These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
133 related articles for article (PubMed ID: 788782)
1. Nuclear magnetic resonance relaxation time studies on the manganese(II) ion complex with succinyl coenzyme A synthetase from Escherichia coli. Lam YF; Bridger WA; Kotowycz G Biochemistry; 1976 Oct; 15(21):4742-8. PubMed ID: 788782 [TBL] [Abstract][Full Text] [Related]
2. Interactions of phospho- and dephosphosuccinyl coenzyme A synthetase with manganous ion and substrates. Studies of manganese complexes by NMR relaxation rates of water protons. Buttlaire DH; Chon M J Biol Chem; 1977 Mar; 252(6):1957-64. PubMed ID: 321448 [TBL] [Abstract][Full Text] [Related]
3. Manganese(II) and substrate interaction with unadenylylated glutamine synthetase (Escherichia coli w). I. Temperature and frequency dependent nuclear magnetic resonance studies. Villafranca JJ; Ash DE; Wedler FC Biochemistry; 1976 Feb; 15(3):536-43. PubMed ID: 766828 [TBL] [Abstract][Full Text] [Related]
4. Manganese (II) and substrate interaction with unadenylylated glutamine synthetase (Escherichia coli w). II. Electron paramagnetic resonance and nuclear magnetic resonance studies of enzyme-bound manganese(II) with substrates and a potential transition-state analogue, methionine sulfoximine. Villafranca JJ; Ash DE; Wedler FC Biochemistry; 1976 Feb; 15(3):544-53. PubMed ID: 3200 [TBL] [Abstract][Full Text] [Related]
5. 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. Vogel HJ; Bridger WA J Biol Chem; 1982 May; 257(9):4834-42. PubMed ID: 7040388 [No Abstract] [Full Text] [Related]
6. Catalysis of a step of the overall reaction by the alpha subunit of Escherichia coli succinyl coenzyme A synthetase. Pearson PH; Bridger WA J Biol Chem; 1975 Nov; 250(21):8524-9. PubMed ID: 1104606 [TBL] [Abstract][Full Text] [Related]
7. Contribution of subunit interactions to the effectiveness of catalysis by succinyl coenzyme A synthetase. Bridger WA Curr Top Cell Regul; 1984; 24():345-55. PubMed ID: 6389023 [No Abstract] [Full Text] [Related]
8. 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. Nishimura JS; Mitchell T J Biol Chem; 1984 Feb; 259(4):2144-8. PubMed ID: 6365903 [TBL] [Abstract][Full Text] [Related]
9. An n.m.r. probe of succinyl-coenzyme A synthetase: subunit interactions and the mechanism of action. Vogel HJ; Bridger WA Biochem Soc Trans; 1983 Jun; 11(3):315-23. PubMed ID: 6347742 [No Abstract] [Full Text] [Related]
10. Role of metal ions in Escherichia coli alkaline phosphatase. A study of the metal-water interaction by nuclear relaxation rate measurements on water protons. Zukin RS; Hollis DP J Biol Chem; 1975 Feb; 250(3):835-42. PubMed ID: 163241 [TBL] [Abstract][Full Text] [Related]
11. Evidence for a second histidine at the active site of succinyl-CoA synthetase from Escherichia coli. Collier GE; Nishimura JS J Biol Chem; 1979 Nov; 254(21):10925-30. PubMed ID: 387761 [TBL] [Abstract][Full Text] [Related]
12. Affinity labeling of succinyl-CoA synthetase from porcine heart and Escherichia coli with oxidized coenzyme A disulfide. Collier GE; Nishimura JS J Biol Chem; 1978 Jul; 253(14):4938-43. PubMed ID: 353044 [TBL] [Abstract][Full Text] [Related]
13. Chemical modification and hybrid enzyme formation as probes of the active site and subunit interactions in Escherichia coli succinyl-CoA synthetase. O'Connor-McCourt MD; Bridger WA Can J Biochem Cell Biol; 1985 Jan; 63(1):57-63. PubMed ID: 3886104 [TBL] [Abstract][Full Text] [Related]
14. Fluorescence detection of increased local flexibility induced by coenzyme A in succinyl-coA synthetase from Escherichia coli. Prasad AR; Nishimura JS; Horowitz PM Biochemistry; 1982 Oct; 21(21):5142-7. PubMed ID: 6756468 [No Abstract] [Full Text] [Related]
15. Capacity for alternating sites cooperativity in catalysis by succinyl-coenzyme A synthetase. Wolodko WT; O'Connor MD; Bridger WA Proc Natl Acad Sci U S A; 1981 Apr; 78(4):2140-4. PubMed ID: 7017725 [TBL] [Abstract][Full Text] [Related]
16. Thiophosphorylation as a probe for subunit interactions in Escherichia coli succinyl coenzyme A synthetase. Further evidence for catalytic cooperativity and substrate synergism. Wolodko WT; Brownie ER; O'Connor MD; Bridger WA J Biol Chem; 1983 Dec; 258(23):14116-9. PubMed ID: 6358215 [TBL] [Abstract][Full Text] [Related]
17. Kinetic and magnetic resonance studies of the role of metal ions in the mechanism of Escherichia coli GDP-mannose mannosyl hydrolase, an unusual nudix enzyme. Legler PM; Lee HC; Peisach J; Mildvan AS Biochemistry; 2002 Apr; 41(14):4655-68. PubMed ID: 11926828 [TBL] [Abstract][Full Text] [Related]
18. Chemical modification of tryptophan residues in Escherichia coli succinyl-CoA synthetase. Effect on structure and enzyme activity. Ybarra J; Prasad AR; Nishimura JS Biochemistry; 1986 Nov; 25(22):7174-8. PubMed ID: 3542020 [TBL] [Abstract][Full Text] [Related]
19. Succinyl-CoA synthetase structure-function relationships and other considerations. Nishimura JS Adv Enzymol Relat Areas Mol Biol; 1986; 58():141-72. PubMed ID: 3521216 [No Abstract] [Full Text] [Related]
20. Regulation of Escherichia coli glutamine synthetase. Evidence for the action of some feedback modifiers at the active site of the unadenylylated enzyme. Dahlquist FW; Purich DL Biochemistry; 1975 May; 14(9):1980-9. PubMed ID: 235974 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]