Home Subjects Biochemistry Proteins & Enzymes

Biochemistry
Proteins & Enzymes

Metabolic pathways, enzymes, proteins

100 Q 3 Topics Take Test
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Difficulty: All Easy Medium Hard 41–50 of 100
Topics in Biochemistry
All Proteins & Enzymes 100 Carbohydrates 100 Lipids 78
Which type of enzymatic reaction does DNA ligase catalyze, and what cofactor is required?
A Hydrolysis of RNA; requires Mg2+ only
B Formation of phosphodiester bonds; requires NAD+ or ATP
C Unwinding of double-stranded DNA; requires GTP
D Methylation of cytosine; requires SAM
Correct Answer:  B. Formation of phosphodiester bonds; requires NAD+ or ATP
EXPLANATION

DNA ligase catalyzes the formation of phosphodiester bonds between adjacent DNA strands. In prokaryotes, it uses NAD+ as the energy source, while in eukaryotes, ATP is used. This is essential for DNA replication, repair, and recombination.

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Q.42 Medium Proteins & Enzymes
In hyperammonemia type 1, mutations in which enzyme lead to accumulation of ammonia and subsequent neurotoxicity?
A Carbamoyl phosphate synthetase I (CPS I)
B Glutaminase
C Urease
D Monoamine oxidase
Correct Answer:  A. Carbamoyl phosphate synthetase I (CPS I)
EXPLANATION

Hyperammonemia type 1 (Reye's syndrome-like) results from CPS I deficiency, the first enzyme in the urea cycle. CPS I catalyzes ammonia fixation to form carbamoyl phosphate. Its deficiency prevents ammonia detoxification, causing neurotoxic accumulation.

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Which of the following statements about enzyme-substrate complex formation is correct according to transition state theory?
A The enzyme lowers the activation energy by stabilizing the transition state more than the substrate
B The enzyme preferentially stabilizes the ground state of the substrate
C The enzyme does not interact with the substrate during catalysis
D Transition state stabilization is less important than substrate binding
Correct Answer:  A. The enzyme lowers the activation energy by stabilizing the transition state more than the substrate
EXPLANATION

Transition state theory proposes that enzymes achieve catalysis by stabilizing the transition state more effectively than the substrate ground state. The differential stabilization lowers the activation energy barrier, accelerating the reaction.

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In the proteasome pathway, which E3 ubiquitin ligase specifically recognizes phosphorylated IκB and targets it for degradation, leading to NF-κB activation?
A SCF complex
B APC/C
C MDM2
D CHIP
Correct Answer:  A. SCF complex
EXPLANATION

The SCF (Skp1-Cullin1-F-box protein) complex, specifically SCF-β-TrCP, recognizes phosphorylated IκB and polyubiquitinates it for proteasomal degradation. This is a key regulatory step in the NF-κB inflammatory signaling pathway.

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Q.45 Medium Proteins & Enzymes
Which amino acid residue, when present in the active site, typically acts as a general acid-base catalyst in serine proteases?
A Aspartate
B Histidine
C Cysteine
D Methionine
Correct Answer:  B. Histidine
EXPLANATION

In serine proteases like trypsin and chymotrypsin, histidine (His57) acts as a general acid-base catalyst. Its imidazole ring (pKa ~6) can both accept and donate protons, facilitating the nucleophilic attack by the serine hydroxyl group on the carbonyl carbon.

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Q.46 Medium Proteins & Enzymes
What is the primary role of protein disulfide isomerases (PDI) in the endoplasmic reticulum?
A Synthesis of disulfide bonds
B Catalyzing disulfide bond rearrangement and preventing aggregation during protein folding
C Degradation of misfolded proteins
D Transport of proteins across the ER membrane
Correct Answer:  B. Catalyzing disulfide bond rearrangement and preventing aggregation during protein folding
EXPLANATION

PDI catalyzes the formation, reduction, and rearrangement of disulfide bonds. In the oxidizing ER environment, PDI helps misfolded proteins achieve correct disulfide bonding patterns, acting as both an isomerase and a chaperone to prevent aggregation.

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Q.47 Medium Proteins & Enzymes
Which of the following correctly describes the relationship between enzyme concentration and reaction velocity in zero-order kinetics?
A Velocity is independent of enzyme concentration
B Velocity is directly proportional to enzyme concentration at saturation
C Velocity increases exponentially with enzyme concentration
D Velocity decreases as enzyme concentration increases
Correct Answer:  B. Velocity is directly proportional to enzyme concentration at saturation
EXPLANATION

In zero-order kinetics (when substrate >> Km), all enzyme active sites are saturated. Velocity is directly proportional to enzyme concentration since V = kcat[E]total when enzyme is the limiting factor.

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In the unfolded protein response (UPR), which transmembrane kinase/endonuclease senses ER stress and activates the IRE1 pathway?
A ATF4
B IRE1α (with its RNase domain)
C BiP
D CHOP
Correct Answer:  B. IRE1α (with its RNase domain)
EXPLANATION

IRE1α is a transmembrane protein with both kinase and RNase (endonuclease) domains. Upon ER stress (detected by dissociation from BiP), it autophosphorylates and uses its RNase domain to splice XBP1 mRNA, a key transcription factor in the UPR.

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Which enzyme catalyzes the formation of peptide bonds during protein synthesis on the ribosome?
A Aminoacyl-tRNA synthetase
B Peptidyl transferase (part of the 23S/28S rRNA)
C EF-Tu
D Protease
Correct Answer:  B. Peptidyl transferase (part of the 23S/28S rRNA)
EXPLANATION

Peptidyl transferase activity is catalyzed by the 23S rRNA (in prokaryotes) or 28S rRNA (in eukaryotes) component of the ribosome. This ribozyme catalyzes the formation of the peptide bond between the incoming aminoacyl-tRNA and the growing polypeptide chain.

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Q.50 Medium Proteins & Enzymes
What is the Hill coefficient (n) when it equals 1.0 in enzyme kinetics, and what does this indicate?
A Positive cooperativity with multiple binding sites
B Negative cooperativity between subunits
C No cooperativity; the enzyme follows Michaelis-Menten kinetics
D The enzyme is inhibited competitively
Correct Answer:  C. No cooperativity; the enzyme follows Michaelis-Menten kinetics
EXPLANATION

A Hill coefficient of 1.0 indicates no cooperativity and follows simple Michaelis-Menten kinetics. n > 1 indicates positive cooperativity (like hemoglobin), while n < 1 indicates negative cooperativity.

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