PMID:9750179
| Citation |
Wu, MX and Preiss, J (1998) The N-terminal region is important for the allosteric activation and inhibition of the Escherichia coli ADP-glucose pyrophosphorylase. Arch. Biochem. Biophys. 358:182-8 |
|---|---|
| Abstract |
The ADPglucose pyrophosphorylase (EC 2.7.7.27) from Escherichia coli is allosterically activated by fructose 1,6-bisphosphate and inhibited by AMP. Proteolysis of the enzyme with proteinase K causes loss of activity and generates two peptides, 21 and 28 kDa, from the 49.7-kDa subunit. The presence of ADPglucose, Mg2+, and fructose 1, 6-bisphosphate during the incubation with proteinase K protected the enzyme activity and prevented cleavage at sites Met181-Ala182 and Phe192-Val193. Proteolysis of the protected enzyme removed 10 to 13 amino acids from the N-terminal and 2 amino acids from the C-terminal. The resulting enzyme was almost independent of the need for fructose 1,6-bisphosphate for maximal activity and insensitive to inhibition by AMP. The apparent affinity for the substrates was similar to that of the fully-activated wild-type enzyme. These data suggest that amino acid residues in the N-terminal portion and possibly the C-terminal portion of ADPglucose pyrophosphorylase are part of the regulatory domain of the enzyme, critical for allosteric regulation of the enzyme. |
| Links |
PubMed Online version:10.1006/abbi.1998.0846 |
| Keywords |
Allosteric Regulation; Amino Acid Sequence; Endopeptidase K/metabolism; Enzyme Activation/drug effects; Escherichia coli/enzymology; Glucose-1-Phosphate Adenylyltransferase; Hydrolysis; Kinetics; Magnesium/metabolism; Molecular Sequence Data; Nucleotidyltransferases/antagonists & inhibitors; Nucleotidyltransferases/isolation & purification; Nucleotidyltransferases/metabolism; Peptide Fragments/metabolism; Peptide Fragments/physiology; Substrate Specificity |
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