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
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
Problem 1P
icon
Related questions
Question

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)
Expert Solution
steps

Step by step

Solved in 3 steps

Blurred answer
Similar questions
  • SEE MORE QUESTIONS
Recommended textbooks for you
Biochemistry
Biochemistry
Biochemistry
ISBN:
9781319114671
Author:
Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:
W. H. Freeman
Lehninger Principles of Biochemistry
Lehninger Principles of Biochemistry
Biochemistry
ISBN:
9781464126116
Author:
David L. Nelson, Michael M. Cox
Publisher:
W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul…
Fundamentals of Biochemistry: Life at the Molecul…
Biochemistry
ISBN:
9781118918401
Author:
Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:
WILEY
Biochemistry
Biochemistry
Biochemistry
ISBN:
9781305961135
Author:
Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:
Cengage Learning
Biochemistry
Biochemistry
Biochemistry
ISBN:
9781305577206
Author:
Reginald H. Garrett, Charles M. Grisham
Publisher:
Cengage Learning
Fundamentals of General, Organic, and Biological …
Fundamentals of General, Organic, and Biological …
Biochemistry
ISBN:
9780134015187
Author:
John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:
PEARSON