Article
The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domains.
FEBS letters - 27 Aug 2004
Bejar Clarisa M, Ballicora Miguel A, Gómez-Casati Diego F, Iglesias Alberto A, Preiss Jack
Abstract excerpt
Computational analysis of ADP-glucose pyrophosphorylases predicts a fold with two domains. Co-expression of two polypeptides comprising residues 1-323 and 328-431 from the Escherichia coli ADP-glucose pyrophosphorylase yielded an enzyme form as active as the wild type. The only difference from the wild type was a slightly modified affinity for allosteric effectors. The two polypeptides could not be separated by...
Topics
- Allosteric Regulation
- Amino Acid Sequence
- Base Sequence
- Catalytic Domain
- Electrophoresis, Polyacrylamide Gel
- Escherichia coli
- Glucose-1-Phosphate Adenylyltransferase
- Kinetics
- Molecular Sequence Data
- Molecular Weight
- Mutation
- Nucleotidyltransferases
- Protein Structure, Secondary