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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, yagd protein, s-methylmethionine homocysteine methyltransferase, athmt-2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosylmethionine transmethylase
-
-
-
-
adenosylmethionine:homocysteine methyltransferase
-
-
-
-
AtHMT-1
AtHMT-2
homocysteine methylase
-
-
-
-
homocysteine methyltransferase
-
-
-
-
homocysteine transmethylase
-
-
-
-
L-homocysteine S-methyltransferase
-
-
-
-
methylmethionine:homocysteine methyltransferase
-
-
-
-
S-adenosyl-L-methionine:L-homocysteine methyltransferase
-
-
-
-
S-adenosylmethionine homocysteine transmethylase
-
-
-
-
S-adenosylmethionine-homocysteine transmethylase
-
-
-
-
S-adenosylmethionine:homocysteine methyltransferase
-
-
-
-
S-methylmethionine homocysteine transmethylase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-methyl-L-methionine + L-homocysteine = 2 L-methionine
-
-
-
-
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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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
-
higher affinity for R,S form
-
-
?
S-adenosyl-L-ethionine + L-homocysteine
S-adenosyl-L-homocysteine + L-ethionine
-
-
-
?
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
-
-
-
?
S-adenosyl-L-methionine + DL-selenocysteine
S-adenosyl-L-homocysteine + Se-methyl-DL-selenocysteine
-
-
-
?
S-adenosyl-L-methionine + L-cysteine
S-adenosyl-L-homocysteine + S-methyl-L-cysteine
-
-
-
?
S-adenosyl-L-methionine + L-selenocysteine
S-adenosyl-L-homocysteine + Se-methyl-L-selenocysteine
-
-
-
?
(R,S)-S-adenosyl-L-methionine + L-homocysteine
L-methionine + S-adenosyl-L-homocysteine
-
-
(R,S)-S-adenosyl-L-methionine is preferred over (S,S)-S-adenosyl-L-methionine
-
?
(R,S)-S-adenosyl-L-methionine + L-homocysteine
L-methionine + S-adenosyl-L-homocysteine
-
-
-
-
?
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
-
-
?
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
-
-
?
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
-
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
-
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
-
-
-
?
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
-
-
?
S-methyl-L-methionine + L-homocysteine
?
-
S-methyl-L-methionine more effective methyl donor than S-adenosyl-L-methionine
-
-
?
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
-
-
?
S-methyl-L-methionine + L-homocysteine
?
-
S-methyl-L-methionine more effective methyl donor than S-adenosyl-L-methionine
-
-
?
S-methyl-L-methionine + L-homocysteine
?
-
S-methyl-L-methionine more effective methyl donor than S-adenosyl-L-methionine
-
-
?
S-methyl-L-methionine + L-homocysteine
?
-
S-methyl-L-methionine more effective methyl donor than S-adenosyl-L-methionine
-
-
?
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
-
-
?
additional information
?
-
no activity with D-cysteine, L-cysteine, DL-selenocysteine, glutathione, coenzyme A, sulfide, or thiocyanate
-
-
?
additional information
?
-
no activity with D-cysteine, L-cysteine, DL-selenocysteine, glutathione, coenzyme A, sulfide, or thiocyanate
-
-
?
additional information
?
-
no activity with DL-selenocysteine, glutathione, coenzyme A, sulfide, or thiocyanate
-
-
?
additional information
?
-
no activity with DL-selenocysteine, glutathione, coenzyme A, sulfide, or thiocyanate
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of selenocysteine methyltransferase
-
-
?
additional information
?
-
-
the enzyme also catalyzes the reaction of selenocysteine methyltransferase
-
-
?
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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
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
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
in most tissues, low expression of BHMT coincides with a preferential nuclear localization of the protein
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
prevents accumulation of (R,S)-S-adenosyl methionine (formed by spontaneous racemization)
physiological function
physiological function
Escherichia coli harboring the recombinant HMT1 plasmid shows much higher tolerance to selenate and selenite
physiological function
oxidative stress associated with D-galactosamine (Gal) or buthionine sulfoximine (BSO) treatments induces BHMT translocation from cytoplasm to nucleus, which is prevented by administration of N-acetylcysteine and glutathione ethyl ester, respectively. The hepatic nuclear accumulation induced by Gal associates with reduced nuclear BHMT activity and a trend towards increased protein homocysteinylation
Show AA Sequence and Transmembrane Helices (2746 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
40000
-
SDS-PAGE, 73% sequence identity with the 45 kDa BHMT protein (EC 2.1.1.5)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
?
x * 35150, calculated from sequence, x * 40000, SDS-PAGE, recombinant protein
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y71F/T169Y
mutant designed to mimic the betaine-homocysteine methyltransferase substrate binding pocket, complete loss of activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli, recombinant protein, intein/chitin-binding fusion constructs, pTBY3 vector
-
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
HMT1 transcript amounts in different organs are increased by Na2SeO4 treatment
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Balish, E.; Shapiro, S.K.
Methionine biosynthesis in Escherichia coli: induction and repression of methylmethionine(or adenosylmethionine):homocysteine methyltransferase
Arch. Biochem. Biophys.
119
62-68
1967
Escherichia coli, Escherichia coli Texas M
brenda
Shapiro, S.K.
Adenosylmethionine-homocysteine transmethylase
Biochim. Biophys. Acta
29
405-409
1958
Klebsiella aerogenes, Saccharomyces cerevisiae, Cyberlindnera jadinii, Escherichia coli, Equus caballus, Klebsiella aerogenes NRRL 199
brenda
Shapiro, S.K.; Yphantis, D.A.
Assay of S-methylmethionine and S-adenosylmethionine homocysteine transmethylases
Biochim. Biophys. Acta
36
241-244
1959
Klebsiella aerogenes, Saccharomyces cerevisiae, Escherichia coli, Rattus norvegicus
brenda
Shapiro, S.K.
S-Adenosylmethionine:L-homocysteine S-methyltransferase (Saccharomyces cerevisiae)
Methods Enzymol.
17B
400-405
1971
Klebsiella aerogenes, Saccharomyces cerevisiae, Rattus norvegicus
-
brenda
Nakamura, K.D.; Schlenk, F.
The activity of adenosyl-D-methionine and adenosyl-2-methylmethionine in transmethylations
Arch. Biochem. Biophys.
177
170-175
1976
Saccharomyces cerevisiae
brenda
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Arabidopsis thaliana (Q9M1W4), Arabidopsis thaliana (Q9SDL7)
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Saccharomyces cerevisiae
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Saccharomyces cerevisiae
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Mudd, S.H.; Datko, A.H.
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Lemna aequinoctialis
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Brassica oleracea (A4ZGQ8)
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Szegedi, S.S.; Castro, C.C.; Koutmos, M.; Garrow, T.A.
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Homo sapiens
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Thanbichler, M.; Neuhierl, B.; Bck A.
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Escherichia coli (Q47690), Escherichia coli
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Neuhierl, B.; Thanbichler, M.; Lottspeich, F.; Bck, A.
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Escherichia coli (Q47690), Escherichia coli
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Grue-Sorensen, G.; Kelstrup, E.; Kjaer, A.; Madsen, J.O.
Diastereospecific, enzymically catalysed transmethylation from S-methyl-L-Lmethionine to L-homocysteine, a naturally occurring process
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Canavalia ensiformis
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Ranocha, P.; McNeil, S.D.; Ziemak, M.J.; Li, C.; Tarczynski, M.C.; Hanson, A.D.
The S-methylmethionine cycle in angiosperms: ubiquity, antiquity and activity
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Arabidopsis thaliana (Q8LAX0)
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Vinci, C.R.; Clarke, S.G.
Homocysteine methyltransferases Mht1 and Sam4 prevent the accumulation of age-damaged (R,S)-AdoMet in the yeast Saccharomyces cerevisiae
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Saccharomyces cerevisiae
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Bradbury, L.M.; Ziemak, M.J.; El Badawi-Sidhu, M.; Fiehn, O.; Hanson, A.D.
Plant-driven repurposing of the ancient S-adenosylmethionine repair enzyme homocysteine S-ethyltransferase
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Escherichia coli
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Li, K.; Li, G.; Bradbury, L.M.; Hanson, A.D.; Bruner, S.D.
Crystal structure of the homocysteine methyltransferase MmuM from Escherichia coli
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Escherichia coli (Q47690), Escherichia coli
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Perez-Miguelsanz, J.; Vallecillo, N.; Garrido, F.; Reytor, E.; Perez-Sala, D.; Pajares, M.A.
Betaine homocysteine S-methyltransferase emerges as a new player of the nuclear methionine cycle
Biochim. Biophys. Acta
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Rattus norvegicus (O09171)
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Wu, L.; Shang, Y.; Liu, T.; Chen, W.; Liu, B.; Zhang, L.; Liu, D.; Zhang, B.; Zhang, H.
Characterization of a selenium-resistance-enhancing homocysteine s-methyltransferase from Aegilops tauschii
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Aegilops tauschii (M8C0H7)
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