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Organic Chemistry; Organic Chemistry Study Guide A Format: Kit/package/shrinkwrap
8th Edition
ISBN: 9780134581064
Author: Bruice, Paula Yurkanis
Publisher: Prentice Hall
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Question
Chapter 22.13, Problem 27P
Interpretation Introduction
Interpretation: The reason why during glycolysis,
Concept introduction:
- Enzyme is a protein that is a biological catalyst. The reactant in a reaction catalyzed by the enzyme is called substrate. In the enzyme, a pocket like cleft is present called active site where it binds the substrate.
- Some amino acid chains in the enzyme act as base, acid and nucleophilic catalyst. Many of the enzymes contain metal ions at the active site which acts as catalyst.
- Acid Catalyst helps in increasing the rate of a particular reaction by the donation of a proton to substrate.
- Base Catalyst helps in increasing the rate of a particular reaction by the removal of a proton to substrate.
- Nucleophilic catalysis helps in increasing the rate of a particular reaction by the formation of a covalent bond with substrate
- Glycolysis: A series of reactions where glucose is converted to two pyruvate molecules in the presence of enzymes catalysis.
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Students have asked these similar questions
sketch the nature of the metal-alkylidene bonding interactions.
Part C
The perspective formula of isoleucine, an amino acid, is provided below.
HOOC
H₂NIC
H
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CH3
CH,CH3
Draw the Newman projection in staggered conformation for isoleucine by viewing the molecule along the
C-2-C-3 bond.
1. Edit the Newman projection on the canvas.
2. Replace the appropriate hydrogens with the appropriate -CH3 or other groups.
3. If you need to start over, Undo or choose a Newman projection from the Templates toolbar
(bottom).
Important: Never delete the hydrogen atoms or bonds directly attached to the template, and do not move
them by dragging or dropping them. That will break the projections structures. Only replace them!
▸ View Available Hint(s)
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Chapter 22 Solutions
Organic Chemistry; Organic Chemistry Study Guide A Format: Kit/package/shrinkwrap
Ch. 22.2 - Compare each of the mechanisms listed here with...Ch. 22.2 - Prob. 3PCh. 22.2 - Prob. 4PCh. 22.3 - a. Draw the mechanism for the following reaction...Ch. 22.5 - Prob. 7PCh. 22.5 - Propose a mechanism for the Co2+ catalyzed...Ch. 22.6 - Prob. 9PCh. 22.7 - Prob. 10PCh. 22.7 - Prob. 12PCh. 22.7 - Prob. 13P
Ch. 22.9 - Which of the following amino acid side chains can...Ch. 22.9 - Which of the following C-terminal peptide bonds is...Ch. 22.9 - Carboxypeptidase A has esterase activity as well...Ch. 22.10 - Arginine and lysine side chains fit into trypsins...Ch. 22.10 - Explain why serine proteases do not catalyze...Ch. 22.11 - If H2 18O is used in the hydrolysis reaction...Ch. 22.11 - Draw the pH-activity profile for an enzyme that...Ch. 22.12 - The pHactivity profile for glucose-6-phosphate...Ch. 22.12 - Prob. 23PCh. 22.13 - Draw the mechanism for the hydroxide ion-catalyzed...Ch. 22.13 - What advantage does the enzyme gain by forming an...Ch. 22.13 - Prob. 26PCh. 22.13 - Prob. 27PCh. 22.13 - Aldolase shows no activity if it is incubated with...Ch. 22 - Which of the following parameters would be...Ch. 22 - Prob. 29PCh. 22 - Prob. 30PCh. 22 - Prob. 31PCh. 22 - Indicate the type of catalysis that is occurring...Ch. 22 - The deuterium kinetic isotope effect (KH2O/KD2O)...Ch. 22 - Prob. 34PCh. 22 - Co2+ catalyzes the hydrolysis of the lactam shown...Ch. 22 - there are two kinds of aldolases. Class I...Ch. 22 - Prob. 37PCh. 22 - The hydrolysis of the ester shown here is...Ch. 22 - Prob. 39PCh. 22 - At pH = 12, the rate of hydrolysis of ester A is...Ch. 22 - 2-Acetoxycyclohexyl tosylate reacts with acetate...Ch. 22 - Proof that an imine was formed between aldolase...Ch. 22 - Prob. 43PCh. 22 - a. Explain why the alkyl halide shown here reacts...Ch. 22 - Triosephosphate isomerase (TIM) catalyzes the...
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