2.1.1.5: betaine-homocysteine S-methyltransferase
This is an abbreviated version!
For detailed information about betaine-homocysteine S-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.5
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2.1.1.5
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cystathionine
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s-adenosylmethionine
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choline
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folate
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remethylation
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hyperhomocysteinemia
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s-adenosylhomocysteine
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adenosyltransferase
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n-methyltransferase
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one-carbon
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beta-synthase
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dimethylglycine
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transsulfuration
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methylenetetrahydrofolate
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5-methyltetrahydrofolate-homocysteine
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transmethylation
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medicine
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mthfd1
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guanidinoacetate
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homocysteine-induced
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folate-dependent
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homocystinuria
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5-methyltetrahydrofolate
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transcobalamin
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b-vitamins
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slc19a1
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hypotaurine
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molecular biology
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analysis
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nutrition
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food industry
- 2.1.1.5
- cystathionine
- s-adenosylmethionine
- choline
- folate
-
remethylation
- hyperhomocysteinemia
- s-adenosylhomocysteine
-
adenosyltransferase
- n-methyltransferase
-
one-carbon
- beta-synthase
- dimethylglycine
-
transsulfuration
- methylenetetrahydrofolate
-
5-methyltetrahydrofolate-homocysteine
-
transmethylation
- medicine
- mthfd1
- guanidinoacetate
-
homocysteine-induced
-
folate-dependent
- homocystinuria
- 5-methyltetrahydrofolate
-
transcobalamin
-
b-vitamins
-
slc19a1
- hypotaurine
- molecular biology
- analysis
- nutrition
- food industry
Reaction
Synonyms
betaine homocysteine methyltransferase, betaine homocysteine methyltransferase-1, betaine homocysteine S-methyltransferase, betaine-homocysteine methyltransferase, betaine-homocysteine S-methyltransferase, betaine-homocysteine S-methyltransferase 2, betaine-homocysteine S-methyltransferase-2, betaine-homocysteine transmethylase, betaine:homocysteine methyltransferase, betaine:homocysteine S-methyltransferase, BHMT, BHMT-1, BHMT-2, BHMT1, BHMT2, methyltransferase, betaine-homocysteine
ECTree
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Metals Ions
Metals Ions on EC 2.1.1.5 - betaine-homocysteine S-methyltransferase
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K+
Km value around 0.1 mM. The presence of potassium ions lowers the apparent KM of the enzyme for homocysteine, but it does not affect the apparent KM for betaine or the apparent kcat for either substrate
Zinc
wild-type enzyme contains zinc. Mutant enzymes H338A, R346A, W352A, R361A, P362A, Y363A, N364A, P365A maintain normal or near-normal ability to bind zinc
Zn
Zn2+
Zn2+
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wild-type enzyme contains catalytic active zinc which is bound by three thiolates and one hydroxyl group. Long-term exposure of BHMT to reducing agent-free buffer results in the slow, irreversible loss of its catalytic Zn and a corresponding loss of activity