Biochemistry (Looseleaf)
9th Edition
ISBN: 9781319114800
Author: BERG
Publisher: MAC HIGHER
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Question
Chapter 8, Problem 2P
Interpretation Introduction
Interpretation:
The substance that is needed by an apoenzyme to become a holoenzyme is to be stated.
Concept introduction:
A type of an inactive enzyme whose activation depends upon the binding with another substance is known as apoenzyme. Another type of enzyme which can perform all the catalytic activities is known as holoenzyme.
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METABOLIC PATHWAYS. Carefully analyze the diagram below. Complete the diagram
below by providing the name of the pathway (in oblongs beside arrows), OR the product or
the precursor (rectangles). Choose your answer from the terms provided below. Write the
capital letters of your answer on the space provided. The same answer can be used more
than once.
starch
sucrose
lactose
19
20
18
glucose
gly cogen
glycogenoly sis
17
Urea
1
cycle
glucose
ribos
3
16
gluconeogenesis
glycolysis
some amino acids
4
lactic acid
amino acid catabolism
15
13
11
6
fats
12
acety FCOA
ketone bodi
14
fatty add
synthesis
A.glucose
B.fructose
TERM BANK
P. glycolysis
Q. glycogenolysis
C. galactose R. lipolys is
FAD
NAD+
S. ketogenesis
E. pyruvate T. B-oxidation
F.NADPH U. Kreb's cycle
G. FADH2 V. fermentation
W. glycogenesis
X. lipogenesis
J. glycerol Y.hydrolysis
Z. oxidation
AB. pentose phosphate
pathway
N. cellulose XY, electron transport
chain
D. urea
10
8
H. NADH
I. NH3
9.
K. H20
L. CO2
АТР
M. maltose
O. fatty…
Modified TRUE or FALSE. Write the word TRUE if the statement is correct. If the statement is false, write the incorrect underlined word/s and indicate the correct word/s to make the statement true.
Catabolic pathways synthesize complex end products from simple substrates and require energy use.
I. Active site analysis.
Below is a diagram of a putative active site for Monoamine oxidase. As we learned, the purpose of
tertiary structure is to form a scaffold so you can orient just a few amino acids in the right orientation
to promote binding and/or catalysis. The position where this occurs is the active site. The amino acid
architecture of an active site is designed to bind substrates. Amino acid side chains are capable of
hydrogen bonding, ionic and hydrophobic interactions. Fill in each amino acid that you think is
suitable for interacting with the part of the substrate it is closest to. Assume the pH will be at 7.0
a.a.#1
a.a.#2
a.a.#6
HO
Lond
NH₂
НО
a.a.#5
OH
a.a.#3
a.a.#4
Chapter 8 Solutions
Biochemistry (Looseleaf)
Ch. 8 - Prob. 1PCh. 8 - Prob. 2PCh. 8 - Prob. 3PCh. 8 - Prob. 4PCh. 8 - Prob. 5PCh. 8 - Prob. 6PCh. 8 - Prob. 7PCh. 8 - Prob. 8PCh. 8 - Prob. 9PCh. 8 - Prob. 10P
Ch. 8 - Prob. 11PCh. 8 - Prob. 12PCh. 8 - Prob. 13PCh. 8 - Prob. 14PCh. 8 - Prob. 15PCh. 8 - Prob. 16PCh. 8 - Prob. 17PCh. 8 - Prob. 18PCh. 8 - Prob. 19PCh. 8 - Prob. 20PCh. 8 - Prob. 21PCh. 8 - Prob. 22PCh. 8 - Prob. 23PCh. 8 - Prob. 24PCh. 8 - Prob. 25PCh. 8 - Prob. 26PCh. 8 - Prob. 27PCh. 8 - Prob. 28PCh. 8 - Prob. 29PCh. 8 - Prob. 30PCh. 8 - Prob. 31PCh. 8 - Prob. 32PCh. 8 - Prob. 33PCh. 8 - Prob. 34PCh. 8 - Prob. 35PCh. 8 - Prob. 36PCh. 8 - Prob. 37PCh. 8 - Prob. 38PCh. 8 - Prob. 39PCh. 8 - Prob. 40PCh. 8 - Prob. 41PCh. 8 - Prob. 42PCh. 8 - Prob. 43PCh. 8 - Prob. 44PCh. 8 - Prob. 45PCh. 8 - Prob. 46PCh. 8 - Prob. 47PCh. 8 - Prob. 48PCh. 8 - Prob. 49P
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