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Information on EC 2.1.1.10 - homocysteine S-methyltransferase
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EC Tree
2.1.1.10 homocysteine S-methyltransferaseIUBMB Comments
The enzyme uses S-adenosyl-L-methionine as methyl donor less actively than S-methyl-L-methionine.
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Word Map
- 2.1.1.10
- methyltetrahydrofolate
- mthfr
-
b12-dependent
- cystathionine
- n5-methyltetrahydrofolate
- methylenetetrahydrofolate
- tetrahydrofolate
-
mete
- selenocysteine
-
methylmalonic
-
2.1.1.13
- se-methylselenocysteine
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
homocysteine methyltransferase, homocysteine s-methyltransferase, athmt-1, homocysteine transmethylase, l-homocysteine s-methyltransferase, s-methylmethionine homocysteine methyltransferase, yagd protein, athmt-2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosylmethionine transmethylase
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-
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adenosylmethionine:homocysteine methyltransferase
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-
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AtHMT-1
AtHMT-2
homocysteine methylase
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-
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homocysteine methyltransferase
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-
-
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homocysteine transmethylase
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L-homocysteine S-methyltransferase
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methylmethionine:homocysteine methyltransferase
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S-adenosyl-L-methionine:L-homocysteine methyltransferase
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S-adenosylmethionine homocysteine transmethylase
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S-adenosylmethionine-homocysteine transmethylase
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S-adenosylmethionine:homocysteine methyltransferase
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S-methylmethionine homocysteine transmethylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-methyl-L-methionine + L-homocysteine = 2 L-methionine
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-
-
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S-methyl-L-methionine + L-homocysteine = 2 L-methionine
high homology to betaine-homocysteine methyltransferase (BHMT, EC 2.1.1.5), betaine is not a substrate for BHMT-2 but high activity with S-methyl-L-methionine
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
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-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:L-homocysteine S-methyltransferase
The enzyme uses S-adenosyl-L-methionine as methyl donor less actively than S-methyl-L-methionine.
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CAS REGISTRY NUMBER
COMMENTARY
9012-40-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S,S)-S-adenosyl-L-methionine + L-homocysteine
L-methionine + S-adenosyl-L-homocysteine
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higher affinity for R,S form
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-
?
S-adenosyl-L-ethionine + L-homocysteine
S-adenosyl-L-homocysteine + L-ethionine
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-
-
?
S-adenosyl-L-methionine + DL-cysteine
S-adenosyl-L-homocysteine + S-methyl-DL-cysteine
-
-
-
?
S-adenosyl-L-methionine + DL-homocysteine
L-methionine + S-adenosyl-L-homocysteine
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-
-
?
S-adenosyl-L-methionine + DL-selenocysteine
S-adenosyl-L-homocysteine + Se-methyl-DL-selenocysteine
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-
-
?
S-adenosyl-L-methionine + L-cysteine
S-adenosyl-L-homocysteine + S-methyl-L-cysteine
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-
-
?
S-adenosyl-L-methionine + L-selenocysteine
S-adenosyl-L-homocysteine + Se-methyl-L-selenocysteine
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-
-
?
(R,S)-S-adenosyl-L-methionine + L-homocysteine
L-methionine + S-adenosyl-L-homocysteine
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-
(R,S)-S-adenosyl-L-methionine is preferred over (S,S)-S-adenosyl-L-methionine
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?
(R,S)-S-adenosyl-L-methionine + L-homocysteine
L-methionine + S-adenosyl-L-homocysteine
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-
-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
the enzyme uses S-methyl-L-methionine and S-adenosyl-L-methionine as methyl donor in vivo
-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
the Km-value for S-adenosyl-L-methionine is higher than for S-methyl-L-methionine and the Vmax value is lower
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-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
the Km-value for S-adenosyl-L-methionine is higher than for S-methyl-L-methionine and the Vmax value is lower
-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
-
enzymic preference of the pro-(R)-methyl group to the extent of 94% or more
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-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
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-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
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-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
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-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
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-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
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-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
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-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
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biosynthesis of methionine
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?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
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biosynthesis of methionine
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?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
-
biosynthesis of methionine
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?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
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-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
-
biosynthesis of methionine
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?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
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-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
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-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
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-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
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-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
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-
-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
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-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
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-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
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-
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?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
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-
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?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
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-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
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-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
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-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
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-
-
?
S-methyl-L-methionine + L-homocysteine
2 L-methionine
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-
-
?
S-methyl-L-methionine + L-homocysteine
2 L-methionine
synthesis of L-methionine from homocysteine
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-
?
S-methyl-L-methionine + L-homocysteine
2 L-methionine
the enzyme uses S-methyl-L-methionine and S-adenosyl-L-methionine as methyl donor in vivo
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-
?
S-methyl-L-methionine + L-homocysteine
?
-
S-methyl-L-methionine more effective methyl donor than S-adenosyl-L-methionine
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-
?
S-methyl-L-methionine + L-homocysteine
?
-
high homology to betaine-homocysteine methyltransferase (BHMT, EC 2.1.1.5), betaine is not a substrate for BHMT-2 but high activity with S-methyl-L-methionine
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?
S-methyl-L-methionine + L-homocysteine
?
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S-methyl-L-methionine more effective methyl donor than S-adenosyl-L-methionine
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?
S-methyl-L-methionine + L-homocysteine
?
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S-methyl-L-methionine more effective methyl donor than S-adenosyl-L-methionine
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?
S-methyl-L-methionine + L-homocysteine
?
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S-methyl-L-methionine more effective methyl donor than S-adenosyl-L-methionine
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?
S-methyl-L-methionine + L-homocysteine
L-methionine
metabolism of S-methylmethionine requires a functional YagD protein, since inactivation of the yagD gene abolishes the capacity to grow on S-methylmethionine
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?
additional information
?
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no activity with D-cysteine, L-cysteine, DL-selenocysteine, glutathione, coenzyme A, sulfide, or thiocyanate
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-
?
additional information
?
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no activity with D-cysteine, L-cysteine, DL-selenocysteine, glutathione, coenzyme A, sulfide, or thiocyanate
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?
additional information
?
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no activity with DL-selenocysteine, glutathione, coenzyme A, sulfide, or thiocyanate
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?
additional information
?
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no activity with DL-selenocysteine, glutathione, coenzyme A, sulfide, or thiocyanate
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-
?
additional information
?
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the enzyme also catalyzes the reaction of selenocysteine methyltransferase
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-
?
additional information
?
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-
the enzyme also catalyzes the reaction of selenocysteine methyltransferase
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-methyl-L-methionine + L-homocysteine
L-methionine
metabolism of S-methylmethionine requires a functional YagD protein, since inactivation of the yagD gene abolishes the capacity to grow on S-methylmethionine
-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
the enzyme uses S-methyl-L-methionine and S-adenosyl-L-methionine as methyl donor in vivo
-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
-
biosynthesis of methionine
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
-
biosynthesis of methionine
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
-
biosynthesis of methionine
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
-
biosynthesis of methionine
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
-
-
-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
-
-
-
?
S-methyl-L-methionine + L-homocysteine
2 L-methionine
synthesis of L-methionine from homocysteine
-
-
?
S-methyl-L-methionine + L-homocysteine
2 L-methionine
the enzyme uses S-methyl-L-methionine and S-adenosyl-L-methionine as methyl donor in vivo
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
Zn2+
additional information
Zn2+
required. The metallated crystal form has residues C229, C295 and C296 coordinated to a Zn2+ center. the coordination of homocysteine to metal with a distance of 2.8 A contributes to near-ideal Zn2+-centered tetrahedron geometry
additional information
contains a zinc-binding motif, no stimulation by 0.1 or 1 mM Zn2+
additional information
contains a zinc-binding motif, no stimulation by 0.1 or 1 mM Zn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
-
complete inhibition, reversible by addition of excess of Zn2+
S-adenosyl-L-methionine
-
weak inhibitor of, does not inhibit BHMT (EC 2.1.1.5), not inhibited by betaine
additional information
no product inhibition by L-methionine below 0.5 mM, no inhibition by EDTA
-
additional information
no product inhibition by L-methionine below 0.5 mM, no inhibition by EDTA
-
additional information
-
relative inhibition of human BHMT (EC 2.1.1.5) and human BHMT-2 activities by methyl donor substrates determined
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
increases activity at low substrate concentrations
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
homocysteine s-methyltransferase deficiency
[N5-methyltetrahydrofolate: homocysteine methyltransferase deficiency]
Hyperglycinemia, Nonketotic
Novel mutations in the P-protein (glycine decarboxylase) gene in patients with glycine encephalopathy (non-ketotic hyperglycinemia).
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.018
L-homocysteine
pH 7.5, 30°C, cosubstrate: S-adenosyl-L-methionine
0.027
L-homocysteine
pH 7.5, 25°C, cosubstrate: S-adenosyl-L-methionine
0.03
L-homocysteine
pH 7.5, 25°C, cosubstrate: S-methyl-L-methionine
0.035
L-homocysteine
pH 7.5, 30°C, cosubstrate: S-methyl-L-methionine
0.045
L-homocysteine
pH 6, 30°C, cosubstrate: S-adenosyl-L-methionine
0.067
L-homocysteine
pH 7.5, 30°C, cosubstrate: S-adenosyl-L-methionine
0.077
L-homocysteine
pH 7.5, 30°C, cosubstrate: S-methyl-L-methionine
0.94
S-methyl-L-methionine
-
final concentrations of S-methyl-L-methionine ranging from 0.1 mM to 9 mM, lower value than obtained for BHMT (EC 2.1.1.5)
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.38
L-homocysteine
pH 6, 30°C, cosubstrate: S-adenosyl-L-methionine
additional information
additional information
-
similar turnover number like betaine-homocysteine methyltransferase (BHMT, EC 2.1.1.5)
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
structural comparison and enzymatic properties of purified human betaine-homocysteine methyltransferase (BHMT, EC 2.1.1.5) and human betaine-homocysteine methyltransferase-2 (BHMT-2) determined, methylation capacities of homocysteine analyzed, S-adenosyl-L-methionine-dependent methylation of homocysteine predicted mostly occurs via BHMT-2 in vivo
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 35
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
