2.1.1.8: histamine N-methyltransferase
This is an abbreviated version!
For detailed information about histamine N-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.8
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2.1.1.8
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diamine
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histaminergic
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metoprine
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thr105ile
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l-histidine
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radioenzymatic
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thioperamide
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tele-methylhistamine
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aminoguanidine
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histamine-induced
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amodiaquine
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s-adenosyl-l-homocysteine
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3hhistamine
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histamine-related
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histamine-degrading
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n-myristoyltransferase
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pentagastrin
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gene-dose
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mepyramine
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pyrilamine
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phenylethanolamine
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r-alpha-methylhistamine
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histaminase
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medicine
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dimaprit
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degradation
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analysis
- 2.1.1.8
-
diamine
-
histaminergic
- metoprine
-
thr105ile
- l-histidine
-
radioenzymatic
- thioperamide
-
tele-methylhistamine
- aminoguanidine
-
histamine-induced
- amodiaquine
- s-adenosyl-l-homocysteine
-
3hhistamine
-
histamine-related
-
histamine-degrading
- n-myristoyltransferase
- pentagastrin
-
gene-dose
-
mepyramine
-
pyrilamine
- phenylethanolamine
-
r-alpha-methylhistamine
- histaminase
- medicine
- dimaprit
- degradation
- analysis
Reaction
Synonyms
histamine 1-methyltransferase, histamine methyltransferase, histamine N-methyltransferase, histamine-methylating enzyme, histamine-N-methyltransferase, HMT, HNMT, imidazole methyltransferase, imidazole N-methyltransferase, imidazolemethyltransferase, methyltransferase, histamine, Ntau-methyltransferase, S-adenosylmethionine-histamine N-methyltransferase
ECTree
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Reaction
Reaction on EC 2.1.1.8 - histamine N-methyltransferase
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2 half-reactions in a ping pong mechanism with the intermediate formation of a methylated enzyme
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S-adenosyl-L-methionine + histamine = S-adenosyl-L-homocysteine + Ntau-methylhistamine
ordered sequential bi bi reaction mechanism with S-adenosylmethionine as the first substrate and histamine as the second substrate, 1-methylhistamine is the first product to leave and S-adenosylhomocysteine the second
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S-adenosyl-L-methionine + histamine = S-adenosyl-L-homocysteine + Ntau-methylhistamine
sequential reaction mechanism
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S-adenosyl-L-methionine + histamine = S-adenosyl-L-homocysteine + Ntau-methylhistamine
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
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