@article{67f1bb98e54b429c9a834df7488d0795,
title = "Domain Swapping between a Cyanobacterial and a Plant Subunit ADP-Glucose Pyrophosphorylase",
author = "Iglesias, {Alberto A.} and Ballicora, {Miguel A.} and Sesma, {Juliana I.} and Jack Preiss",
note = "ADP-glucose pyrophosphorylase (ADP-Glc PPase) catalyzes the regulatory step in the pathway for synthesis of bacterial glycogen and starch in plants. ADP-Glc PPases from cyanobacteria (homotetramer) and from potato (Solanum tuberosum) tuber (heterotetramer) are activated by 3-phosphoglycerate and inhibited by inorganic orthophosphate. To study the function of two putative domains, chimeric enzymes were constructed.",
year = "2006",
month = apr,
day = "1",
doi = "10.1093/pcp/pcj021",
language = "American English",
volume = "47",
journal = "Plant and Cell Physiology",
issn = "1471-9053",
number = "4",
}