Mechanism and structural requirements for transformation of substrates by the (S)-adenosyl-L-methionine:Δ24(25)sterol methyl transferase from Saccharomyces cerevisiae

Biochimica et Biophysica Acta - Lipids and Lipid Metabolism

Volumn 1299, Issue 3, 1996, Pages 313-324

  Venkatramesh, Mylavarapu ^a   Guo, De An ^a,b   Jia, Zhonghua ^a   Nes, W David ^a  

^a TEXAS TECH UNIVERSITY   (United States)

^b PEKING UNIVERSITY HEALTH SCIENCE CENTER   (China)

Author keywords

(S. Cerevisiae); Kinetics; Membrane fluidity; Sterol biomethylation

Indexed keywords

METHYLTRANSFERASE; STEROL;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME KINETICS; ENZYME SPECIFICITY; MEMBRANE FLUIDITY; NONHUMAN; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE; STEREOCHEMISTRY; STRUCTURE ACTIVITY RELATION;

CELL FRACTIONATION; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; ENZYME INHIBITORS; KINETICS; METHYLATION; METHYLTRANSFERASES; MICROSOMES; MODELS, BIOLOGICAL; S-ADENOSYLMETHIONINE; SACCHAROMYCES CEREVISIAE; SOLUBILITY; STEROLS; SUBSTRATE SPECIFICITY;

EID: 0030044184     PISSN: 00052760     EISSN: None     Source Type: Journal    
DOI: 10.1016/0005-2760(95)00218-9     Document Type: Article

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