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Synthesis and proteolytic activation of chitin synthetase in Phycomyces blakesleeanus Burgeff

Synthesis and proteolytic activation of chitin synthetase in Phycomyces blakesleeanus Burgeff 203 116 116 2 2 André J. van Laere Albert R. Carlier Laboratorium voor plantenbiochemie K. U. Leuven Vaartstraat 24 B-3000 Leuven Belgium Abstract The chitin synthetase of Phycomyces blakesleeanus mycelium is a particulate enzyme sedimenting mostly at 1000xg. The activity in crude extracts or cellular fractions can be increased more than tenfold by mild trypsin treatment. Plotting the reaction velocity versus UDP-N-acetylglucosamine concentration yields a sigmoidal curve. N-acetylglucosamine, which greatly stimulates the enzyme, changes the kinetics to an almost normal hyperbolic relationship. The enzyme is nearly absent in dormant spores and is synthesized “de novo” in germinating spores (from 4 h germination on). Trypsin treatment of extracts from germinating spores to assay the synthesis of the proenzyme did not reveal an earlier synthesis of the zymogen, which therefore might have some activity of its own. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Microbiology Springer Journals

Synthesis and proteolytic activation of chitin synthetase in Phycomyces blakesleeanus Burgeff

Laere, André; Carlier, Albert
Archives of Microbiology , Volume 116 (2) – Feb 1, 1978
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References (12)

Publisher
Springer Journals
Copyright
Copyright © 1978 by Springer-Verlag
Subject
Life Sciences; Biotechnology; Biochemistry, general; Cell Biology; Ecology; Microbial Ecology; Microbiology
ISSN
0302-8933
eISSN
1432-072X
DOI
10.1007/BF00406034
Publisher site
See Article on Publisher Site

Abstract

203 116 116 2 2 André J. van Laere Albert R. Carlier Laboratorium voor plantenbiochemie K. U. Leuven Vaartstraat 24 B-3000 Leuven Belgium Abstract The chitin synthetase of Phycomyces blakesleeanus mycelium is a particulate enzyme sedimenting mostly at 1000xg. The activity in crude extracts or cellular fractions can be increased more than tenfold by mild trypsin treatment. Plotting the reaction velocity versus UDP-N-acetylglucosamine concentration yields a sigmoidal curve. N-acetylglucosamine, which greatly stimulates the enzyme, changes the kinetics to an almost normal hyperbolic relationship. The enzyme is nearly absent in dormant spores and is synthesized “de novo” in germinating spores (from 4 h germination on). Trypsin treatment of extracts from germinating spores to assay the synthesis of the proenzyme did not reveal an earlier synthesis of the zymogen, which therefore might have some activity of its own.

Journal

Archives of Microbiology – Springer Journals

Published: Feb 1, 1978

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