Information on EC 2.1.1.10 - homocysteine S-methyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.1.1.10
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RECOMMENDED NAME
GeneOntology No.
homocysteine S-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-methyl-L-methionine + L-homocysteine = 2 L-methionine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-methionine salvage from L-homocysteine
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S-methyl-L-methionine cycle
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methionine metabolism
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Cysteine and methionine metabolism
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Metabolic pathways
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Biosynthesis of secondary metabolites
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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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
var. italica, broccoli
TrEMBL
Manually annotated by BRENDA team
strain ATCC 9950
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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prevents accumulation of (R,S)-S-adenosyl methionine (formed by spontaneous racemization)
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R,S)-S-adenosyl-L-methionine + L-homocysteine
L-methionine + S-adenosyl-L-homocysteine
show the reaction diagram
(S,S)-S-adenosyl-L-methionine + L-homocysteine
L-methionine + S-adenosyl-L-homocysteine
show the reaction diagram
-
higher affinity for R,S form
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-
?
S-adenosyl-D-methionine + L-homocysteine
?
show the reaction diagram
S-adenosyl-L-ethionine + L-homocysteine
S-adenosyl-L-homocysteine + L-ethionine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + D-homocysteine
?
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + DL-cysteine
S-adenosyl-L-homocysteine + S-methyl-DL-cysteine
show the reaction diagram
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-
-
?
S-adenosyl-L-methionine + DL-homocysteine
L-methionine + S-adenosyl-L-homocysteine
show the reaction diagram
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-
-
?
S-adenosyl-L-methionine + DL-selenocysteine
S-adenosyl-L-homocysteine + Se-methyl-DL-selenocysteine
show the reaction diagram
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-
-
?
S-adenosyl-L-methionine + L-cysteine
S-adenosyl-L-homocysteine + S-methyl-L-cysteine
show the reaction diagram
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-
-
?
S-adenosyl-L-methionine + L-homocysteine
?
show the reaction diagram
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low activity
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-
?
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
show the reaction diagram
S-adenosyl-L-methionine + L-homocysteine thiolactone
?
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + L-selenocysteine
S-adenosyl-L-homocysteine + Se-methyl-L-selenocysteine
show the reaction diagram
-
-
-
?
S-methyl-L-methionine + L-cysteine
?
show the reaction diagram
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-
-
?
S-methyl-L-methionine + L-homocysteine
2 L-methionine
show the reaction diagram
S-methyl-L-methionine + L-homocysteine
?
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
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
Q47690
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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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-methionine
N-Hydroxymethyl-DL-methionine
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S-adenosyl-L-homocysteine
S-adenosyl-L-methionine
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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increases activity at low substrate concentrations
cysteine
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homocysteine
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induces reaction
homoserine
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S-[(2R)-2-amino-2-carboxyethyl]-L-homocysteine
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additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.072
DL-homocysteine
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0.018 - 0.077
L-homocysteine
0.225 - 1.95
S-adenosyl-L-methionine
0.029 - 0.94
S-methyl-L-methionine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0375
DL-homocysteine
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0.38
L-homocysteine
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pH 6, 30°C, cosubstrate: S-adenosyl-L-methionine
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
0.0008
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kidney, S-methyl-L-methionine as methyl donor
0.0009
using L-selenocysteine as substrate
0.0017
using DL-selenocysteine as substrate
0.0022
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liver, S-adenosyl-L-methionine as methyl donor
0.0054
using L-cysteine as substrate
0.0087
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liver, S-methyl-L-methionine as methyl donor
0.012
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S-methyl-L-methionine as methyl donor
0.014
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S-methyl-L-methionine as methyl donor
0.0147
using DL-cysteine as substrate
0.017
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S-methyl-L-methionine as methyl donor
0.0936
using DL-homocysteine as substrate
1.37
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purified enzyme, S-adenosyl-L-methionine as methyl donor
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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activity assay at
30 - 35
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
rosette leaves, cauline leaves
Manually annotated by BRENDA team
additional information
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no activity detected in brain and heart
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
Escherichia coli (strain K12);
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
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from sedimentation coefficient
32500
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1 * 32500, calculated from sequence
34000
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gel filtration
34490
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1 * 34490, calculated, 1 * 35000, SDS-PAGE
35400
calculated from amino acid sequence
36000
gel filtration; gel filtration
36400
1 * 36400, calculated from sequence
40000
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SDS-PAGE, 73% sequence identity with the 45 kDa BHMT protein (EC 2.1.1.5)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in oxidized, apo, and metallated form, to 1.8-1.9 A resolution
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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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recombinant enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli, recombinant protein, intein/chitin-binding fusion constructs, pTBY3 vector
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expression in Escherichia coli
expression in Escherichia coli; expression in Escherichia coli
in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y71F/T169Y
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mutant designed to mimic the betaine-homocysteine methyltransferase substrate binding pocket, complete loss of activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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determination of total homocysteine in plasma and serum
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