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UNE BIOCHEMISTRY WEEK 1 REVIEW WITH 100% CORRECT ANSWERS.
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- Oxford University (OX)
UNE BIOCHEMISTRY WEEK 1 REVIEW WITH 100% CORRECT ANSWERS.
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UNE BIOCHEMISTRY WEEK 1 REVIEWWITH 100% CORRECT ANSWERS
Allosteric activators of hemoglobin will increase substrate binding through which of the
following mechanisms? - answer 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 - answer cysteine, serine, and
histidine
Which of the following best describes the structure of heme? - answer A planar porphyrin ring
that binds iron
How do most enzymes reduce the activation energy needed to move a reaction forward? -
answer 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? - answer 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? - answer Lyase.
Examples of prosthetic groups - answer pyridoxal phosphate
flavin mononucleotide (FMN)
Flavin adenine dinucleotide (FAD)
Thiamin pyrophosphate
, lipoic acid
biotin
and transition metals
Transition metals that are prosthetic groups - answer 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 - answer Prosthetic groups, cofactors
and coenzymes
Difference between cofactors and prosthetic groups - answer 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? - answer Metal ions.
Enzymes that need a metal ion cofactor are called metal-activated enzymes
Many coenzymes, cofactors and prosthetic groups are derivatives of ? - answer Vitamin B
Nicotinamide (B3) is a component of ? - answer Nicotinamide is a component of the redox
coenzymes NAD and NADP
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