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Information on EC 2.1.1.10 - homocysteine S-methyltransferase and Organism(s) Homo sapiens

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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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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
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The taxonomic range for the selected organisms is: Homo sapiens
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
adenosylmethionine transmethylase
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-
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adenosylmethionine:homocysteine methyltransferase
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-
-
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BHMT-2
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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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-
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methylmethionine:homocysteine methyltransferase
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-
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S-adenosyl-L-methionine:L-homocysteine methyltransferase
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S-adenosylmethionine homocysteine transmethylase
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-
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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 hide
ORGANISM
UNIPROT
LITERATURE
S-methyl-L-methionine + L-homocysteine = 2 L-methionine
show the reaction diagram
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 hide
LITERATURE
methyl group transfer
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
9012-40-2
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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
?
show the reaction diagram
-
low activity
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-
?
S-methyl-L-methionine + L-homocysteine
?
show the reaction diagram
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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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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
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required for activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-methionine
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stronger inhibitor of BHMT-2 than of BHMT (EC 2.1.1.5)
S-adenosyl-L-methionine
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weak inhibitor of, does not inhibit BHMT (EC 2.1.1.5), not inhibited by betaine
additional information
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relative inhibition of human BHMT (EC 2.1.1.5) and human BHMT-2 activities by methyl donor substrates determined
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.94
S-methyl-L-methionine
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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)
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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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 hide
LITERATURE
additional information
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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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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activity assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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tissue extracts, activities measured in
Manually annotated by BRENDA team
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tissue extracts, activities measured in
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BHMT2_HUMAN
363
0
40354
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
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SDS-PAGE, 73% sequence identity with the 45 kDa BHMT protein (EC 2.1.1.5)
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
high concentrations of glycerol (40%, v/v) greatly stabilized activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
gel filtration, recombinant protein
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli, recombinant protein, intein/chitin-binding fusion constructs, pTBY3 vector
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Szegedi, S.S.; Castro, C.C.; Koutmos, M.; Garrow, T.A.
Betaine-homocysteine S-methyltransferase-2 is an S-methylmethionine-homocysteine methyltransferase
J. Biol. Chem.
283
8939-8945
2008
Homo sapiens
Manually annotated by BRENDA team