Ultrasensitive glycogen synthesis in Cyanobacteria.
Cyanobacter ADPglucose pyrophosphorylase exhibits a ultrasensitive response in activity towards its allosteric effector 3-phosphoglycerate, elicited by orthophosphate and polyethyleneglycol-induced molecular crowding. The ultrasensitive response was observed either when the enzyme operates in the zero or first order region for its physiological substrates. The ultrasensitivity exhibited maximal amplification factors of 15-19-fold with respect to 1% of the maximal system velocity. Only a 2.4-3.8-fold increase in 3PGA concentration was necessary to augment the flux from 10% to 90% through AGPase as compared with 200-fold required for the control. The results are discussed in terms of finely tuned regulatory mechanisms of polysaccharide synthesis in oxygenic photosynthetic organisms.
Gómez Casati
D F
DF
Instituto Tecnológico de Chascomús (INTECH-CONICET), Argentina.
Aon
M A
MA
Iglesias
A A
AA
D001426:Bacterial Proteins / Q000378:metabolism; D000458:Cyanobacteria / Q000378:metabolism*; D051599:Glucose-1-Phosphate Adenylyltransferase; D005988:Glyceric Acids / Q000494:pharmacology*; D006003:Glycogen / Q000096:biosynthesis*; D009713:Nucleotidyltransferases / Q000378:metabolism*; D011994:Recombinant Proteins / Q000096:biosynthesis
D001426:Bacterial Proteins; D005988:Glyceric Acids; D011994:Recombinant Proteins; C005156:3-phosphoglycerate; D006003:Glycogen; D009713:Nucleotidyltransferases; D051599:Glucose-1-Phosphate Adenylyltransferase