Alpha-methylhistamine methylation by histamine methyltransferase

Lindsay B. Hough; J. K. Khandelwal; Thomas W. Mittag

doi:10.1007/BF02004701

Alpha-methylhistamine methylation by histamine methyltransferase

Lindsay B. Hough
, J. K. Khandelwal
, Thomas W. Mittag

Research output: Contribution to journal › Article › peer-review

17 Scopus citations

Abstract

Enzymatic methylation of histamine and analogues by histamine methyltransferase (HMT) was studied. Incubation of histamine or alpha-methylhistamine with HMT and S-adenosylmethionine was shown by GC-MS to yield tele-methyl and alpha-methyl-tele-methyl-histamine, respectively. Kinetic analysis of the reactions indicated that both substrates exhibited equivalent V_max values, but that histamine's K_m was ten-fold lower than that of alphamethylhistamine. these results indicate that alphamethylhistamine can be methylated as effectively as histamine, and may be a useful tool in further studies of HMT.

Original language	English
Pages (from-to)	425-428
Number of pages	4
Journal	Agents and Actions
Volume	11
Issue number	5
DOIs	https://doi.org/10.1007/BF02004701
State	Published - Nov 1981
Externally published	Yes

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title = "Alpha-methylhistamine methylation by histamine methyltransferase",

abstract = "Enzymatic methylation of histamine and analogues by histamine methyltransferase (HMT) was studied. Incubation of histamine or alpha-methylhistamine with HMT and S-adenosylmethionine was shown by GC-MS to yield tele-methyl and alpha-methyl-tele-methyl-histamine, respectively. Kinetic analysis of the reactions indicated that both substrates exhibited equivalent Vmax values, but that histamine's Km was ten-fold lower than that of alphamethylhistamine. these results indicate that alphamethylhistamine can be methylated as effectively as histamine, and may be a useful tool in further studies of HMT.",

author = "Hough, \{Lindsay B.\} and Khandelwal, \{J. K.\} and Mittag, \{Thomas W.\}",

year = "1981",

month = nov,

doi = "10.1007/BF02004701",

language = "English",

volume = "11",

pages = "425--428",

journal = "Agents and Actions",

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T1 - Alpha-methylhistamine methylation by histamine methyltransferase

AU - Hough, Lindsay B.

AU - Khandelwal, J. K.

AU - Mittag, Thomas W.

PY - 1981/11

Y1 - 1981/11

N2 - Enzymatic methylation of histamine and analogues by histamine methyltransferase (HMT) was studied. Incubation of histamine or alpha-methylhistamine with HMT and S-adenosylmethionine was shown by GC-MS to yield tele-methyl and alpha-methyl-tele-methyl-histamine, respectively. Kinetic analysis of the reactions indicated that both substrates exhibited equivalent Vmax values, but that histamine's Km was ten-fold lower than that of alphamethylhistamine. these results indicate that alphamethylhistamine can be methylated as effectively as histamine, and may be a useful tool in further studies of HMT.

AB - Enzymatic methylation of histamine and analogues by histamine methyltransferase (HMT) was studied. Incubation of histamine or alpha-methylhistamine with HMT and S-adenosylmethionine was shown by GC-MS to yield tele-methyl and alpha-methyl-tele-methyl-histamine, respectively. Kinetic analysis of the reactions indicated that both substrates exhibited equivalent Vmax values, but that histamine's Km was ten-fold lower than that of alphamethylhistamine. these results indicate that alphamethylhistamine can be methylated as effectively as histamine, and may be a useful tool in further studies of HMT.

UR - https://www.scopus.com/pages/publications/0019772616

U2 - 10.1007/BF02004701

DO - 10.1007/BF02004701

M3 - Article

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SN - 0065-4299

VL - 11

SP - 425

EP - 428

JO - Agents and Actions

JF - Agents and Actions

IS - 5

ER -

Alpha-methylhistamine methylation by histamine methyltransferase

Abstract

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