88 Questions
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
- LDH- Lactate dehydrogenase 2.. G-6-PDH- Glucose-6-phosphate dehyrdrogenase
- 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?
- AST- Aspartate aminotransferase
- ALT- Alanine aminotransferase
- CK- Creatinine kinase
- GGT- Gamma glutamyl transferase
- α- GST- Glutathione-S-transferase
- GP- Glycogen phosphorylase
- PK- Pyruvate kinase
This class of enzyme catalyzes the hydrolysis of various bonds with the addition of water.
Hydrolases
List of Hydrolases
- ALP- Alkaline phosphatase
- ACP- Acid phosphatase
- AMY- Amylase
- PCHIE- Cholinesterase
- TRY- Trypsin
- CHY- Chymotripsin
- NTP - 5'nucleotidase
- 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
- ALD-Aldolase
This class of enzyme catalyzes the interconversion of geometric, optical or positional isomers within a molecule.
Isomerases
Lists of Isomerases
- TPI- triosephosphate isomerase
- 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
- GSH-S - Glutathione synthetase
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