Limited proteolysis of the pyruvate dehydrogenase multienzyme complex of Bacillus subtilis
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چکیده
منابع مشابه
Limited proteolysis and proton n.m.r. spectroscopy of the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli.
The 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli was treated with trypsin at pH 7.0 at 0 degrees C. Loss of the overall catalytic activity was accompanied by rapid cleavage of the lipoate succinyltransferase polypeptide chains, this apparent Mr falling from 50 000 to 36 000 as judged by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. A slower shortening of th...
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The neisserial P64k antigen is a dihydrolipoamide dehydrogenase which is partially found on the cell envelope. Given its unusual localization pattern and taking into account that dihydrolipoamide dehydrogenases are generally associated with the bulky complexes of cytoplasmic α-ketoacid dehydrogenases, we have tried to determine if at least part of the P64k participates in either pyruvate dehydr...
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The peripheral subunit-binding domain (PSBD) of the dihydrolipoyl acetyltransferase (E2, EC 2.3.1.12) binds tightly but mutually exclusively to dihydrolipoyl dehydrogenase (E3, EC 1.8.1.4) and pyruvate decarboxylase (E1, EC 1.2.4.1) in the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. Isothermal titration calorimetry (ITC) experiments demonstrated that the enthalpie...
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متن کاملTheoretical Study of the Catalytic Mechanism of E1 Subunit of Pyruvate Dehydrogenase Multienzyme Complex from <italic>Bacillus stearothermophilus</italic>
Pyruvate dehydrogenase multienzyme complex (PDHc) is a member of a family of 2-oxo acid dehydrogenase (OADH) multienzyme complexes involved in several central points of oxidative metabolism, and the E1 subunit is the most important component in the entire PDHc catalytic system, which catalyzes the reversible transfer of an acetyl group from a pyruvate to the lipoyl group of E2 subunit lipoly do...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1985
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2250249