Výsledky vyhledávání - "J S, Nishimura"

Sensitivity of Escherichia coli succinyl-CoA mutants at Trp beta 76 to clostripain and to trypsin. ADP and ATP protect against cleavage by clostripain at Arg beta 80

Autor: J S, Nishimura, J, Ybarra, C J, Mann, T, Mitchell

Publikováno v: The Journal of biological chemistry. 268(18)

Mutant forms of Escherichia coli succinyl-CoA synthetase, W76F (Trp beta 76 replaced by Phe) (Nishimura, J. S., Mann, C. J., Ybarra, J., Mitchell, T., and Horowitz, P. M. (1990) Biochemistry 29, 862-865), and W43,76,248F (all three Trp replaced by Ph

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1fce9b490a3e60ac4bf5660ff6daa2b1
https://pubmed.ncbi.nlm.nih.gov/8514803

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Adenosine 5'-tetraphosphate is synthesized by the histidine alpha 142----asparagine mutant of Escherichia coli succinyl-CoA synthetase

Autor: G X, Luo, J S, Nishimura

Publikováno v: The Journal of biological chemistry. 267(14)

Recently, we described the properties of a mutant (H142N) of Escherichia coli succinyl coenzyme A (CoA) synthetase in which His-142 of the alpha-subunit was changed to Asn (Luo, G.-X., and Nishimura, J.S. (1991) J. Biol. Chem. 266, 20781-20785). The

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::cb832d64a94c47d6f141d1f048153a8c
https://pubmed.ncbi.nlm.nih.gov/1577794

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Affinity labeling of succinyl-CoA synthetase from porcine heart and Escherichia coli with oxidized coenzyme A disulfide

Autor: J S Nishimura, G E Collier

Publikováno v: Journal of Biological Chemistry. 253:4938-4943

Incubation of oxidized coenzyme A disulfide (produced by oxidation of reduced CoA with 1 eq of sodium periodiate or of CoA disulfide with 1 eq of peracetic acid) with succinyl-CoA disulfide with 1 eq of peracetic acid) with succinyl-CoA synthetase fr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::80206944cead8f7d58a1279c44541ea2
https://doi.org/10.1016/s0021-9258(17)34638-0

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Acetate kinase from Veillonella alcalescens. Regulation of enzyme activity by succinate and substrates

Autor: J S Nishimura, C M Bowman, R O Valdez

Publikováno v: Journal of Biological Chemistry. 251:3117-3121

Acetate kinase of Veillonella alcalescens has been shown to be highly regulated enzyme exhibiting two levels of control: the requirement for succinate as a heterotropic allosteric effector, and cooperative binding at the substrate level. Succinate ad

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::31a0f2050370ec71ebf4430976a78c6d
https://doi.org/10.1016/s0021-9258(17)33506-8

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Escherichia coli succinyl coenzyme A synthetase. Inhibition of ATP-stimulated succinate—-succinyl coenzyme A exchange at low succinyl coenzyme A concentrations by an ADP trap

Autor: J S Nishimura, T Mitchell

Publikováno v: Journal of Biological Chemistry. 259:2144-2148

The hypothesis that Escherichia coli succinyl-CoA synthetase functions by a cooperative alternating sites mechanism is based largely on the results of [18O]phosphate exchange experiments (Bild, G. S., Janson, C. A., and Boyer, P. D. (1980) J. Biol. C

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c28c8ce882f99055cbf9d289f681cf37
https://doi.org/10.1016/s0021-9258(17)43328-x

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Acetate kinase from Veillonella alcalescens. Regulation by succinate and substrates

Autor: M J Griffith, J S Nishimura

Publikováno v: Journal of Biological Chemistry. 254:6698-6702

The kinetic properties of acetate kinase from Veillonella alcalescens were investigated. In the presence of high concentrations of nucleotide both forward and reverse reactions were observed. In the presence of succinate the degree of cooperativity b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::596b62d80f537aa0e687bbb6d3b9845b
https://doi.org/10.1016/s0021-9258(18)50425-7

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Evidence for a second histidine at the active site of succinyl-CoA synthetase from Escherichia coli

Autor: G E Collier, J S Nishimura

Publikováno v: Journal of Biological Chemistry. 254:10925-10930

Ethoxyformic anhydride was used to demonstrate the existence of a second important histidine in succinyl-CoA synthetase from Escherichia coli. Differential labeling of the enzyme by [3H]ethoxyformic anhydride gave a stoichiometry of one important his

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b74439c57768751c63f5b08862f2fa86
https://doi.org/10.1016/s0021-9258(19)86612-7

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Escherichia coli succinic thiolinase. Stoichiometry of phosphorylation and coenzyme A binding

Autor: C M Bowman, J S Nishimura

Publikováno v: Journal of Biological Chemistry. 250:5609-5613

Equilibrium and covalent binding studies of succinic thiokinase from Escherichia coli indicates that there can be a stoichiometric relationship between coenzyme A binding and the phosphoyrlation capacity of the enzyme. A comparison of homogeneous enz

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2ece590b0e7511adbb025fe70af8b187
https://doi.org/10.1016/s0021-9258(19)41223-4

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Affinity chromatography and affinity labeling of rat liver succinyl-CoA synthetase

Autor: J S Nishimura, D J Ball

Publikováno v: Journal of Biological Chemistry. 255:10805-10812

Succinyl-CoA synthetase has been purified to apparent homogeneity from rat liver. The key step in the purification procedure involved adsorption on a GDP dialdehyde (dial-GDP)-adipic dihydrazide-Sepharose 4B column and elution by GDP-Mg2+. Like the p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::efbb02269b6535b2435c4e35ce027c26
https://doi.org/10.1016/s0021-9258(19)70379-2

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