Enzyme-enzyme interaction in the chloroplast: glyceraldehyde-3-phosphate dehydrogenase, triose phosphate isomerase and aldolase.
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 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.
Anderson
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LE
Department of Biological Sciences, University of Illinois at Chicago 60607-7060, USA.
Goldhaber-Gordon
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IM
Li
D
D
Tang
X Y
XY
Xiang
M
M
Prakash
N
N
D000595:Amino Acid Sequence; D000818:Animals; D002736:Chloroplasts / Q000201:enzymology*; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D003377:Countercurrent Distribution; D005634:Fructose-Bisphosphate Aldolase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008969:Molecular Sequence Data; D018532:Pisum sativum / Q000201:enzymology*; D017386:Sequence Homology, Amino Acid; D014305:Triose-Phosphate Isomerase / Q000302:isolation & purification / Q000378:metabolism*
D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D005634:Fructose-Bisphosphate Aldolase; D014305:Triose-Phosphate Isomerase