Abstract
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.
Keywords: acetyl enzyme, K. aerogenes, enzyme mechanism, hydroxylamine
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Selected References
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