Abstract
Publisher Summary This chapter discusses the assay method, purification procedures, and properties of pyruvate dehydrogenase complex (PDC) isolated from Neurospora. The pyruvate dehydrogenase complex (PDC) is isolated from a number of sources, including Escherichia coli and other bacteria, the pigeon muscle, mammalian tissues Neurospora crassa, and higher plants. The conversion of pyruvate to acetyl-CoA is catalyzed by three enzymes associated in an enzyme complex: (1) pyruvate dehydrogenase, (2) dihydrolipoyl transacetylase, and (3) dihydrolipoyl dehydrogenase. The pyruvate dehydrogenase complex activity is measured by monitoring nicotinamide adenine dinucleotide (NADH) formation spectrophotometrically at 340 nm. NADH oxidase activity, which is present in the sonication supernatant, is removed by the protamine fractionation. Neurospora PDC is known to be localized on the outer mitochondrial membrane. The detergent Lubrol-WX is used in place of sonication to liberate PDC from the mitochondria. Adenosine triphosphate at 5 mM inhibits enzyme activity by 93%. The inhibition of Neurospora PDC by ATP is because of the phosphorylation of the complex by an associated kinase.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
