120:360 Biochemistry (Fall 2021) LAST NAME, FIRST NAME LAST NAME, FIRST NAMEMetabolic

120:360 Biochemistry (Fall 2021)

LAST NAME, FIRST NAME

LAST NAME, FIRST NAMEMetabolic Pathways Homework

Due: November 23, 11:50 P.M.                Student Name 

Extra credit, 5 % towards final grade.

(Insert rows if necessary)

Glycolysis

Enzyme

EC

Reaction

ΔGo’ (kJ/mol)

Cofactors

Regulation

Notes

Fructose-bisphosphate aldolase

4.1.2.13

D-fructose 1,6-bisphosphate = glycerol phosphate + D-glyceraldehyde 3-phosphate

 +8.23

Zinc (bacterial and yeast enzymes)

Ribulose 1,5-bisphosphate (RuBP)

This enzyme also acts on (3S,4R)-ketose 1-phosphates. The yeast and bacterial enzymes are zinc proteins. The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it; others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. Zn2+.

Gluconeogenesis (work only on the enzymes that are not shared with the glycolytic pathway)

Enzyme

EC

Reaction

ΔGo’ (kJ/mol)

Cofactors

Regulation

Notes

Tricarboxylic Acid Cycle (include pyruvate dehydrogenase complex) = KREBS

Enzyme

EC

Reaction

ΔGo’ (kJ/mol)

Cofactors

Regulation

Notes

Pyruvate dehydrogenase complex

1.2.4.1

Pyruvate Acetyl-S-CoA + CO2

–33.4

Lipoic acid, thiamine pyrophosphate, FAD, NAD+, Coenzyme A.

Inhibited by NADH + H+, ATP, acetyl-S-CoA.

Stimulated by NAD+, AMP and coenzyme A

PDH deficiency: ataxia, poor muscle tone, high lactate, etc. (GHR, 2012)

Pentose-Phosphate Pathway

Enzyme

EC

Reaction

ΔGo’ (kJ/mol)

Cofactors

Regulation

Notes

Calvin-Benson Cycle

Enzyme

EC

Reaction

ΔGo’ (kJ/mol)

Cofactors

Regulation

Notes

Ribulose-1,5-bisphosphate carboxylase oxygenase

4.1.1.39

Ribulose-1,5-bisphosphate + CO2 + H2O
2 (3-phosphoglycerate) + H+

Ribulose-1,5-bisphosphate + O2 + H2O
3-phosphoglycerate +
2-phosphoglycolate + H+

+70.0

Mg2+, cobalamin (B12), coenzyme-A, NADH + H+, Fe-S clusters, and possibly ATP

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

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)

References → USE ANY STYLE APA, Chicago, ASPB, etc. JUST BE CONSISTENT
Here is an example with the references I used in my notes:

Feller U, Anders I, Mae T (2008) Rubiscolytics: Fate of Rubisco after its enzymatic function in a cell is terminated. J Exp Bot 59:1615-1624

Genetics Home Reference (2012) Pyruvate dehydrogenase deficiency. Downloaded 2Apr19 from https://ghr.nlm.nih.gov/condition/pyruvate-dehydrogenase-deficiency