Docsity
Docsity

Prepare for your exams
Prepare for your exams

Study with the several resources on Docsity


Earn points to download
Earn points to download

Earn points by helping other students or get them with a premium plan


Guidelines and tips
Guidelines and tips

UNE Biochem week 1 quiz with well explained test., Exams of Medical Biochemistry

UNE Biochem week 1 quiz with well explained test.

Typology: Exams

2024/2025

Available from 07/03/2025

annie-wanjiru
annie-wanjiru 🇺🇸

469 documents

1 / 2

Toggle sidebar

This page cannot be seen from the preview

Don't miss anything!

bg1
UNE Biochem week 1 quiz with well
explained test.
An enzyme has a mutation within the substrate binding site that reduces the binding of
the coenzyme needed for covalent catalysis. Which of the following is likely to result as
a consequence of this mutation? - correct answers.the enzyme will not be able to form
the transition state complex
Covalent catalysis is used by many enzymes to cleave peptide bonds. Which of the
following amino acids would not facilitate this type of catalysis? (Think of the structure of
the R-group of these amino acids) - correct answers.Valine
The R-group on valine does not have an active group to participate in covalent
catalysis. The most commonly participating amino acids are cysteine, serine and
histidine.
A 55-year old man is brought to the emergency room with a chief complaint of chest
pain and tingling in his left arm. Elevation of which of the following enzymes in
circulation would be most indicative of a myocardial infarction? - correct
answers.Troponin
MI is diagnosed by elevation of troponin, cardiac specific troponins would be the most
accurate answer for this diagnosis. Amylase and lipase would indicate pancreatitis;
elevation of lactate dehydrogenase is non-specific for muscle damage. Although LDH
may be elevated, in the case of an MI it would not be a definitive indicator.
Prosthetic groups are complex nonprotein molecules that participate in catalysis by
providing functional groups that form a covalent intermediate between the enzyme and
the substrate. Which of the following is an example of a coenzyme or cofactor that
participates in a covalent catalysis reaction? - correct answers.Pyridoxal phosphate
Amino transferases are commonly used in the movement of ammonia and use the
covalent catalysis "ping-pong method". NADH and FAD are commonly used in oxidation
reduction reactions and ATP is typically an energy carrier within an reaction.
pf2

Partial preview of the text

Download UNE Biochem week 1 quiz with well explained test. and more Exams Medical Biochemistry in PDF only on Docsity!

UNE Biochem week 1 quiz with well

explained test.

An enzyme has a mutation within the substrate binding site that reduces the binding of the coenzyme needed for covalent catalysis. Which of the following is likely to result as a consequence of this mutation? - correct answers.the enzyme will not be able to form the transition state complex Covalent catalysis is used by many enzymes to cleave peptide bonds. Which of the following amino acids would not facilitate this type of catalysis? (Think of the structure of the R-group of these amino acids) - correct answers.Valine The R-group on valine does not have an active group to participate in covalent catalysis. The most commonly participating amino acids are cysteine, serine and histidine. A 55-year old man is brought to the emergency room with a chief complaint of chest pain and tingling in his left arm. Elevation of which of the following enzymes in circulation would be most indicative of a myocardial infarction? - correct answers.Troponin MI is diagnosed by elevation of troponin, cardiac specific troponins would be the most accurate answer for this diagnosis. Amylase and lipase would indicate pancreatitis; elevation of lactate dehydrogenase is non-specific for muscle damage. Although LDH may be elevated, in the case of an MI it would not be a definitive indicator. Prosthetic groups are complex nonprotein molecules that participate in catalysis by providing functional groups that form a covalent intermediate between the enzyme and the substrate. Which of the following is an example of a coenzyme or cofactor that participates in a covalent catalysis reaction? - correct answers.Pyridoxal phosphate Amino transferases are commonly used in the movement of ammonia and use the covalent catalysis "ping-pong method". NADH and FAD are commonly used in oxidation reduction reactions and ATP is typically an energy carrier within an reaction.

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 answers.Transferases Amino transferases are commonly used in the movement of ammonia and use the covalent catalysis "ping-pong method" Which of the following best describes a protein domain? - correct answers.A section of a protein structure sufficient to perform a particular chemical or physical task By definition, domains would include multiple elements of secondary structure to generate a region on the protein with a distinct function and spatial arrangement. None of the other choices fit this definition. Changes in the physiological variables listed below can alter the affinity of hemoglobin for oxygen. Which of the following will lower the affinity of hemoglobin for oxygen? - correct answers.Increase in 2,3 bisphosphoglycerate (BPG) A decreased affinity will increase the rate of oxygen delivery to the tissues. This will occur when pH is low, there is an increase in CO2, protons or 2,3 BPG. The other scenarios (a, c, d) will all increase the affinity for O2. Which amino acid would not be commonly found in the middle of a an α-helical domain?

  • correct answers.Proline Proline is a non-traditional amino acid. Peptide bond formation with this amino acid generates a kink or turn in a primary amino acid strand. If introduced in a helix it will destabilized the hydrogen bonding between resides in the helix.