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Enzymes Quiz

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Specific biologic proteins that catalyze biochemical reactions without being consumed or changed.

Enzymes

This is where plasma specific enzymes are synthesized

Liver

Cofactors are nonprotein entities that must bind to particular enzymes before a reaction occurs. Coenzymes, Activators, Metalloenzymes are the three types of ________.

cofactors

Coenzymes are second ________.

substrates

Activators are inorganic ions that alters the spatial configuration of the enzyme for proper ________ binding.

substrate

Metalloenzymes are inorganic ions attached to a ________.

molecule

Binding site consists of sequences of amino acids which determines____ of the enzyme

enzyme

______ are nonprotein entities that must bind to particular enzymes before a reaction occurs.

Cofactors

______ are second substrates.

Coenzymes

Activators include inorganic ions which may be ______ or anions.

cations

______ are inorganic ions attached to a molecule.

Metalloenzymes

Active site consists of binding site and catalytic site. Binding site consists of sequences of amino acids which determines specificity of ______.

Binding site and catalytic site

What is the function of isoforms in terms of serum protein?

Result from post translational modifications

How do isoforms differ from isoenzymes?

Isoforms result from gene modifications while isoenzymes result from post translational modifications

What effect does the presence of isoforms have on enzyme activity?

Enhances catalytic efficiency

Which statement about isoforms is true?

Isoforms exhibit different biochemical properties

How do isoforms contribute to enzyme diversity?

By varying catalytic activity

What are isoenzymes?

Different forms of an enzyme that catalyze the same biochemical reaction

What is a distinguishing factor between different isoenzymes?

Their ability to be inhibited by specific agents

In what way do isoforms impact enzyme functionality?

By enhancing enzyme-substrate interactions

How do isoenzymes differ from each other in terms of physical properties?

Isoelectric point and electrophoretic mobility

What differentiates isoenzymes in terms of their enzymatic properties?

Reactivity with specific agents and substrates

Why is the assessment of specific tissue damage important in relation to isoenzymes?

To locate the tissue distribution of specific isoenzymes

In the context of isoenzymes, what influences their ability to catalyze biochemical reactions?

Their interaction with activators and metalloenzymes

What does the term 'stereoisomer specific' mean in relation to enzymes?

The enzyme acts on a particular steric or optical isomer.

How does the enzyme commission classify enzymes?

By assigning an EC numerical code for each enzyme.

Why were trivial recommended names assigned to enzymes?

To make the systematic names more usable due to their length.

Which of the following best describes the function of enzymes?

Catalyze biochemical reactions without being consumed

What role do coenzymes play in enzyme reactions?

Binding to the active site of enzymes.

Why are enzymes effective in small concentrations?

To affect the speed of attaining equilibrium without changing final concentrations

How does the first digit of an EC numerical code categorize enzymes?

By placing the enzyme in one of six classes.

What is the role of plasma specific enzymes?

Perform definite and specific physiological functions in plasma at higher concentrations

Why are changes in enzyme concentration considered a sensitive diagnostic tool?

To track changes that have occurred in various types of tissues

What characteristic defines the specificity of an enzyme's binding site?

The sequences of amino acids that make up the binding site.

Where are plasma specific enzymes synthesized?

Exclusively in the liver

What is the effect of enzyme isoforms on physiologic functions?

Are essential to physiologic functions such as nerve conduction and muscle contraction

Which class of enzyme catalyzes the interconversion of geometric, optical, or positional isomers within a molecule?

Isomerases

What is the main function of ligases or synthetases among the classes of enzymes mentioned?

Catalyze bond formation reactions

What do the second and third digits of the EC code number represent for an enzyme?

The subclass and sub-subclass

Which enzyme is responsible for converting glyceraldehyde 3 phosphate to dihydroxy acetone phosphate?

Triosephosphate isomerase

What is a common feature of the substrate molecules joined by ligases or synthetases?

They form a double bond during the reaction

Which type of enzyme catalyzes the removal of groups from substrates without hydrolysis, resulting in products with double bonds?

Aldolase

Which of the following statements regarding Oxidoreductases is TRUE?

They catalyze the transfer of a hydrogen group from one substrate to another.

Creatine kinase is primarily found in which organ?

Pancreas

Which enzyme was formerly known as SGPT?

AST

Which element is NOT listed as being part of the composition of enzymes?

Chlorine

Amylase is classified as which type of enzyme?

Hydrolase

What is the approximate molecular weight range of enzymes as mentioned in the text?

10,000-100,000 Daltons

What does the first digit on the EC code of an enzyme indicate?

Class of the enzyme

What type of proteins are enzymes classified as in the text?

Globular proteins

Where are plasma specific enzymes primarily synthesized according to the text?

Liver tissues

How do enzymes affect the speed of attaining equilibrium at any given temperature?

By not changing the concentrations of substrates and products

What defines absolute specificity in enzymes?

The enzyme combines with only one substrate

Which type of specificity involves the enzyme reacting with substrates containing similar structural groups?

Group specificity

What is the characteristic of enzymes that exhibit bond specificity?

They combine with only one substrate

In enzyme classification, what distinguishes metalloenzymes?

Inorganic ions attached to the enzyme

What is the defining feature of a proenzyme/zymogen?

Inactivation until altered by other enzymes

How does the binding site of an active site influence enzyme activity?

Determining the enzyme's specificity through sequences of amino acids

How do allosteric sites differ from active sites in terms of their effect on enzyme activity?

Allosteric sites inhibit enzyme activity by blocking substrate binding

What is a key characteristic that distinguishes isoforms from isoenzymes?

Post-translational modifications resulting in multiple forms of serum protein

How do different factors impact the plasma concentration of enzymes?

Regulating the expression of enzyme genes through DNA methylation

How are isoenzymes metabolized and excreted in biological systems?

By tissue-specific expression leading to differential excretion rates

This is the protein portion of the enzyme

Apoenzyme

A complete and active system which is formed when an enzyme is bound with its respective coenzyme

Holoenzyme

Inactive form of an enzyme

Proenzyzme

Enzyme combines with one substrate catalyzes one reaction

Absolute specificity

Acts only on molecules with specific functional group

Group specificity

Enzyme reacts with substrates that contains similar structural group

Group Specificity

Type of specificity of amino, phosphate, and methyl group

Group Specificity

Enyzme acts on a particular steric or optical isomer.

Stereoisomer specific

Chemical reaction where carbohydrate is attached to a protein to form glycoprotein

Glycosylation

Chemical reaction that involves adding phosphate to an organic compound

Phosphorylation

Cleavage of proteins into smaller components.

Proteolytic cleavage

Cleavage of proteins into smaller components

Protein degradation

What are the list of oxidoreductases

  1. LDH- Lactate dehydrogenase 2.. G-6-PDH- Glucose-6-phosphate dehyrdrogenase
  2. GLD- Glutamate dehydrogenase

This class of enzyme catalyzes an electron transfer or oxidation-reduction reaction between two substrates

Oxidoreductase

This class of enzyme catalyzes the transfer of a group (amino, carboxyl, methyl, or phosphoryl group) other than hydrogen from one substrate to another substrate

Transferases

What are the list of transferases?

  1. AST- Aspartate aminotransferase
  2. ALT- Alanine aminotransferase
  3. CK- Creatinine kinase
  4. GGT- Gamma glutamyl transferase
  5. α- GST- Glutathione-S-transferase
  6. GP- Glycogen phosphorylase
  7. PK- Pyruvate kinase

This class of enzyme catalyzes the hydrolysis of various bonds with the addition of water.

Hydrolases

List of Hydrolases

  1. ALP- Alkaline phosphatase
  2. ACP- Acid phosphatase
  3. AMY- Amylase
  4. PCHIE- Cholinesterase
  5. TRY- Trypsin
  6. CHY- Chymotripsin
  7. NTP - 5'nucleotidase
  8. LPS-Triacylglycerol lipase

This class of enzyme catalyzes the removal of groups from substrates without hydrolysis in which the product contains double bonds.

Lyases

This class of enzyme hydrolyzes bonds by elimination with the formation of a double bond.

Lyases

List of Lyases

  1. ALD-Aldolase

This class of enzyme catalyzes the interconversion of geometric, optical or positional isomers within a molecule.

Isomerases

Lists of Isomerases

  1. TPI- triosephosphate isomerase
  2. Glucose phosphate isomerase

This class of enzyme catalyzes the joining of two substrate molecules coupled with breaking of the pyrophosphate bond in ATP

Ligases/Synthetases

List of Ligases

  1. GSH-S - Glutathione synthetase

Test your knowledge on specific biologic proteins that catalyze biochemical reactions without being consumed or changed.

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