Literature summary for 2.1.1.5 extracted from

Miller, C.M.; Szegedi, S.S.; Garrow, T.A.
Conformation-dependent inactivation of human betaine-homocysteine S-methyltransferase by hydrogen peroxide in vitro (2005), Biochem. J., 392, 443-448.

General Stability

General Stability	Organism
partial digestion of ligand-free enzyme with trypsin produces two large peptides, excising a seven residue peptide with loop L2. Carboxybutylhomocysteine but not methionine slows proteolysis by trypsin	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
H2O2	causes a loss of catalytic Zn and a correlative loss of activity, irreversible	Homo sapiens
methyl methanethiosulfonate	causes a loss of catalytic Zn and a correlative loss of activity. Addition of beta-mercaptoethanol and exogenous Zn after methyl methanethiosulfonate treatment restores activity	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q93088	-	-

Oxidation Stability

Oxidation Stability	Organism
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	Homo sapiens

Organism

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

Homo sapiens

Synonyms

Synonyms	Comment	Organism
BHMT	-	Homo sapiens