BIOCHEM. II-EBOOK ACCESS>CUSTOM<
18th Edition
ISBN: 9781337700320
Author: GARRETT
Publisher: CENGAGE LEARNING (CUSTOM)
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Chapter 12, Problem 7P
Interpretation Introduction
Interpretation:
The sequence of the amino acid of the fusion protein is to be stated. Also, the junction between
Concept introduction:
The organic compounds that contain
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Students have asked these similar questions
9. Which one of the compounds below is the major organic product obtained from
the following reaction sequence, starting with ethyl acetoacetate?
요요.
1. NaOCH2CH3
CH3CH2OH
1. NaOH, H₂O
2. H3O+
3. A
OCH2CH3
2.
ethyl acetoacetate
ii
A
3. H3O+
OH
B
C
D
E
7. Only one of the following ketones cannot be made via an acetoacetic ester
synthesis. Which one is it?
Ph
کہ
A
B
C
D
E
2. Which one is the
major organic
product obtained
from the following
reaction sequence?
HO
A
OH
1. NaOEt, EtOH
1. LiAlH4
EtO
OEt
2. H3O+
2. H3O+
OH
B
OH
OH
C
-OH
HO
-OH
OH
D
E
.CO₂Et
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- Examine the metabolic pathway. The enzymes that catalyze each step are identified as "e" with a numeric subscript. e₁ e3 e4 A B с 1° B' 02 e5 e6 e7 E F Which enzymes catalyze irreversible reactions? ப e ez ☐ ez e4 ☐ ப es 26 5 e7 Which of the enzymes is likely to be the allosteric enzyme that controls the synthesis of G? €2 ез e4 es 26 5 e7arrow_forwardAn allosteric enzyme that follows the concerted model has an allosteric coefficient (T/R) of 300 in the absence of substrate. Suppose that a mutation reversed the ratio. Select the effects this mutation will have on the relationship between the rate of the reaction (V) and substrate concentration, [S]. ㅁㅁㅁ The enzyme would likely follow Michaelis-Menten kinetics. The plot of V versus [S] would be sigmoidal. The enzyme would mostly be in the T form. The plot of V versus [S] would be hyperbolic. The enzyme would be more active.arrow_forwardPenicillin is hydrolyzed and thereby rendered inactive by penicillinase (also known as ẞ-lactamase), an enzyme present in some penicillin-resistant bacteria. The mass of this enzyme in Staphylococcus aureus is 29.6 kDa. The amount of penicillin hydrolyzed in 1 minute in a 10.0 mL. solution containing 1.00 x 10 g of purified penicillinase was measured as a function of the concentration of penicillin. Assume that the concentration of penicillin does not change appreciably during the assay. Plots of V versus [S] and 1/V versus 1/[S] for these data are shown. Vo (* 10 M minute"¹) 7.0 6.0 5.0 4.0 3.0 20 1.0 0.0 о 10 20 30 1/Vo (* 10 M1 minute) 20 103 90 BO 70 50 [S] (* 100 M) 40 50 60 y=762x+1.46 × 10" [Penicillin] (M) Amount hydrolyzed (uM) 1 0.11 3 0.25 5 0.34 10 0.45 30 0.58 50 0.61arrow_forward
- Consider the four graphs shown. In each graph, the solid blue curve represents the unmodified allosteric enzyme and the dashed green curve represents the enzyme in the presence of the effector. Identify which graphs correctly illustrate the effect of a negative modifier (allosteric inhibitor) and a positive modifier (allosteric activator) on the velocity curve of an allosteric enzyme. Place the correct graph in the set of axes for each type of modifier. Negative modifier Reaction velocity - Positive modifier Substrate concentration - Reaction velocity →→→→ Substrate concentration Answer Bankarrow_forwardConsider the reaction: phosphoglucoisomerase Glucose 6-phosphate: glucose 1-phosphate After reactant and product were mixed and allowed to reach at 25 °C, the concentration of each compound at equilibrium was measured: [Glucose 1-phosphate] = 0.01 M [Glucose 6-phosphate] = 0.19 M Calculate Keq and AG°'. Код .0526 Incorrect Answer 7.30 AG°' kJ mol-1 Incorrect Answerarrow_forwardClassify each phrase as describing kinases, phosphatases, neither, or both. Kinases Phosphatases Neither Both Answer Bank transfer phosphoryl groups to acidic amino acids in eukaryotes may use ATP as a phosphoryl group donor remove phosphoryl groups from proteins catalyze reactions that are the reverse of dephosphorylation reactions regulate the activity of other proteins catalyze phosphorylation reactions PKA as an example turn off signaling pathways triggered by kinasesarrow_forward
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