Jun 10, 1976

The activating system of chitin synthetase from Saccharomyces cerevisiae. Purification and properties of the activating factor

The Journal of Biological Chemistry
R E Ulane, E Cabib

Abstract

The yeast proteinase that causes activation of the chitin synthetase zymogen has been purified by a procedure that includes affinity chromatography on an agarose column to which the proteinaceous inhibitor of the enzyme had been covalently attached. The purified enzyme yielded a single band upon disc gel electrophoresis at pH 4.5 in the presence of urea. At the same pH, but without urea, a faint band was detected in coincidence with enzymatic activity, whereas at pH 9.5, either in the absence or in the presence of sodium dodecyl sulfate, no protein zone could be seen. From sedimentation and gel filtration data, a molecular weight of 44,000 was estimated. The proteinase was active within a wide range of pH values, with an optimum between pH 6.5 AND 7. Titraton of the activity with the protein inhibitor from yeast required 1 mol of inhibitor/mol of enzyme. A similar result was obtained with phenylmethylsulfonyl fluoride, an indication that 1 serine residue is required for enzymatic activity. The enzyme exhibited hydrolytic activity with several proteins and esterolytic activity with many synthetic substrates, including benzoylarginine ethyl ester and acetyltyrosine ethyl ester.A comparison of the properties of the enzyme with tho...Continue Reading

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Mentioned in this Paper

Chitin Synthetase 2
Saccharomyces cerevisiae allergenic extract
Structure-Activity Relationship
Peptide Hydrolases
Proteinase B Activity
Endopeptidases
Proteolytic Enzyme
Gel Chromatography
Electrophoresis, Disc
Hydrolase

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