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Journal Abstract Search

188 related items for PubMed ID: 4403555

  • 1. [Effect of effectors and substrate regulating the inactivation of glutamine synthetase from Escherichia coli: conformation changes of ATP:glutamine synthetase-adenylyltransferase].
    Wolf D, Ebner E.
    Hoppe Seylers Z Physiol Chem; 1972 May; 353(5):770-1. PubMed ID: 4403555
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  • 2. Studies on the reaction mechanism of adenosine triphosphate: glutamine synthetase adenylyltransferase from Escherichia coli B. Conformational changes elicited by effectors and substrates: reactivity of sulfhydryl groups.
    Wolf DH, Ebner E.
    J Biol Chem; 1972 Jul 10; 247(13):4208-12. PubMed ID: 4402512
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  • 5. Studies on the reaction mechanism of adenosine triphosphate: glutamine synthetase adenylyltransferase from Escherichia coli B. Evidence for an ordered mechanism.
    Wohlhueter RM, Ebner E, Wolf DH.
    J Biol Chem; 1972 Jul 10; 247(13):4213-8. PubMed ID: 4402513
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  • 6. Equilibrium of the ATP: glutamine synthetase adenyltransferase reaction.
    Eur J Biochem; 1971 Aug 25; 21(4):575-81. PubMed ID: 4398630
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  • 8. Enzymological characterization of the signal-transducing uridylyltransferase/uridylyl-removing enzyme (EC 2.7.7.59) of Escherichia coli and its interaction with the PII protein.
    Jiang P, Peliska JA, Ninfa AJ.
    Biochemistry; 1998 Sep 15; 37(37):12782-94. PubMed ID: 9737855
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  • 11. [Adenylylation and desadenylylation of glutamine synthetase in intact E. coli cells].
    Schutt H, Wohlhueter R, Holzer H.
    Hoppe Seylers Z Physiol Chem; 1972 Oct 15; 353(10):1568-9. PubMed ID: 4405474
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  • 12. ATP: glutamine synthetase adenylyltransferase from Escherichia coli B. Purification and properties.
    Ebner E, Wolf D, Gancedo C, Elsässer S, Holzer H.
    Eur J Biochem; 1970 Jul 15; 14(3):535-44. PubMed ID: 4920894
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  • 16. Formation of pyrophosphate during ATP: glutamine synthetase-adenylyltransferase-reaction in E. coli.
    Heinrich CP, Battig FA, Mantel M, Holzer H.
    Arch Mikrobiol; 1970 Jul 15; 73(2):104-10. PubMed ID: 4321114
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  • 17. Some kinetics of the interaction of divalent cations with glutamine synthetase from Escherichia coli. Metal ion induced conformational changes.
    Hunt JB, Ginsburg A.
    Biochemistry; 1972 Sep 26; 11(20):3723-35. PubMed ID: 4403683
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  • 18. Adenosine triphosphate: glutamine synthetase adenylyltransferase of Escherichia coli: two active molecular forms.
    Hennig SB, Anderson WB, Ginsburg A.
    Proc Natl Acad Sci U S A; 1970 Dec 26; 67(4):1761-8. PubMed ID: 4923119
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  • 19. Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase.
    Xu Y, Zhang R, Joachimiak A, Carr PD, Huber T, Vasudevan SG, Ollis DL.
    Structure; 2004 May 26; 12(5):861-9. PubMed ID: 15130478
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  • 20. In situ inactivation of E. coli uridylylation cycle is independent of the state of covalent modification of the components of the glutamine synthetase cascade.
    Mura U, Ceccherelli M, Gini S.
    Arch Biochem Biophys; 1982 Dec 26; 219(2):366-70. PubMed ID: 6131644
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