Acetyl-CoA; CO2; ATP; NADH; [FADH2]
Malonyl-CoA; water; NADH; [FADH2]; ATP
succinyl-CoA; CO2; ATP; NADH; NADPH
acetyl-CoA; CO2; NADH; ATP; NADPH
Malonate; water; NADH; ATP; NADPH
Dehydration; pyruvate dehydration complex
Decarboxylation; pyruvate dehydrogenase complex
Decarboxylation; pyruvate decarboxylase
Transacylation; pyruvate transacylase
none of the above.
It uses thiamin pyrophosphate as a catalytic coenzyme.
It oxidatively decarboxylates pyruvate.
It binds NAD+ in its active site.
It transfers an acetyl group to lipoamide of ETA.
It forms a hydroxyethyl-TPP intermediate.
it is the link between glycolysis and the TCA cycle
The activity of the complex is regulated by the phosphorylation of EPDH.
NAD+ is the direct oxidant of reduced lipoamide.
An FAD is covalently linked to the EDLD, the lipoamide dehydrogenase component.
Although EPDH is called "pyruvate dehydrogenase" it is not a dehydrogenase.
A, B, C, D, E
C, B, A, E, D
C, D, B, E, A
B, D, E, A, C
C, E, D, B, A
Citrate synthase is allosterically activated by ATP.
The complete chemical equation is: Oxaloacetate + acetyl-CoA + H2O -> citrate + CoA
Citryl-CoA is formed as an intermediate.
The mechanism involves attack of the carbanion of acetyl-CoA on the carbonyl carbon of oxaloacetate.
The enzyme uses general base catalysis to generate the reactive species.
Large positive; reversible; oxidation
Nearly zero; reversible; reduction
Nearly zero; irreversible; reduction
large negative; irreversible; hydrolysis
Large negative; reversible; hydrolysis
Dimer; OAA; increasing; NADH
Dimer; OAA; decreasing; NADH
Tetramer; OAA; decreasing; NAD+
Monomer; pyruvate; decreasing; ATP
Monomer; pyruvate; increasing; ATP
It catalyzes the first reaction in the TCA cycle
It is not regulated
OAA and acetyl-CoA bind to the active sites
The citrate synthase reaction liberates a relatively large amount of energy
All of the above are true
Ketone; primary alcohol
Tertiary alcohol; secondary alcohol
Ketone; secondary alcohol
Aldehyde; primary alcohol
Secondary alcohol; ketone
Citrate isomerase; CO2; trans-aconitate; carboxylation
Citrate isomerase; water; trans-aconitate; rehydration
Aconitase; water; cis-aconitate; rehydration
Aconitase; CO2; cis-aconitate; carboxylation
None are true
Iron atom acts as a Lewis acid.
Equilibrium favors citrate.
Contains an iron-sulfur cluster.
One Fe3+ coordinates with C-3 carbonyl and hydroxyl group of citrate.
All are true.
malate dehydrogenase and citrate synthase
Fumarase and succinate dehydrogenase
A-ketoglutarate dehydrogenase and succinate dehydrogenase
Isocitrate dehydrogenase and a-ketoglutarate dehydrogenase
aconitase and succinate dehydrogenase
A and B
B and C
C and D
A and C
B and D
ATP; NADH; ADP; lowering
ATP; ADP; AMP; lowering
NADH; NADPH; AMP; increasing
NADH; ATP; ADP; increasing
NADH; ATP; AMP; lowering
ADP raises the Km for isocitrate by a factor of 10.
Virtually inactive in the absence of ADP.
Sufficiently exergonic to pull the aconitase reaction forward.
Allosterically inhibited by NADH and ATP.
An oxidative-decarboxylation reaction.
Nucleotide triphosphate kinase.
Succinyl-CoA can be used to drive phosphorylation of GDP or ADP.
The enzyme is named for the reverse reaction.
it provides an example of substrate-level phosphorylation.
Succinyl-phosphate is an intermediate in the reaction catalyzed by succinyl-CoA synthetase.
All of the above are true.
A, B, C
B, C, A
A, C, D
C, B, A
D, A, B
It is also known as succinate-Coenzyme Q reductase.
It has covalently bound FAD.
It is a membrane-bound enzyme.
It removes hydrogens from C-O bonds.
it carries out either 1-electron or 2-electron transfers to/from FAD.
Oxidation; reduction of NAD+
Reduction; oxidation of NAD+
Oxidation; reduction of [FAD]
Reduction; oxidation of [FAD]
None are true