-methyltransferase appeared to occur in these species in multiple forms. They had different kinetic parameters, different pH optimum values, displayed different response towards inhibitors, and had different heat stability. © 1972.