Pre-steady-state kinetic studies of Saccharomyces cerevisiae myristoylCoA:protein N-myristoyltransferase mutants identify residues involved in catalysis.

Farazi, T A; Manchester, J K; Waksman, G; Gordon, J I

Farazi, T A; Manchester, J K; Waksman, G; Gordon, J I.

Affiliation

Farazi TA; Department of Molecular Biology and Pharmacology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.

Biochemistry ; 40(31): 9177-86, 2001 Aug 07.

Article in En | MEDLINE | ID: mdl-11478885

Subject(s)

Acyltransferases/genetics; Acyltransferases/metabolism; Amino Acid Substitution/genetics; Ion Pumps; Multienzyme Complexes; Mutagenesis, Site-Directed; Saccharomyces cerevisiae/enzymology; Saccharomyces cerevisiae/genetics; Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/metabolism; Alanine/genetics; Animals; Arsenate Reductases; Arsenite Transporting ATPases; Asparagine/genetics; Catalysis; Cattle; Kinetics; Leucine/genetics; Myristic Acid/metabolism; Peptide Fragments/genetics; Phenylalanine/genetics; Rabbits; Saccharomyces cerevisiae Proteins; Sequence Deletion; Spectrometry, Fluorescence; Substrate Specificity/genetics; Swine; Threonine/genetics

Search on Google

Add to My VHL

XML

PubMed Links

Collection: 01-internacional Database: MEDLINE Main subject: Saccharomyces cerevisiae / Acyltransferases / Mutagenesis, Site-Directed / Ion Pumps / Amino Acid Substitution / Multienzyme Complexes Type of study: Prognostic_studies Limits: Animals Language: En Journal: Biochemistry Year: 2001 Document type: Article Affiliation country: United States Country of publication: United States

Search on Google

Add to My VHL

XML

PubMed Links