Moore P M, Peberdy J F
Microbios. 1975;12(47-48):29-39.
The enzyme chitin synthetase (UDP-acetylaminodeoxyglucosyl transferase, EC 2.4.1.16) in Cunninghamella elegans has been investigated. The enzyme was present in the microsomal, cell wall, mitochondrial and the soluble cytoplasmic fraction of the mycelium, with the former having the highest specific activity. The properties of the enzyme in this fraction were investigated; the Km for UDP GlcNAc was 1.23 mM and 2.08 mM GlcNAc in the presence of 1 mM UDP GlcNAc. The temperature optimum was between 26 degrees and 29 degrees C and maximal activity was at pH 6.25. Mg++ ions had no effect on chitin synthesis, but soluble chitodextrins inhibited the enzyme. The production of chitin synthetase was correlated with the growth of the fungus, maximum activity being found during the late exponential phase of growth. Chitin was confirmed as the sole product of enzyme action, by digestion with chitinase.
对雅致小克银汉霉中的几丁质合成酶(UDP-乙酰氨基脱氧葡萄糖基转移酶,EC 2.4.1.16)进行了研究。该酶存在于菌丝体的微粒体、细胞壁、线粒体和可溶性细胞质部分,其中微粒体部分的比活性最高。对该部分中酶的性质进行了研究;在存在1 mM UDP GlcNAc的情况下,UDP GlcNAc的Km为1.23 mM,GlcNAc的Km为2.08 mM。最适温度在26℃至29℃之间,最大活性在pH 6.25时出现。Mg++离子对几丁质合成没有影响,但可溶性几丁质糊精会抑制该酶。几丁质合成酶的产生与真菌的生长相关,在生长的指数后期发现最大活性。通过用几丁质酶消化,证实几丁质是酶作用的唯一产物。