Dissecting the catalytic mechanism of betaine-homocysteine S-methyltransferase by use of intrinsic tryptophan fluorescence and site-directed mutagenesis.

Castro, Carmen

Dissecting the catalytic mechanism of betaine-homocysteine S-methyltransferase by use of intrinsic tryptophan fluorescence and site-directed mutagenesis. [electronic resource] - Biochemistry May 2004 - 5341-51 p. digital

Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.

0006-2960

10.1021/bi049821x doi


Betaine--metabolism
Betaine-Homocysteine S-Methyltransferase
Binding Sites--genetics
Catalysis
Enzyme Inhibitors--chemistry
Glutamic Acid--genetics
Homocysteine--analogs & derivatives
Humans
Kinetics
Ligands
Methionine--metabolism
Methyltransferases--antagonists & inhibitors
Mutagenesis, Site-Directed
Protein Binding--genetics
Sarcosine--analogs & derivatives
Spectrometry, Fluorescence--methods
Substrate Specificity--genetics
Tryptophan--chemistry
Tyrosine--genetics