Biochem 7: Protein Enzymes

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Which of the following is NOT a level of protein structure?

Secondary

Tertiary

Octet (correct)

Primary

What is the term for the disruption in folding or shape of a protein?

Classification

Catalysis

Denaturation (correct)

Specificity

Which of the following can cause protein denaturation?

Strong acids or bases

Organic solvents

Salts

All of the above (correct)

What type of bonds within proteins can be disrupted by heavy metal ions?

Ionic binds Signup and view all the answers

Which of the following heavy metals can denature proteins based on charge?

Both mercury and lead Signup and view all the answers

What type of amino acid side chain can heavy metals like mercury and lead bind to?

Charged side chains Signup and view all the answers

Which of the following interactions within a protein would be disrupted by heavy metals?

Sulfhydryl group Signup and view all the answers

Which of the following is NOT a way in which cofactors and coenzymes can help enzymes speed up reactions?

Prevent the formation of enzyme-substrate complexes Signup and view all the answers

What effect does temperature have on enzyme activity?

Increases enzyme activity Signup and view all the answers

Which types of bonds between the enzyme and substrate would potentially be disrupted by a change in pH?

Hydrogen bonds Signup and view all the answers

What is the function of a lysosome?

Main site of intracellular enzymatic degradation Signup and view all the answers

At what pH are lysosomal enzymes active?

pH of ~4.5 Signup and view all the answers

What type of enzyme modification alter the structure of an enzyme making or breaking covalent bonds?

Covalent modification Signup and view all the answers

What is the main type of covalent modification that can alter the structure of an enzyme?

Phosphorylation Signup and view all the answers

Which of the following is the basis of lead poisoning?

Binding to sulfhydryl (SH) groups Signup and view all the answers

Enzymes speed up a reaction by lowering the __________ of the reaction.

Activation energy (Ea) Signup and view all the answers

The highest energy configuration formed when changing from reactants to products is called the __________.

Transition state (TS) Signup and view all the answers

Enzymes are highly specific because __________.

They have a special cleft called the active site Signup and view all the answers

Which amino acid side chain can easily function as an acid or a base?

Serine (Ser) Signup and view all the answers

Which nucleophilic side groups can form a temporary covalent bond with the substrate in enzyme active sites?

Serine (Ser) and Cysteine (Cys) Signup and view all the answers

What is the role of magnesium in glycolytic enzymes involving ATP?

To position the ATP in the enzyme active site Signup and view all the answers

Which enzyme catalyzes the phosphorylation in glycogen metabolism?

Glycogen phosphorylase kinase Signup and view all the answers

Which enzyme is inhibited by covalent modification in glycogen metabolism?

Glycogen synthase Signup and view all the answers

What type of modification is involved in irreversible covalent modification of enzymes?

Cleavage of peptide bonds Signup and view all the answers

Which type of modification changes the conformation and activity of the enzyme by binding to its allosteric site?

Allosteric modification Signup and view all the answers

What is the effect of an effector molecule binding to an allosteric enzyme?

Activating or inhibiting binding of the substrate to the enzyme Signup and view all the answers

Which enzyme is allosterically inhibited by high levels of ATP?

Phosphofructokinase-1 Signup and view all the answers

Which enzyme is allosterically activated by high levels of AMP?

Phosphofructokinase-1 Signup and view all the answers

What is the purpose of compartmentalization of enzymes via membrane-bound organelles?

To create unique microenvironments Signup and view all the answers

At what pH do lysosomal enzymes function?

Around 4.5-5 Signup and view all the answers

What is the term for the disruption in folding or shape of a protein?

Denaturation Signup and view all the answers

Which of the following interactions within a protein would be disrupted by heavy metals?

Disulfide bridges Signup and view all the answers

What is the function of a lysosome?

Intracellular digestion Signup and view all the answers

Which amino acid side chain can easily function as an acid or a base?

Histidine Signup and view all the answers

What type of amino acid side chain can heavy metals like mercury and lead bind to?

Basic Signup and view all the answers

At what pH do lysosomal enzymes function?

Acidic Signup and view all the answers

Which of the following is the basis of lead poisoning?

Binding to enzymes and interfering with their function Signup and view all the answers

Which of the following can cause protein denaturation?

All of the above Signup and view all the answers

Which type of protein is generally long and rod-shaped, providing strength and often insoluble in water?

Fibrous Protein Signup and view all the answers

Which type of protein is generally compact and spherical, often soluble in water, and has dynamic functions such as catalyzing reactions?

Globular Protein Signup and view all the answers

Which level of protein structure refers to the linear sequence of amino acids in a protein?

Primary Structure Signup and view all the answers

Which level of protein structure refers to the folding and twisting of the polypeptide chain due to hydrogen bonding between amino acids?

Secondary Structure Signup and view all the answers

Which level of protein structure refers to the overall 3D arrangement of a single polypeptide chain?

Tertiary Structure Signup and view all the answers

Which level of protein structure refers to the arrangement of multiple polypeptide chains in a protein complex?

Quaternary Structure Signup and view all the answers

What is the term for the process of unfolding or disruption in the shape of a protein, resulting in loss of function?

Denaturation Signup and view all the answers

Which type of catalysis involves the transfer of a proton from an acid to a base?

Acid-Base Catalysis Signup and view all the answers

Which type of catalysis involves the formation of a covalent bond between the enzyme and substrate?

Covalent Catalysis Signup and view all the answers

What are small molecules or ions that are required for the proper functioning of some enzymes called?

Cofactors Signup and view all the answers

Biochem 7: Protein Enzymes

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Questions and Answers

Which of the following is NOT a level of protein structure?

What is the term for the disruption in folding or shape of a protein?

Which of the following can cause protein denaturation?

What type of bonds within proteins can be disrupted by heavy metal ions?

Which of the following heavy metals can denature proteins based on charge?

What type of amino acid side chain can heavy metals like mercury and lead bind to?

Which of the following interactions within a protein would be disrupted by heavy metals?

Which of the following is NOT a way in which cofactors and coenzymes can help enzymes speed up reactions?

What effect does temperature have on enzyme activity?

Which types of bonds between the enzyme and substrate would potentially be disrupted by a change in pH?

What is the function of a lysosome?

At what pH are lysosomal enzymes active?

What type of enzyme modification alter the structure of an enzyme making or breaking covalent bonds?

What is the main type of covalent modification that can alter the structure of an enzyme?

Which of the following is the basis of lead poisoning?

Enzymes speed up a reaction by lowering the __________ of the reaction.

The highest energy configuration formed when changing from reactants to products is called the __________.

Enzymes are highly specific because __________.

Which amino acid side chain can easily function as an acid or a base?

Which nucleophilic side groups can form a temporary covalent bond with the substrate in enzyme active sites?

What is the role of magnesium in glycolytic enzymes involving ATP?

Which enzyme catalyzes the phosphorylation in glycogen metabolism?

Which enzyme is inhibited by covalent modification in glycogen metabolism?

What type of modification is involved in irreversible covalent modification of enzymes?

Which type of modification changes the conformation and activity of the enzyme by binding to its allosteric site?

What is the effect of an effector molecule binding to an allosteric enzyme?

Which enzyme is allosterically inhibited by high levels of ATP?

Which enzyme is allosterically activated by high levels of AMP?

What is the purpose of compartmentalization of enzymes via membrane-bound organelles?

At what pH do lysosomal enzymes function?

What is the term for the disruption in folding or shape of a protein?

Which of the following interactions within a protein would be disrupted by heavy metals?

What is the function of a lysosome?

Which amino acid side chain can easily function as an acid or a base?

What type of amino acid side chain can heavy metals like mercury and lead bind to?

At what pH do lysosomal enzymes function?

Which of the following is the basis of lead poisoning?

Which of the following can cause protein denaturation?

Which type of protein is generally long and rod-shaped, providing strength and often insoluble in water?

Which type of protein is generally compact and spherical, often soluble in water, and has dynamic functions such as catalyzing reactions?

Which level of protein structure refers to the linear sequence of amino acids in a protein?

Which level of protein structure refers to the folding and twisting of the polypeptide chain due to hydrogen bonding between amino acids?

Which level of protein structure refers to the overall 3D arrangement of a single polypeptide chain?

Which level of protein structure refers to the arrangement of multiple polypeptide chains in a protein complex?

What is the term for the process of unfolding or disruption in the shape of a protein, resulting in loss of function?

Which type of catalysis involves the transfer of a proton from an acid to a base?

Which type of catalysis involves the formation of a covalent bond between the enzyme and substrate?

What are small molecules or ions that are required for the proper functioning of some enzymes called?

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