Literature DB >> 3760857

Catalysis of the dephosphorylation of an ATP-molybdate complex by calcium and magnesium ions.

W T Jenkins, J S Patrick.   

Abstract

Calcium and magnesium catalyze the dephosphorylation of a molybdate complex of adenosine triphosphate but not the corresponding molybdate complex of adenosine disphosphate. We conclude that catalysis of breaking the bond between the beta and gamma phosphates involves metal chelation of the alpha and beta phosphates. ATP hydrolysis with calcium was stimulated by phosphate, apparently because of formation of a calcium-phosphomolybdate complex. The reaction with magnesium, which does not form a comparable complex, was not affected by phosphate. Strontium, cadmium, and barium behaved like calcium. The reactions with transition metal cations showed autoinhibition.

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Year:  1986        PMID: 3760857     DOI: 10.1016/0162-0134(86)80057-5

Source DB:  PubMed          Journal:  J Inorg Biochem        ISSN: 0162-0134            Impact factor:   4.155


  1 in total

1.  Molybdate pumping into the molybdenum storage protein via an ATP-powered piercing mechanism.

Authors:  Steffen Brünle; Martin L Eisinger; Juliane Poppe; Deryck J Mills; Julian D Langer; Janet Vonck; Ulrich Ermler
Journal:  Proc Natl Acad Sci U S A       Date:  2019-12-06       Impact factor: 11.205

  1 in total

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