A phosphorus 31 nuclear magnetic resonance study of the intermediates of the Escherichia coli succinyl coenzyme A synthetase reaction. Evidence for substrate synergism and catalytic cooperativity.
H J Vogel,W A Bridger +1 more
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This article is published in Journal of Biological Chemistry.The article was published on 1982-05-10 and is currently open access. It has received 34 citations till now. The article focuses on the topics: Succinyl coenzyme A synthetase & Cooperativity.read more
Citations
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Journal ArticleDOI
Primary structure of the succinyl-CoA synthetase of Escherichia coli
TL;DR: The primary structure of the succinyl-CoA synthetase of Escherichia coli has been deduced from the nucleotide sequence of a 2451-base-pair segment of DNA containing the corresponding sucC (beta sub unit) and sucD (alpha subunit) genes.
Journal ArticleDOI
Photoaffinity-labeling peptide substrates for farnesyl-protein transferase and the intersubunit location of the active site.
TL;DR: Pseudo first-order photolytic inhibition of FPTase preparations with BZ-peptides, as well as protection from photoinactivation by unmodified -CAAX motif peptides, supported the capacity of these Bz- peptides to serve as co-substrates and their specificity for seeking the catalytic site of the enzyme.
Book ChapterDOI
Phosphorus-31 nuclear magnetic resonance studies of phosphorylated proteins
Manfred Brauer,Brian D. Sykes +1 more
TL;DR: This chapter focuses on the characterization of phosphorylated target protein by phosphorus-31 nuclear magnetic resonance (31P NMR), which can provide a range of information about the nature and dynamics of the phosphorylation site that cannot be obtained by other methods.
Journal ArticleDOI
Phosphorus-31 nuclear magnetic resonance study of the active site phosphohistidine and regulatory phosphoserine residues of rat liver ATP-citrate lyase
TL;DR: 31P NMR spectra of ATP-citrate lyase that had previously been exposed to fairly high concentrations of potassium chloride (1.5 M), or that had been denatured in detergent and 2-mercaptoethanol, clearly identified phosphohistidine as the catalytic phosphate group.
References
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Book ChapterDOI
The Role of Negative Cooperativity and Half-of-the-Sites Reactivity in Enzyme Regulation
TL;DR: The role of negative cooperativity and half-of-the-sites reactivity in enzyme regulation and diagnostic tests for the property are discussed, and some well studied regulatory enzymes are described.
Journal ArticleDOI
Phosphorus-31 nuclear magnetic resonance study of alkaline phosphatase: the role of inorganic phosphate in limiting the enzyme turnover rate at alkaline pH
TL;DR: The 31P NMR line width of the E-P1 complex indicates that the dissociation of noncovalent phosphate is the rate-limiting step in the turnover of the enzyme at high pH.
Journal ArticleDOI
The Preparation, Properties, and Reactions of Succinyl Coenzyme A Synthetase and Its Phosphorylated Form
TL;DR: Capacity of different preparations for E-P formation, as compared to catalytic activity, varies in an unexplained manner.
Journal ArticleDOI
Substrate synergism and phosphoenzyme formation in catalysis by succinyl coenzyme A synthetase.
Journal ArticleDOI
The phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus aureus. 2. 1H and 31P-nuclear-magnetic-resonance studies on the phosphocarrier protein HPr, phosphohistidines and phosphorylated HPr
Martin K. Gassner,Dietmar Stehlik,Otto Schrecker,Wolfgang Hengstenberg,Wolfgang Maurer,Heinz Rüterjans +5 more
Related Papers (5)
Substrate synergism and phosphoenzyme formation in catalysis by succinyl coenzyme A synthetase.
Catalysis of a step of the overall reaction by the alpha subunit of Escherichia coli succinyl coenzyme A synthetase.
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Affinity labeling of succinyl-CoA synthetase from porcine heart and Escherichia coli with oxidized coenzyme A disulfide.
G E Collier,J S Nishimura +1 more