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:1972
卷号:69
期号:5
页码:1201-1202
DOI:10.1073/pnas.69.5.1201
语种:English
出版社:The National Academy of Sciences of the United States of America
摘要:Citrate lyase from Klebsiella aerogenes inactivated by reaction in the presence of substrate or by treatment with hydroxylamine can be reactivated with acetic anhydride only if its sulfhydryl groups are reduced. Alkaline hydrolysis of pure citrate lyase yields about 3 mol of phosphopantothenate per mol of enzyme.
关键词:acetyl enzyme ; K. aerogenes ; enzyme mechanism ; hydroxylamine