@article{mbs:/content/journal/micro/10.1099/00221287-99-1-69, author = "Ryder, N. S. and Peberdy, J. F.", title = "Chitin Synthase in Aspergillus nidulans: Properties and Proteolytic Activation", journal= "Microbiology", year = "1977", volume = "99", number = "1", pages = "69-76", doi = "https://doi.org/10.1099/00221287-99-1-69", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-99-1-69", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "Summary: Chitin synthase (EC 2.4.1.16) from membrane preparations of Aspergillus nidulans was characterized and the optimum conditions for enzyme activity were determined. A reaction velocity-substrate concentration plot was sigmoidal, but was hyperbolic in the presence of N-acetylglucosamine when the K m for UDP-N-acetylglucosamine was 3·1 mmol 1−1. Chitin synthase activity could be increased sixfold by digestion of enzyme preparations with trypsin for short periods. The trypsin-activated enzyme had altered kinetic and storage properties.", }