INVESTIGADORES
IGLESIAS Alberto Alvaro
artículos
Título:
Involvement of Arginine Residues in the Allosteric Activation and Inhibition of Synechocystis PCC 6803 ADPglucose Pyrophosphorylase
Autor/es:
A.A. IGLESIAS, G. KAKEFUDA, J. PREISS
Revista:
JOURNAL OF PROTEIN CHEMISTRY
Referencias:
Año: 1992 vol. 11 p. 119 - 128
ISSN:
0277-8033
Resumen:
J Protein Chem. 1992 Apr;11(2):119-28.
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-->LinksInvolvement
of arginine residues in the allosteric activation and inhibition of
Synechocystis PCC 6803 ADPglucose pyrophosphorylase.Iglesias AA, Kakefuda G, Preiss J.Department of Biochemistry, Michigan State University, East Lansing 48824.ADPglucose
pyrophosphorylase (EC 2.7.7.27) from the cyanobacterium Synechocystis
PCC 6803 was desensitized to the effects of allosteric ligands by
treatment with the arginine reagent, phenylglyoxal. Enzyme modification
by phenylglyoxal resulted in inactivation when the enzyme was assayed
under 3P-glycerate-activated conditions. There was little loss of the
catalytic activity assayed in the absence of activator. Pi,
3P-glycerate, and pyridoxal-P were able to protect the enzyme from
inactivation, whereas substrates gave minimal protection. The
protective effect exhibited by Pi and 3P-glycerate was dependent on
effector concentration. MgCl2 enhanced the protection afforded by
3P-glycerate. The enzyme partially modified by phenylglyoxal was more
resistant to 3P-glycerate activation and Pi inhibition than the
unmodified form. Vmax at saturating 3P-glycerate concentrations and the
apparent affinity of the enzyme toward Pi were decreased upon
phenylglyoxal modification. Incorporation of labeled phenylglyoxal into
the enzyme was proportional to the loss of activity. Pi and
3P-glycerate nearly completely prevented incorporation of the reagent
to the protein. Results suggest that one arginine residue per mol of
enzyme subunit is involved in the binding of allosteric effector in the
cyanobacterial ADPglucose pyrophosphorylase.