期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1979
卷号：76
期号：9
页码：4581-4585
DOI：10.1073/pnas.76.9.4581
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Strains of Saccharomyces cerevisiae bearing nonsense mutations in the structural gene for proteinase B (EC 3.4.22.9 ) have been examined for the ability to make the transition from growth on acetate to growth on glucose and for the ability to inactivate three glucoeogenic enzymes during the transition because proteinase B has been proposed by others to be responsible for the inactivation of the three enzymes during the growth transition. The mutant strains make the growth transition normally. Catabolite inactivation of hexosediphosphatase (D-fructose-1,6-biphosphate 1-phosphohydrolase, EC 3.1.3.11 ), malate dehydrogenase (L-malate:NAD+ oxidoreductase, EC 1.1.1.37 ), and phosphoenolpyruvate carboxykinase (ATP) [ATP:oxaloacetate carboxy-lyase (transphosphorylating), EC 4.1.1.49 ] occurred in prb1 mutants with kinetics similar to those seen in wild-type strains. We infer that proteinase B activity is not essential for the process of catabolite inactivation.
