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UNE Biochemistry Week 1 Review – Questions & Correct Answers
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- UNE Biochemistry
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- UNE Biochemistry
UNE Biochemistry Week 1 Review – Questions & Correct Answers
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UNE Biochemistry Week 1 Review – Questions &Correct Answers
Allosteric activators of hemoglobin will increase substrate binding through
which of the following mechanisms? Correct Ans - Binding the
protein and keeping it in the R conformation. Allosteric activators of
hemoglobin stabilize the R state, allowing increased affinity for oxygen and
rapid saturation.
The R-group on valine does not have an active group to participate in
covalent catalysis. Which amino acids most commonly participate in
covalent catalysis Correct Ans - cysteine, serine, and histidine
Which of the following best describes the structure of heme? Correct
Ans - A planar porphyrin ring that binds iron
How do most enzymes reduce the activation energy needed to move a
reaction forward? Correct Ans - Providing an active site most
complementary the transition state. n the induced fit model, the active site
is more homologous to the transition state of the reaction and this reduces
the activation energy of the transition.
Movement of ammonia from an amino acid to an α-keto acid involves a
family of enzymes best categorized as which of the following? Correct
Ans - transferases. Amino transferases are commonly used in the
movement of ammonia and use the covalent catalysis "ping-pong method".
Cleavage of fructose 1, 6-bisphosphate to dihydroxyacetone and
glyceraldehyde 3-phosphate is achieved by what class of enzymes?
Correct Ans - Lyase.
Examples of prosthetic groups Correct Ans - pyridoxal phosphate
flavin mononucleotide (FMN)
Flavin adenine dinucleotide (FAD)
Thiamin pyrophosphate
lipoic acid
biotin
and transition metals
, Transition metals that are prosthetic groups Correct Ans - Fe
Co (cobalt)
Cu (copper)
Mg
Mn (Manganese)
Zn (Zinc)
What extends the repertoire of catalytic capabilities beyond those afforded
by the functional groups present on the aminoacyl side chains of peptides
Correct Ans - Prosthetic groups, cofactors and coenzymes
Difference between cofactors and prosthetic groups Correct Ans -
Prosthetic groups tightly and stably are incorporated into a proteins
structure - verse cofactors which serve similar functions, they bind weakly
and transiently to their cognate enzymes or substrates forming dissociable
complexes. Thus cofactors must be present in surrounding environment to
promote complex formation for catalysis to occur.
What are the most common cofactors? Correct Ans - Metal ions.
Enzymes that need a metal ion cofactor are called metal-activated enzymes
Many coenzymes, cofactors and prosthetic groups are derivatives of ?
Correct Ans - Vitamin B
Nicotinamide (B3) is a component of ? Correct Ans - Nicotinamide
is a component of the redox coenzymes NAD and NADP
Riboflavin (B2) is a component of? Correct Ans - Riboflavin is a
component of the coenzymes FMN and FAD
Pantothenic acid (B5) is a component of ? Correct Ans - Pantothenic
acid (B5) is a component of the acyl group carrier coenzyme A
Pyrophosphate thiamin participates in the ? Correct Ans -
Pyrophosphate thiamin (B1) participates in the decarboxylation of a-keto
acids
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