Evidence for an arginine residue at the allosteric sites of spinach leaf ADPglucose pyrophosphorylase

K L Ball, J Preiss

Research output: Contribution to journalArticlepeer-review

Abstract

The covalent modification of spinach leaf ADPglucose pyrophosphorylase leads to inactivation of both activator-stimulated and -unstimulated activity. Inactivation can be prevented if either the activator 3PGA or the inhibitor Pi are present during the modification. Pi proved to be more effective at protecting the enzyme from inactivation as it afforded 50% protection at 51 microM compared to 50% protection by 405 microM 3PGA. Partial modification of the enzyme using [14C]-phenylglyoxal leads to a decrease in both Vmax, A0.5 and a decrease in the ability of the 3PGA to stimulate the enzyme's activity. Modification increased the enzyme's susceptibility to inhibition by Pi and completely abolished the cooperative binding of Pi seen in the unmodified enzyme in the presence of 3PGA. Thus, phenylglyoxal appears to interfere, with the normal allosteric regulation of ADPglucose pyrophosphorylase from spinach leaf. Greater than 90% of the enzyme's activity is lost when 7.2 mol [14C]-phenylglyoxal are bound per mole of tetramer and this label is present in both the larger and small subunits. In addition, inactivation appears to involve two different arginine residues having different rates of modification.
Original languageEnglish
Pages (from-to)231-8
Number of pages8
JournalJournal of protein chemistry
Volume11
Issue number3
Publication statusPublished - Jun 1992

Keywords

  • Allosteric Site
  • Arginine
  • Electrophoresis, Polyacrylamide Gel
  • Glucose-1-Phosphate Adenylyltransferase
  • Kinetics
  • Nucleotidyltransferases
  • Phenylglyoxal
  • Phosphates
  • Plants
  • Substrate Specificity

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