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2.1.1.5: betaine-homocysteine S-methyltransferase

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

Word Map on EC 2.1.1.5

Reaction

betaine
+
L-homocysteine
=
dimethylglycine
+
L-methionine

Synonyms

betaine homocysteine methyltransferase, betaine homocysteine methyltransferase-1, betaine homocysteine S-methyltransferase, betaine-homocysteine methyltransferase, betaine-homocysteine S-methyltransferase, betaine-homocysteine S-methyltransferase 2, betaine-homocysteine S-methyltransferase-2, betaine-homocysteine transmethylase, betaine:homocysteine methyltransferase, betaine:homocysteine S-methyltransferase, BHMT, BHMT-1, BHMT-2, BHMT1, BHMT2, methyltransferase, betaine-homocysteine

ECTree

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

Oxidation Stability

Oxidation Stability on EC 2.1.1.5 - betaine-homocysteine S-methyltransferase

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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is susceptible to conformation-dependent oxidative inactivation. When BHMT is incubated with up to 78 mM t-butyl hydroperoxide, no appreciable amount of ZN or activity is lost, indicating that oxidation of surface met residues are not involved in the oxidative inactivation of BHMT. Methyl methanethiosulfonate and H2O2, cause a loss of catalytic Zn and a correlative loss of activity. Addition of beta-mercaptoethanol and exogenous Zn after methyl methanethiosulfonate treatment restores activity, but oxidation due to H2O2 is irreversible. The L2 loop is involved in the conformational change associated with accupancy at the betaine binding site. This conformational change and/or occupancy at both ligand binding sites protects the enzyme from oxidative inactivation
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