Biochemistry:

1. Which enzyme is associated with phosphorylation of ADP at the substrate

level? Pyruvate kinase
2. NADPH-reduction, Biotin-carboxylation, nadh&fadh2-oxidation
3. Epinephrine and glucagon cause? Glycogenolysis+ GLUCEONEOGENESIS
4. Glucagon phosphorylates? Glycogen phosphorylation
5. Mechanism of action of glucagon? Phosphorylation of protein kinase
6. Glucagon signals through? cAMP
7. What is the second messenger for glycogen? cAMP
8. cAMP MOA: phosphorylate kinase
9. What is allosteric inhibitor in glycolysis? ATP
10. Allosteric activator of glycolysis? AMP
11. What enzyme catalyzes glycogen to glucose? glycogen phosphorylase
12. Which of the following inhibit the activity of acetyl-coA carboxylase?
Glucagon
13. Sphingolipid regarding their structure? Sphingosine, 1 fatty acid chain and a
functional group.
Sphingomyelin: FA+ sphingosine+Choline

Lecithins: FA+Glycerol+Choline

Cephalins: FA+Glycerol+Serine (or 2-ethanolamine)

Functional groups:
a. Glucose in cerebroside
b. Choline in sphingomyelin
c. Bunch of sugars in ganglioside
d. Hydrogen in ceramide
14. ATPase bind to? Tropomyosin Myosin head
15. Insulin receptor? Tyrosine kinase
16. Mobilization of glucose based on ACTIVATION of PROTEIN KINASE A.
17. Insulin and somatomedin attach to which receptors- creatine tyrosine kinase
receptor! I doubt this since Creatine kinase (CK) is an enzyme found in muscle.
18. Promote osteogenesis? Somatotropin (GH)
19. Direct source of energy? ATP = ADP + phosphorus
20. Activation or action of an enzyme includes? Phosphorylation of serine residue
or hydrolysis of a peptide unit
21. Bond between DNA units? Phosphodiester
22. Bond between monomeric nucleotide? Phosphodiester
23. Bonds between 2 DNA? H bond
24. Bonds in alpha helical structure of proteins? H BONDS
25. Alpha structure in protein holding bond? Hydrogen bond
26. Alpha helix & beta sheets form (2ndary protein structure)? Hydrogen bonds
27. What is the main AA in the tertiary structure of protein? Cysteine (disulfide
bond)
28. 8m urea brakes which type of bonds? Disulfide bonds
29. Bonds between GAGs? Glycosidic bonds
30. Bonding of glycoprotein formation? Glycosidic bond
31. Bond glycogen between glucose unit? Glycosidic bond
32. 8molar urea denatures protein by 1. ______ which brake 2. ________
bonds in tertiary structure? Carbamylation reactions, disulfide bonds.
33. Seal DNA? Ligase
34. What is the beginning of the urea cycle? NH4 + CO2 +ATP forming
carbamoyl phosphate
35. Nitrogen sources in urea cycle? Carbamoyl phosphate and aspartate
36. Last step of gluconeogenesis on liver? Glucose 6 phosphatase
37. Not essential in lysine hydroxylation? Vitamin k
38. Extracellular event of collagen formation? cross-linking�
39. Cholesterol? HMG reductase
40. Major regulatory enzyme in cholesterol synthesis? Hmg COA reductase
41. To form prostaglandins? Polyunsaturated fa is needed
42. Hydrolysis of which of the following will not yield glucose? Mannose
43. Which is not found in collagen? Tropoelastin
a. glycine, proline, alanine and lysine all present in Collagen
44. Glucagon and epinephrine have in common? Glycogenolysis
epinephrine want acts on alpha receptor inhibit insulin secretion by pancreas and
in turn stimulate glycogenolysis in liver and muscle norepinephrine increases
glucose production either by glycogenolysis or gluconeogenesis, glucagon binds
with glucagon receptors in liver which then converts glycogen to glucose and
releases into blood stream - (glycogenolysis) also to make up/synthesize
additional glucose it encourages the liver and kidney to undergo gluconeogenesis
45. UTP in glycogen? Reacts with glucose 1 phosphate to form glycogen
46. Who is the final electron receptor in electron transport chain? Organic
compound in case of fermentation (i.e. O2)
47. Biotin à carboxylation
• any carboxylase needs biotin cofactor
48. Biotin for? Pyruvate carboxylase (pyruvate to OAA)
49. What enzymes produce oxaloacetate? Pyruvate Carboxylase (pyruvate
oxaloacetate)
50. What is biotin used for? Pyruvate Carboxylase, acetyl CoA (cofactor)
51. Biotin (= Vit H)? carboxylation of acetyl CoA à Malonyl CoA, in fatty acid
synthesis
52. Oxidative decarboxylation? pyruvate dehydrogenase
• Vit B6 (pyridoxine) is involved with transamination and decarboxylation
53. Oxidative phosphorylation occurs in what enzyme? Pyruvate dehydrogenase
54. Regeneration of pyruvate by? Lactate dehydrogenase
55. 1st step in correcting thiamine dimmers? Photo reactivation by photolyase
enzyme
56. Amino acid in interior of proteoglycans? serine and threonine
57. Central protein is rich in which amino acids? serine and threonine
58. Purely ketogenic aa? leucine, lysine
59. AA typically found in inner part of protein — alanine, isoleucine, leucine,
valine, and phenylalanine — are all strongly hydrophobic and thus more likely to
be found in the interior of proteins, away from water on the surface of the
protein.
60. What is always found inside protein structure? Alanine
61. What is most likely found in interior of proteins? Tyrosine or LUECINE
62. Troponin changes the position of? Tropomyosin
63. What is found in the inner membrane of hepatitis virus? Glycoprotein
64. Influenza antigenicity due to? Glycoproteins
65. ORINTHINE is an intermediate of the UREA CYCLE in mitochondria
66. CITRULLINE is an intermediate of the UREA CYCLE in cytoplasm
67. production of carbamoyl phosphate and citrulline takes place INSIDE the
mitochondria �
68. Immediate precursor of urea: arginine �
69. What is an intermediate in the urea & precursor for ornithine? Arginine
70. Precursor of urea (aspartate+________)? Arginine
71. End step in urea cycle? Arginine to urea by Arginase
72. Last product of urea cycle? Arginine and urea
73. Carbonyl phosphate, citrulline, aspartate & ammonia are sources from which
nitrogen is derived in? Urea cycle
74. Where does the Nitrogen come from in urea cycle? ammonia & aspartate
75. Amino acid used in urea cycle? Aspartic acid
76. Max ammonia produce by which amino acid? glutamate
77. What type of enzyme is Fumerase? Isoenzyme
78. Fumerase/fumarate connects urea cycle via? TCA Cycle
79. Fumarate connect to TCA by which enzyme? Argininosuccinate lyase
80. Fumarase is what kind of reaction? Hydration/dehydration
81. Fumarate to malate- hydration/dehydration
82. Fumarase is what type of reaction-REVERSIBLE HYDRATION
DEHYDRATION FROM FUMARATE TO MALATE
83. Malate to oxaloacetate is a Dehydrogenation (dehydrogenase, nadh2 is
formed)
84. Purine synthesis? Folic acid. Folic acid is important for the biosynthesis of
purines and pyrimidines
85. Purine metabolism product? Uric acid
86. Purine metabolism? Xanthine oxidase
87. Last step in purine and pyrimidine synthesis? R5P + ATP à PRPP (5-
RIBOSYL-1-PYROPHOSPHATE), IMP à AMP and GMP
88. Glycolysis its enzymes and products? Phosphofructokinase and pyruvate
89. Acetyl coal not synthesized by? Adenosine
90. Pyrimidine dimer break down by which enzyme? Endonuclease
91. DNA fingerprinting, restriction sites? Palindrome are the sites where DNA is
cut & the enzyme used is restriction endonuclease
92. N glycosylation? Between sugar and amino acid (peptidoglycan) – In RER
93. O glycosylation? gOlgi
94. Niacin deficiency (B3)? Pellagra
95. GTP action? Activate and inactivate adenyl cyclase or cleaved by proteasome
96. Related to cell surface receptors with CDR complex? T cells
97. Mhc I bind? Cd8 (cytotoxic cells) used in apoptosis
98. Mhc II bind? Cd4 (B cells)
Cytotoxic T- cells (CD8) bind to MHC Class 1
Helper T cells (CD4) bind to MHC Class 2
99. Action of macrophages on t cells? Macrophages express MHC II and attract t
helper cells which in turn activate macrophages for phagocytosis to release
cytokines
100. T cell receptor binding? Fab
101. gamma-glutamyl carboxylase is needed for coagulation
102. gamma-glutamyl carboxylase is an enzyme that catalyzes the
posttranslational modification of vitamin K-dependent proteins
103. Biosynthesis of cholesterol? Squalene
104. de novo synthesis of cholesterol? Squalene as intermediate
105. De novo cholesterol formation? HMG coa reducatase
106. Which of the following is necessary for de novo synthesis of cholesterol?
NADPH
107. Low carb diet --> low level of Malonyl; why? b/c you want less ketone bodies
forming!
108. IL2? Produced by T cells, attract more T cells
109. Linkages in carbohydrate? Alpha 1,4 (Carbo = Arba’a 4)
110. Linkage in Dextran is? Alpha 1-6 (Dex = Six 6)
111. Linkage glycogen is? Alpha 1,4 glycosidic linkages
112. Linkage in peptidoglycan? Beta 1,4
113. Cross Adenosine nucleoside mitochondria via? Translocation
114. What steps restores oxaloacetate in TCA? Malate, malate dehydrogenase
115. What enzymes produce oxaloacetate? Pyruvate Carboxylase
116. Pyruvate gets decarboxylated and forms what product along with citrate?
OOA (Oxaloacetate + citrate)
117. What is the main source of Glycerol? Glucose/pyruvate
118. Where is phosphoenolpyruvate (PEP) found? Liver
119. Pyrimidine synthesis begins with what? Ribose 5 - phosphate
R5P = Result of pentose phosphate pathway, makes ribose for nucleotide
synthesis & NAPD for fatty acid/steroid
120. What process makes NADPH? Pentose Phosphate Shunt
121. Primary molecule for reduction biosynthesis? NADPH
122. NADPH not necessary for? Glycolysis
123. Which of the following does NOT use NADPH? Ans: making glucose from
pyruvate �
● NADPH made by pentose pathway and utilize in the calvin cycle (in plants) to
make glucose
124. Purine metabolism, intermediate and precursor of adenosine and guanine,
IMP (inosine monophosphate)
125. When taking away phosphate group from (named a nucleotide)? Nucleoside
126. What’s the difference between thymidine & uracil? Methyl group on thymine
127. What kind of force holds proteins in the lipid bilayer? Hydrophobic
Interaction
128. tRNA wobble is in the 3rd position of the codon
129. Which one plays an important role in detecting the starting codon
(initiation) for RNA transcription? Sigma Part
130. What determines protein turnover? H-bonds & peptide bones: breakdown &
synthesis of proteins
131. Product of enzyme isocitrate dehydrogenase in TCA cycle? Alpha-
ketogluterate
132. Alpha ketoglutarate is a requirement for hydroxylation of proline to
hydroxyproline
133. In the amino acid metabolism, what are the 2 primary acceptors of amine
groups? OAA & alpha-ketogluterate
134. The transamination of pyruvate to alanine yields either a-ketoglutarate or
oxaloacetate.
135. How does alanine produced from partial breakdown in muscle?
transamination reaction form pyruvate, can also form urea
136. Phenylketonuria which enzyme is defected? Phenylalanine hydroxylase
(PAH)
• Phenylalanine hydroxylase is responsible for the conversion of phenylalanine
AA to another amino acid, tyrosine.
137. Phenylketonuria: inability to hydroxylate phenylalanine sufficiently
Phenylketonuria (commonly known as PKU) is an inherited disorder that
increases the levels of phenylalanine in the blood. �
138. Acetyl-CoA carboxylase enzyme of fatty acid synthesis
• function is to provide malonyl CoA - substrate for biosynthesis of fatty acids
139. Fatty acid synthesis
• Occurs in the cytosol of mostly hepatocytes.
• The irreversible conversion of acetyl-CoA → malonyl-CoA via acetyl-CoA
carboxylase
• Acetyl-CoA carboxylase is the rate-limiting enzyme.
• Conversion of acetyl-CoA → malonyl-CoA is the rate-limiting step.
• Citrate insulin (+) and glucagon, epinephrine (-)
140. Fatty acid oxidation or beta oxidation
• (mitochondria)
• Acyl CoA ----acetyl CoA
• Fatty acids are carried by carnitine mediated enzyme system.
141. Initiation of substrate
• Phosphorylation – kinases
• Dephosphorylation - phosphatase
• Methylation – methyltranferase
142. Glycosaminoglycan’s? ground substance of ECM
143. D and L version of amino acid in peptidoglycan? Alanine�
144. non-standard amino acid- hydroxyproline and hydroxylysine
Amino Acids in one post!!!
- Nonchiral amino acid
Glycine
-disulfide bond
Cysteine=cysteine
- convert to ammonia at kidney:
Glutamate
- the first urea nitrogen come from ammonia by carbomyl phosphate, another
nitrogen come from Aspartate
-Main metabolite for urea in liver is
Arginine (hydrolysis of arginine by "arginase")
- Amino Acid "freak" in its' structure (make a ring around itself) and does not
resemble any other A.A:
Proline
- histones + DNA = (nucleosome) contain
Arginine & lysine
(HAL) all 3 are positive --- link to DNA (negative"
- all protein in "L"iving cells are:
L-configuration
D-configuration (antibiotic & bacteria)
"""Remember most of carbohydrates are D-configuration"""
- protein absorption:
Co-transport
Small A.A (degradation of protein). / Na-gradient
Di & tri Peptides: H-gradient
Hydroxylysin & hydroxyproline are Non standard amino acids
- non transamination
Lysine
Serine