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2.1.1.10: homocysteine S-methyltransferase

This is an abbreviated version!
For detailed information about homocysteine S-methyltransferase, go to the full flat file.

Word Map on EC 2.1.1.10

Reaction

S-methyl-L-methionine
+
L-homocysteine
= 2 L-methionine

Synonyms

adenosylmethionine transmethylase, adenosylmethionine:homocysteine methyltransferase, AtHMT-1, AtHMT-2, AtHMT-3, BHMT, BHMT-2, F775_07039, HMT, HMT1, homocysteine methylase, homocysteine methyltransferase, homocysteine methyltransferase Mht1, homocysteine methyltransferase Sam4, 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, S-methylmethionine: homocysteine methyltransferase, S-methylmethionine: homocysteine S-methyltransferase, SMM:homocysteine S-methyltransferase, YagD, YagD protein

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.10 homocysteine S-methyltransferase

Specific Activity

Specific Activity on EC 2.1.1.10 - homocysteine S-methyltransferase

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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0008
-
kidney, S-methyl-L-methionine as methyl donor
0.0009
using L-selenocysteine as substrate
0.0017
using DL-selenocysteine as substrate
0.0022
-
liver, S-adenosyl-L-methionine as methyl donor
0.0044
mutant K10A, pH 7.5, 37°C
0.0047
mutant K8A, pH 7.5, 37°C
0.0054
using L-cysteine as substrate
0.0087
-
liver, S-methyl-L-methionine as methyl donor
0.0109
mutant K7A, pH 7.5, 37°C
0.012
-
S-methyl-L-methionine as methyl donor
0.01215
wild-type, pH 7.5, 37°C
0.014
-
S-methyl-L-methionine as methyl donor
0.0147
using DL-cysteine as substrate
0.017
-
S-methyl-L-methionine as methyl donor
0.0936
using DL-homocysteine as substrate
0.164
crude extract, pH 7.2, 37°C
1.37
-
purified enzyme, S-adenosyl-L-methionine as methyl donor
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