Journal of Protein Chemistry

, Volume 13, Issue 2, pp 177–185 | Cite as

Regulatory role of GDP in the phosphoenzyme formation of guanine nucleotide: Specific forms of succinyl coenzyme a synthetase

  • Hong-Duck Um
  • Claudette Klein
Article

Abstract

We have previously shown that micromolar concentrations of GDP stimulate the GTP-mediated phosphorylation of p36, theα subunit of succinyl-CoA synthetase (SCS), in lysates prepared fromDictyostelium discoideum. In this study, we report that this phenomenon represents an enhanced catalytic capacity of SCS to form the phosphoenzyme intermediate. Low concentrations of GDP stimulate phosphoenzyme formation by either GTP, or succinyl-CoA and Pi. Under these conditions GDP enhances the apparent rate of phosphoenzyme formation but does not significantly alter the fraction of phosphorylated enzyme. This effect is retained during purification of the protein and is also observed with purified pig heart SCS, indicating that GDP directly alters the enzyme to enhance its rate of phosphorylation. Under these conditions, GDP does not function at the catalytic site, implying an allosteric regulation of SCS.

Key words

GDP succinyl-CoA synthetase phosphoenzyme formation 

Abbreviations used

SCS

succinyl-CoA synthetase

Pi

inorganic phosphate

NDP

nucleotide diphosphate

NTP

nucleotide triphosphate

PFK

phosphofructokinase A-form; ADP-forming SCS; G-form; GDP-forming SCS

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Copyright information

© Plenum Publishing Corporation 1994

Authors and Affiliations

  • Hong-Duck Um
    • 1
  • Claudette Klein
    • 1
  1. 1.Department of Biochemistry and Molecular BiologySt. Louis University School of MedicineSt. Louis

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