ISSN:
1432-2048
Keywords:
Aldolase
;
Enzyme-enzyme interaction
;
Glyceraldehyde-3-phosphate dehydrogenase
;
Pisum (chloroplastic enzymes)
;
Substrate channeling
;
Triosephosphate isomerase
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract Apparent physical interaction between pea chloroplast (Pisum sativum L.) glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.13) and aldolase (EC 4.1.2.13) is seen in phase-partitioning, fluorescent-anisotropy and isoelectric-focusing experiments. Similarly, results obtained in phase-partitioning and isoelectric-focusing experiments indicate physical interaction between aldolase and triose-phosphate isomerase (EC 5.3.1.1). Kinetic experiments suggest that both aldolase-bound glyceraldehyde-3-phosphate and triose-phosphate isomerase bound glyceraldehyde-3-phosphate can act as substrate for glyceraldehyde-3-phosphate dehydrogenase. These results are consistent with the notion that there is interaction between these three enzymes both during photosynthetic CO2 fixation and during glycolysis in the chloroplast.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00201381
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