1. Amino acids must be obtained from 1.

diet
2. synthesized 2. de novo
3. produced from 3. normal protein degradation
4. The first phase of catabolism 4. removal of the a-amino groups
involves the ___________
5. This is usually by (2) 5. - transamination
- oxidative deamination
6. forming (2) 6. - ammonia
- a-keto acid (carbon skeletons of
amino acids)
7. Digestion and Absorption of 7. Dietary protein → mouth → stomach
proteins (HCL and pepsin) → large
polypeptides → Small intestine
(trypsin, chymotrypsin,
carboxypeptidase, aminopeptidase)
→ amino acids → intestinal lining –?
amino acids in blood stream
8. Protein digestion begins in the ____ 8. Stomach
9. Protein digestion is completed in 9. small intestine
10. causes both hydrochloric acid and 10. gastrin
pepsinogen secretion
11. Hydrochloric acid has three major 11. - its antiseptic properties kill most
functions within the stomach: bacteria
- its denaturing action “unwinds”
globular proteins
- its acidity leads to the activation of
pepsinogen
12. making peptide bonds more 12. denaturing action “unwinds” globular
accessible to digestive enzymes proteins
13. inactive form of the digestive 13. pepsinogen
enzyme pepsin
14. affects the hydrolysis of 14. pepsin
approximately 10% of peptide bonds
present in proteins, producing a
variety of polypeptides.
15. stimulates pancreatic production of 15. secretin
bicarbonate ion
16. Its function is neutralization of 16. bicarbonate ion (HCO3)
gastric hydrochloric acid.
17. Pepsin, trypsin, chymotrypsin, 17. proteolytic
carboxypeptidase, and
aminopeptidase are all examples of
_______ enzymes.
18. Aminopeptidase is secreted by 18. intestinal mucosal cells
19. Proteolytic enzymes are produced 19. zymogens
in inactive forms called
20. is the total supply of free amino 20. amino acid pool
acids available for use in the human
body
21. is one of three sources that 21. dietary protein
contributes amino acids to the amino
acid pool.
22. the other two sources 22. - protein turnover
- biosynthesis of amino acids
23. protein degradation exceeds protein 23. negative nitrogen balance
synthesis, the amount of nitrogen in
the urine exceeds the amount of
nitrogen ingested (dietary protein).
24. is the repetitive process in which 24. protein turnover
proteins are degraded and
resynthesized within the human
body.
25. is the state that results when the 25. nitrogen balance
amount of nitrogen taken into the
human body as protein equals the
amount of nitrogen excreted from
the body in waste materials.
26. nitrogen intake exceeds nitrogen 26. positive nitrogen balance
output, indicating that the rate of
protein anabolism (synthesis)
exceeds that of protein catabolism. 27. - Protein synthesis
27. FOUR WAYS to use the amino acids - Synthesis of nonprotein
from the body’s amino acid pool nitrogen-containing compounds
- Synthesis of nonessential amino
acids
- Production of energy
28. - replace old tissue
28. Proteins are continually needed to - build new tissue
29. urea
29. In all the degradation pathways, the
amino nitrogen atom is removed and
ultimately is excreted from the body
as ________. 30. Phenylalanine
30. Tyrosine Precursor 31. Oxaloacetate
31. Aspartic acid 32. Aspartate
32. Asparagine 33. Serine
33. Cysteine 34. Glutamate
34. Proline
35. Alanine 35. Pyruvate
36. Glutamine 36. Glutamate
37. Glutamic acid 37. α-ketoglutarate
38. Serine 38. 3-phosphoglycerate
39. Glycine 39. serine
40. In carbon portion, TAGs via 40. FA biosynthesis
41. Ketone bodies via 41. ketogenesis
42. Glucose via 42. gluconeogenesis
43. ATP via 43. citric acid cycle
44. In nitrogen portion, Elimination via 44. urea
45. Two stages of amino acid 45. - Removal of the a-amino group
degradation: - Degradation of the remaining
carbon skeleton
46. Removal of the a-amino group 46. - Transamination
- Oxidative deamination
47. always involve two amino acids 47. Transamination
(one as a reactant and one as a
product) and two keto acids (one as
a reactant and one as a product).
48. The two most encountered 48. - a-ketoglutarate/glutamate
keto/amino acid pairs in - oxaloacetate/aspartate
transamination are
49. Succinate as keto acid 49. oxaloacetate
50. as amino acid 50. aspartate
51. Glutarate as amino acid 51. glutamate
52. as keto acid 52. a-ketoglutarate
53. 5-carbon diacid 53. glutarate
54. 4-carbon diacid 54. succinate
55. is a biochemical reaction that 55. transamination reaction
involves the interchange of the
amino group of an a-amino acid with
the keto group of an a-keto acid.
56. The needed enzyme for a 56. aminotransferase
transamination reaction is an
57. are the two amino acids produced in 57. - glutamate (from a-ketoglutarate)
transamination reactions - aspartate (from oxaloacetate)
58. Most aminotransferases accept only 58. - a-ketoglutarate
- to a lesser extent, oxaloacetate.
59. a coenzyme produced from 59. pyridoxal phosphate
pyridoxine (vitamin B6)
60. is the basis for regulation of amino 60. reversibility
acid concentrations in the body
61. Through transamination involving
a-ketoglutarate, the amino groups 61. glutamate
from many different amino acids are
collected into one type of molecule,
the amino acid ______.
62. the ultimate fate of the amino groups
being elimination from the body in 62. urea
the form of ____
63. Two pathways for further processing
of the many glutamate molecules 63. - second transamination reaction
produced via transamination - oxidative deamination
64. produces the amino acid aspartate 64. second transamination reaction
65. production of ammonium ion 65. oxidative deamination
66. is a biochemical reaction in which an 66. oxidative deamination reaction
a-amino acid is converted into an a-
keto acid with release of an
ammonium ion.
67. Oxidative deamination occurs 67. - liver
primarily in the (2) - kidney mitochondria
68. Oxidative deamination of glutamate 68. glutamate dehydrogenase
requires the enzyme
69. only known enzyme that can 69. glutamate dehydrogenase
function with either NADP+ or NAD+
as a coenzyme
70. product of oxidative deamination 70. a-ketoglutarate
reaction
71. a toxic substance if left to 71. NH4+
accumulate in the body, is then
converted to urea in the urea cycle.
72. These amino acids undergo direct 72. - serine
deamination by a - threonine
dehydration–hydration process
rather than oxidative deamination.
73. This different behavior results from 73. side-chain β-hydroxyl group
the presence of a
74. is a cyclic biochemical pathway in 74. urea cycle
which urea is produced for excretion.
75. Urea cycle uses (2) as nitrogen 75. - ammonium ions
sources - aspartate molecules
76. Three amino acids are involved as 76. - arginine
intermediates in the operation of the - ornithine
urea cycle: - citrulline
77. The “fuel” for the urea cycle 77. Carbamoyl Phosphate
78. The carbamoyl phosphate formation 78. mitochondrial matrix
reaction takes place in the
79. Urea cycle reaction 79. - Transfer
- condensation
- cleavage
- hydrolysis
80. urea cycle product 80. - citrulline
- argininosuccinate
- arginine
- ornithine
81. citrulline interacts with __ to produce 81. aspartate
argininosuccinate
82. step 1 of urea cycle (carbamoyl 82. mitochondrial matrix
group transfer) occurs in the
83. step 2, 3, and 4 occurs in the 83. cytosol
84. is a second molecule of “fuel” 84. Aspartate
entering the cycle, having been
previously generated from glutamate
by transamination.
85. step 2 enzyme 85. argininosuccinate synthase
86. catalyzes the cleavage of 86. argininosuccinate lyase
argininosuccinate into arginine, a
standard amino acid, and fumarate,
a citric acid cycle intermediate.
87. step 4 enzyme 87. arginase
88. step 3 enzyme 88. argininosuccinate lyase
89. The removal of the amino group of 89. α-keto acid
an amino acid by
transamination/oxidative
deamination produces an
90. is an amino acid that has a 90. Glucogenic amino acid
carbon-containing product that can
be used to produce glucose via
gluconeogenesis.
91. Amino acids that are degraded to 91. ketogenic
acetyl CoA or acetoacetyl CoA can
contribute to the formation of fatty
acids or ketone bodies and are
called _____
92. Only two amino acids are purely 92. - leucine
ketogenic, these are - lysine
93. Amino acids that are degraded to 93. BOTH KETO & GLUCO
pyruvate
94. ketogenic amino acids 94. L,K
95. amino acid that can be converted 95. KETOGENIC
into glucose through
gluconeogenesis.
96. Glucogenic amino acids 96. V, P, M, N, Q, E, D, H, R
97. both keto and gluco amino acids 97. Y, F, I, A,G,C,S,TW
98. The starting materials for the 98. - glycolysis intermediates: 3-
biosynthesis of the 11 nonessential phosphoglycerate and pyruvate
amino acids are the (2) - citric acid cycle intermediates:
oxaloacetate and a-ketoglutarate
99. three non essential amino acids that 99. alanine
are biosynthesized by aspartate
transamination of the appropriate glutamate
a-keto acid starting material.
100. is a conjugated protein 100. Hemoglobin
101. prosthetic group (nonprotein 101. heme
portion)
102. protein portion 102. globin
103. Lack of this enzyme causes the 103. tyrosine
metabolic disease phenylketonuria
(PKU)
104. Old red blood cells are broken 104. spleen
down in the ___ (primary site) and liver
___ (secondary site).
105. is a colored tetrapyrrole 105. Bile pigment
degradation product present in bile
106. an iron-storage protein 106. ferritin
107. Degradation of heme begins with 107. biliverdin
a ring-opening reaction in which a bilirubin
single carbon atom is removed. The
product is called ____, which is then
converted later to____.
108. excretion in feces 108. stercobilin
109. excretion in urine 109. urobilin
110. dung bile 110. Stercobilin
111. is the condition that occurs when 111. Jaundice
this balance is upset such that
bilirubin concentrations in the blood
become higher than normal.
112. Transamination reactions are 112. PLP
dependent on the cofactor ____
113. Oxidation deamination oxidizing 113. niacin
agent
114. This vitamin is needed in the 114. B12
formation of the degradation product
succinyl CoA.
115. is a rare metabolic condition 115. Alkaptonuria
involving a deficiency in
homogentisic acid oxidase, resulting
in the accumulation of homogentisic
acid
116. refers to a group of conditions in 116. Albinism
which a defect in tyrosine
metabolism results in a deficiency in
the production of melanin.
117. autosomal recessive disorder in 117. Maple syrup urine disease
which there is a partial or complete (MSUD)
deficiency in branched-chain α-keto
acid dehydrogenase
118. is the most common clinically 118. Phenylketonuria (PKU)
encountered inborn error of amino
acid metabolism
119. are a group of disorders 119. Homocystinuria
involving defects in the metabolism
of homocysteine.
120. an enzyme complex that 120. α-keto acid dehydrogenase
decarboxylates leucine, isoleucine,
and valine.
121. The patient’s urine contains 121. homogentisic aciduria
elevated levels of homogentisic acid,
which is oxidized to a dark pigment
on standing, large joint arthritis, and
black ochronotic pigmentation of
cartilage and collagenous tissue.
122. These defects result in the partial 122. Albinism
or full absence of pigment from the
skin, hair, and eyes.