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Information on EC 2.1.1.10 - homocysteine S-methyltransferase and Organism(s) Escherichia coli and UniProt Accession Q47690

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EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.10 homocysteine S-methyltransferase
IUBMB Comments
The enzyme uses S-adenosyl-L-methionine as methyl donor less actively than S-methyl-L-methionine.
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This record set is specific for:
Escherichia coli
UNIPROT: Q47690
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The taxonomic range for the selected organisms is: Escherichia coli
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S-methylmethionine: homocysteine methyltransferase
-
YagD protein
-
adenosylmethionine transmethylase
-
-
-
-
adenosylmethionine:homocysteine methyltransferase
-
-
-
-
homocysteine methylase
-
-
-
-
homocysteine methyltransferase
-
-
-
-
homocysteine transmethylase
-
-
-
-
L-homocysteine S-methyltransferase
-
-
-
-
methylmethionine:homocysteine methyltransferase
-
-
-
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S-adenosyl-L-methionine:L-homocysteine methyltransferase
-
-
-
-
S-adenosylmethionine homocysteine transmethylase
-
-
-
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S-adenosylmethionine-homocysteine transmethylase
-
-
-
-
S-adenosylmethionine:homocysteine methyltransferase
-
-
-
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S-methylmethionine homocysteine transmethylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9012-40-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
show the reaction diagram
-
-
-
?
S-methyl-L-methionine + L-homocysteine
2 L-methionine
show the reaction diagram
-
-
-
?
S-methyl-L-methionine + L-homocysteine
L-methionine
show the reaction diagram
S-methyl-L-methionine + selenohomocysteine
?
show the reaction diagram
-
-
-
?
(R,S)-S-adenosyl-L-methionine + L-homocysteine
L-methionine + S-adenosyl-L-homocysteine
show the reaction diagram
-
-
(R,S)-S-adenosyl-L-methionine is preferred over (S,S)-S-adenosyl-L-methionine
-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
show the reaction diagram
S-methyl-L-methionine + L-homocysteine
2 L-methionine
show the reaction diagram
-
-
-
-
?
S-methyl-L-methionine + L-homocysteine
?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-methyl-L-methionine + L-homocysteine
2 L-methionine
show the reaction diagram
-
-
-
?
S-methyl-L-methionine + L-homocysteine
L-methionine
show the reaction diagram
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
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-methionine
product inhibition above 0.5 mM
S-adenosyl-L-methionine
product inhibition above 0.25 mM
L-methionine
-
product inhibition
S-adenosyl-L-homocysteine
-
product inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cysteine
-
-
homocysteine
-
induces reaction
homoserine
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S-[(2R)-2-amino-2-carboxyethyl]-L-homocysteine
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.045
L-homocysteine
pH 6, 30°C, cosubstrate: S-adenosyl-L-methionine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.38
L-homocysteine
pH 6, 30°C, cosubstrate: S-adenosyl-L-methionine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.012
-
S-methyl-L-methionine as methyl donor
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32500
1 * 32500, calculated from sequence
34000
gel filtration
34490
1 * 34490, calculated, 1 * 35000, SDS-PAGE
35000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in oxidized, apo, and metallated form, to 1.8-1.9 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y71F/T169Y
mutant designed to mimic the betaine-homocysteine methyltransferase substrate binding pocket, complete loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
Manually annotated by BRENDA team
Shapiro, S.K.
Adenosylmethionine-homocysteine transmethylase
Biochim. Biophys. Acta
29
405-409
1958
Cyberlindnera jadinii, Equus caballus, Escherichia coli, Klebsiella aerogenes, Klebsiella aerogenes NRRL 199, Saccharomyces cerevisiae
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Thanbichler, M.; Neuhierl, B.; Bck A.
S-Methylmethionine metabolism in Escherichia coli
J. Bacteriol.
181
662-665
1999
Escherichia coli (Q47690), Escherichia coli
Manually annotated by BRENDA team
Neuhierl, B.; Thanbichler, M.; Lottspeich, F.; Bck, A.
A family of S-methylmethionine-dependent thiol/selenol methyltransferases. Role in selenium tolerance and evolutionary relation
J. Biol. Chem.
274
5407-5414
1999
Escherichia coli (Q47690), Escherichia coli
Manually annotated by BRENDA team
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
Biochem. J.
463
279-286
2014
Escherichia coli
Manually annotated by BRENDA team
Li, K.; Li, G.; Bradbury, L.M.; Hanson, A.D.; Bruner, S.D.
Crystal structure of the homocysteine methyltransferase MmuM from Escherichia coli
Biochem. J.
473
277-284
2015
Escherichia coli (Q47690), Escherichia coli
Manually annotated by BRENDA team