(a)
Interpretation:
Standard free energy change for the pyruvate kinase reaction should be calculated.
Concept Introduction:
In a cell, ATP is one of the major energies. By decarboxylating of the oxaloacetate and hydrolyzing the guanosine triphosphate, PEP is formed. PEP is abbreviated as Phosphoenolpyruvate.
The energy which is used to do work at given pressure and at given temperature especially at 1 bar and 298K respectively is called standard free energy change.
(b)
Interpretation:
Equilibrium constant for the given reaction should be calculated.
Concept Introduction:
In a cell, ATP is one of the major energies. By decarboxylating of the oxaloacetate and hydrolyzing the guanosine triphosphate, PEP is formed. PEP is abbreviated as Phosphoenolpyruvate.
When the reactants and products don’t have any change in the particular time, then it is called equilibrium constant. It is denoted as K
(c)
Interpretation:
Ratio of
Introduction:
In a cell, ATP is one of the major energies. By decarboxylating of the oxaloacetate and hydrolyzing the guanosine triphosphate, PEP is formed. PEP is abbreviated as Phosphoenolpyruvate.
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Biochemistry
- M-CSA Mechanism and Catalytic Site Atlas (ebi.ac.uk) (ii) Acyl Carrier Protein S-acetyltransferase (EC 2.3.1.38) is a transferase enzyme that catalyzes the first biosynthetic pathway for fatty acid synthase. It transfers the acyl group (CH3CO) first from coenzyme A to a cysteine residue in the active site. This is similar to what happens in Chymotrypsin, however utilizing a sulfur instead of an oxygen. The acyl group is then transferred to the molecule ACP. Provide the enzyme- catalyzed mechanism for the reaction below, making sure to identify the roles of all key amino acids: i H3C SCOA acetyl COA enzyme + HS i H3C SACP acetyl ACParrow_forwardWhat is the catalytic efficiency of Catalase ? Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Carbonic anhydrase Substrate CO2 HCO3 KM (M) 1.2 x 10-2 2.6 x 10-2 Kcat (s-1) 1.0 x 106 4.0 x 105 Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 O A. 4 x 108 M-s-1 O B. 4 x 108 M-1.s-1 OC25x 10-9 M-s1 D. 2.5 x 102 M-1.s-1 OE 1.0 x 107 s1arrow_forwardPlease answer fast The equilbrium constant (Keq) under standard conditions for the hydrolysis of ATP is 200,000 M. This would suggest the reaction is: 1. proceeding in reverse direction 2. proceeding in forward direction 3. in equilibrium However, this does not take into consideration the concentration of substrates/products within the cell. This is can be calculated by determining the reaction quotient, Q by: [ATP] x [Pi] / [ADP] [ATP] + [Pi] / [ADP] [ADP] x [ATP] / [Pi] [ADP] x [Pi] / [ATP] Biochemical reactions commonly involve the transfer of groups from ATP. What is one of the products of pyrophosphate cleavage from ATP? AMP Adenosine ADP Inorganic phosphate Q5-6. The hydrolysis of ATP is often coupled to other reactions. For example: Phosphoenolpyruvate (PEP) + H2O → Pyruvate + Pi (ΔG'° = -63.1 kJ/mol) ATP + H2O → ADP + Pi (ΔG'° = -30.5 kJ/mol) (The standard free-energy changes for the reactions are indicated in brackets) Q5. Given the information above, what is the…arrow_forward
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