Liver betaine-homocysteine S-methyltransferase activity undergoes a redox switch at the active site zinc

Archives of Biochemistry and Biophysics

Volumn 472, Issue 1, 2008, Pages 26-33

  Castro, Carmen ^a   Millian, Norman S ^b   Garrow, Timothy A ^b  

^a UNIVERSITY OF CÁDIZ   (Spain)

^b UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

BHMT; Cysteine; Glutamate cysteine ligase modifier subunit Gclm( ) knockout mouse; Glutathione; Methionine; Oxidative stress

Indexed keywords

BETAINE HOMOCYSTEINE METHYLTRANSFERASE; GLUTAMATE CYSTEINE LIGASE; GLUTATHIONE; HYDROXYL GROUP; REDUCING AGENT; THIOL; ZINC;

ANIMAL EXPERIMENT; ARTICLE; CATALYSIS; CONTROLLED STUDY; DISULFIDE BOND; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INACTIVATION; GLUTATHIONE METABOLISM; HUMAN; KNOCKOUT MOUSE; LIGAND BINDING; LIVER; LONG TERM EXPOSURE; MOUSE; NONHUMAN; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PRIORITY JOURNAL;

BETAINE-HOMOCYSTEINE S-METHYLTRANSFERASE; BINDING SITES; CATALYSIS; ENZYME ACTIVATION; HUMANS; LIVER; OXIDATION-REDUCTION; PROTEIN BINDING; SULFHYDRYL COMPOUNDS; ZINC;

MUS;

EID: 40649100255     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2008.01.017     Document Type: Article

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