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Calvin-Benson Cycle EC Ribulose-1,5-bisphosphate carboxylase 4.1.1.39 oxygenase Enzyme Phosphoglyderate Kinase glyceraldehyde 3-phosphate dehydrogenase Triose phosphate Isomerase aldolase Transketolase Phophopentose Isomerase Phosphopentose epimerase phosphoribulokinease 2.7.2.3 1.2.1.12 5.3.1.1 4.1.2.13 2.2.1.1 5.1.3.1 5.1.3.1 2.7.1.19 AG (kJ/mol) Ribulose-1,5-bisphosphate + +70.0 Reaction |CO,+H,O 2(3-phosphoglycerate) +H* Ribulose-1,5-bisphosphate + O₂ + H₂O → 3-phosphoglycerate + 2-phosphoglycolate+H* Cofactors Mg, cobalamin (B₁₂), coenzyme-A, NADH+H* Fe-S clusters, and possibly ATP Regulation Ribulose-1,5-bisphosphate (RuBP) behaves as an inhibitor by strongly binding to the activated form of the enzyme (ECM) Rubisco activase catalyzes the dissociation of RuBP from ECM Notes Rubisco is very inefficient as a carboxylase Photosynthetic efficiency is also reduced if the enzyme acts as an oxygenase It is probably the most abundant protein on earth; up to 50% of leaf protein is rubisco (Feller et al., 2008)

Calvin-Benson Cycle EC Ribulose-1,5-bisphosphate carboxylase 4.1.1.39 oxygenase Enzyme Phosphoglyderate Kinase glyceraldehyde 3-phosphate dehydrogenase Triose phosphate Isomerase aldolase Transketolase Phophopentose Isomerase Phosphopentose epimerase phosphoribulokinease 2.7.2.3 1.2.1.12 5.3.1.1 4.1.2.13 2.2.1.1 5.1.3.1 5.1.3.1 2.7.1.19 AG (kJ/mol) Ribulose-1,5-bisphosphate + +70.0 Reaction |CO,+H,O 2(3-phosphoglycerate) +H* Ribulose-1,5-bisphosphate + O₂ + H₂O → 3-phosphoglycerate + 2-phosphoglycolate+H* Cofactors Mg, cobalamin (B₁₂), coenzyme-A, NADH+H* Fe-S clusters, and possibly ATP Regulation Ribulose-1,5-bisphosphate (RuBP) behaves as an inhibitor by strongly binding to the activated form of the enzyme (ECM) Rubisco activase catalyzes the dissociation of RuBP from ECM Notes Rubisco is very inefficient as a carboxylase Photosynthetic efficiency is also reduced if the enzyme acts as an oxygenase It is probably the most abundant protein on earth; up to 50% of leaf protein is rubisco (Feller et al., 2008)

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
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Please help to fill out the table of the metabolic pathway of Calvin-Benson Cycle 

Calvin-Benson Cycle Enzyme EC Ribulose-1,5-bisphosphate carboxylase 4.1.1.39 oxygenase Phosphoglyderate Kinase glyceraldehyde 3-phosphate dehydrogenase Triose phosphate Isomerase aldolase Transketolase Phophopentose Isomerase Phosphopentose epimerase phosphoribulokinease 2.7.2.3 1.2.1.12 5.3.1.1 4.1.2.13 2.2.1.1 5.1.3.1 5.1.3.1 2.7.1.19 ΔG" Reaction (kJ/mol) Ribulose-1,5-bisphosphate + +70.0 |CO,+H2O 2(3-phosphoglycerate) +H* Ribulose-1,5-bisphosphate + O₂ + H₂O → 3-phosphoglycerate + 2-phosphoglycolate+H* Cofactors 1 Mg cobalamin (B₁₂). coenzyme-A, NADH+H. Fe-S clusters, and possibly ATP Regulation Ribulose-1,5-bisphosphate (RuBP) behaves as an inhibitor by strongly binding to the activated form of the enzyme (ECM) Rubisco activase catalyzes the dissociation of RuBP from ECM Notes Rubisco is very inefficient as a carboxylase Photosynthetic efficiency is also reduced if the enzyme acts as an oxygenase It is probably the most abundant protein on earth; up to 50% of leaf protein is rubisco (Feller et al., 2008)
Transcribed Image Text:Calvin-Benson Cycle Enzyme EC Ribulose-1,5-bisphosphate carboxylase 4.1.1.39 oxygenase Phosphoglyderate Kinase glyceraldehyde 3-phosphate dehydrogenase Triose phosphate Isomerase aldolase Transketolase Phophopentose Isomerase Phosphopentose epimerase phosphoribulokinease 2.7.2.3 1.2.1.12 5.3.1.1 4.1.2.13 2.2.1.1 5.1.3.1 5.1.3.1 2.7.1.19 ΔG" Reaction (kJ/mol) Ribulose-1,5-bisphosphate + +70.0 |CO,+H2O 2(3-phosphoglycerate) +H* Ribulose-1,5-bisphosphate + O₂ + H₂O → 3-phosphoglycerate + 2-phosphoglycolate+H* Cofactors 1 Mg cobalamin (B₁₂). coenzyme-A, NADH+H. Fe-S clusters, and possibly ATP Regulation Ribulose-1,5-bisphosphate (RuBP) behaves as an inhibitor by strongly binding to the activated form of the enzyme (ECM) Rubisco activase catalyzes the dissociation of RuBP from ECM Notes Rubisco is very inefficient as a carboxylase Photosynthetic efficiency is also reduced if the enzyme acts as an oxygenase It is probably the most abundant protein on earth; up to 50% of leaf protein is rubisco (Feller et al., 2008)
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