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Specific biologic proteins that catalyze biochemical reactions without being consumed or changed.
Specific biologic proteins that catalyze biochemical reactions without being consumed or changed.
Enzymes
This is where plasma specific enzymes are synthesized
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 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 ________.
Coenzymes are second ________.
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Activators are inorganic ions that alters the spatial configuration of the enzyme for proper ________ binding.
Activators are inorganic ions that alters the spatial configuration of the enzyme for proper ________ binding.
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Metalloenzymes are inorganic ions attached to a ________.
Metalloenzymes are inorganic ions attached to a ________.
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Binding site consists of sequences of amino acids which determines____ of the enzyme
Binding site consists of sequences of amino acids which determines____ of the enzyme
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______ are nonprotein entities that must bind to particular enzymes before a reaction occurs.
______ are nonprotein entities that must bind to particular enzymes before a reaction occurs.
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______ are second substrates.
______ are second substrates.
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Activators include inorganic ions which may be ______ or anions.
Activators include inorganic ions which may be ______ or anions.
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______ are inorganic ions attached to a molecule.
______ are inorganic ions attached to a molecule.
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Active site consists of binding site and catalytic site. Binding site consists of sequences of amino acids which determines specificity of ______.
Active site consists of binding site and catalytic site. Binding site consists of sequences of amino acids which determines specificity of ______.
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What is the function of isoforms in terms of serum protein?
What is the function of isoforms in terms of serum protein?
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How do isoforms differ from isoenzymes?
How do isoforms differ from isoenzymes?
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What effect does the presence of isoforms have on enzyme activity?
What effect does the presence of isoforms have on enzyme activity?
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Which statement about isoforms is true?
Which statement about isoforms is true?
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How do isoforms contribute to enzyme diversity?
How do isoforms contribute to enzyme diversity?
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What are isoenzymes?
What are isoenzymes?
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What is a distinguishing factor between different isoenzymes?
What is a distinguishing factor between different isoenzymes?
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In what way do isoforms impact enzyme functionality?
In what way do isoforms impact enzyme functionality?
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How do isoenzymes differ from each other in terms of physical properties?
How do isoenzymes differ from each other in terms of physical properties?
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What differentiates isoenzymes in terms of their enzymatic properties?
What differentiates isoenzymes in terms of their enzymatic properties?
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Why is the assessment of specific tissue damage important in relation to isoenzymes?
Why is the assessment of specific tissue damage important in relation to isoenzymes?
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In the context of isoenzymes, what influences their ability to catalyze biochemical reactions?
In the context of isoenzymes, what influences their ability to catalyze biochemical reactions?
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What does the term 'stereoisomer specific' mean in relation to enzymes?
What does the term 'stereoisomer specific' mean in relation to enzymes?
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How does the enzyme commission classify enzymes?
How does the enzyme commission classify enzymes?
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Why were trivial recommended names assigned to enzymes?
Why were trivial recommended names assigned to enzymes?
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Which of the following best describes the function of enzymes?
Which of the following best describes the function of enzymes?
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What role do coenzymes play in enzyme reactions?
What role do coenzymes play in enzyme reactions?
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Why are enzymes effective in small concentrations?
Why are enzymes effective in small concentrations?
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How does the first digit of an EC numerical code categorize enzymes?
How does the first digit of an EC numerical code categorize enzymes?
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What is the role of plasma specific enzymes?
What is the role of plasma specific enzymes?
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Why are changes in enzyme concentration considered a sensitive diagnostic tool?
Why are changes in enzyme concentration considered a sensitive diagnostic tool?
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What characteristic defines the specificity of an enzyme's binding site?
What characteristic defines the specificity of an enzyme's binding site?
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Where are plasma specific enzymes synthesized?
Where are plasma specific enzymes synthesized?
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What is the effect of enzyme isoforms on physiologic functions?
What is the effect of enzyme isoforms on physiologic functions?
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Which class of enzyme catalyzes the interconversion of geometric, optical, or positional isomers within a molecule?
Which class of enzyme catalyzes the interconversion of geometric, optical, or positional isomers within a molecule?
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What is the main function of ligases or synthetases among the classes of enzymes mentioned?
What is the main function of ligases or synthetases among the classes of enzymes mentioned?
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What do the second and third digits of the EC code number represent for an enzyme?
What do the second and third digits of the EC code number represent for an enzyme?
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Which enzyme is responsible for converting glyceraldehyde 3 phosphate to dihydroxy acetone phosphate?
Which enzyme is responsible for converting glyceraldehyde 3 phosphate to dihydroxy acetone phosphate?
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What is a common feature of the substrate molecules joined by ligases or synthetases?
What is a common feature of the substrate molecules joined by ligases or synthetases?
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Which type of enzyme catalyzes the removal of groups from substrates without hydrolysis, resulting in products with double bonds?
Which type of enzyme catalyzes the removal of groups from substrates without hydrolysis, resulting in products with double bonds?
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Which of the following statements regarding Oxidoreductases is TRUE?
Which of the following statements regarding Oxidoreductases is TRUE?
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Creatine kinase is primarily found in which organ?
Creatine kinase is primarily found in which organ?
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Which enzyme was formerly known as SGPT?
Which enzyme was formerly known as SGPT?
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Which element is NOT listed as being part of the composition of enzymes?
Which element is NOT listed as being part of the composition of enzymes?
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Amylase is classified as which type of enzyme?
Amylase is classified as which type of enzyme?
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What is the approximate molecular weight range of enzymes as mentioned in the text?
What is the approximate molecular weight range of enzymes as mentioned in the text?
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What does the first digit on the EC code of an enzyme indicate?
What does the first digit on the EC code of an enzyme indicate?
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What type of proteins are enzymes classified as in the text?
What type of proteins are enzymes classified as in the text?
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Where are plasma specific enzymes primarily synthesized according to the text?
Where are plasma specific enzymes primarily synthesized according to the text?
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How do enzymes affect the speed of attaining equilibrium at any given temperature?
How do enzymes affect the speed of attaining equilibrium at any given temperature?
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What defines absolute specificity in enzymes?
What defines absolute specificity in enzymes?
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Which type of specificity involves the enzyme reacting with substrates containing similar structural groups?
Which type of specificity involves the enzyme reacting with substrates containing similar structural groups?
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What is the characteristic of enzymes that exhibit bond specificity?
What is the characteristic of enzymes that exhibit bond specificity?
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In enzyme classification, what distinguishes metalloenzymes?
In enzyme classification, what distinguishes metalloenzymes?
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What is the defining feature of a proenzyme/zymogen?
What is the defining feature of a proenzyme/zymogen?
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How does the binding site of an active site influence enzyme activity?
How does the binding site of an active site influence enzyme activity?
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How do allosteric sites differ from active sites in terms of their effect on enzyme activity?
How do allosteric sites differ from active sites in terms of their effect on enzyme activity?
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What is a key characteristic that distinguishes isoforms from isoenzymes?
What is a key characteristic that distinguishes isoforms from isoenzymes?
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How do different factors impact the plasma concentration of enzymes?
How do different factors impact the plasma concentration of enzymes?
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How are isoenzymes metabolized and excreted in biological systems?
How are isoenzymes metabolized and excreted in biological systems?
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This is the protein portion of the enzyme
This is the protein portion of the enzyme
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A complete and active system which is formed when an enzyme is bound with its respective coenzyme
A complete and active system which is formed when an enzyme is bound with its respective coenzyme
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Inactive form of an enzyme
Inactive form of an enzyme
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Enzyme combines with one substrate catalyzes one reaction
Enzyme combines with one substrate catalyzes one reaction
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Acts only on molecules with specific functional group
Acts only on molecules with specific functional group
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Enzyme reacts with substrates that contains similar structural group
Enzyme reacts with substrates that contains similar structural group
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Type of specificity of amino, phosphate, and methyl group
Type of specificity of amino, phosphate, and methyl group
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Enyzme acts on a particular steric or optical isomer.
Enyzme acts on a particular steric or optical isomer.
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Chemical reaction where carbohydrate is attached to a protein to form glycoprotein
Chemical reaction where carbohydrate is attached to a protein to form glycoprotein
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Chemical reaction that involves adding phosphate to an organic compound
Chemical reaction that involves adding phosphate to an organic compound
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Cleavage of proteins into smaller components.
Cleavage of proteins into smaller components.
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Cleavage of proteins into smaller components
Cleavage of proteins into smaller components
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What are the list of oxidoreductases
What are the list of oxidoreductases
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This class of enzyme catalyzes an electron transfer or oxidation-reduction reaction between two substrates
This class of enzyme catalyzes an electron transfer or oxidation-reduction reaction between two substrates
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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
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
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What are the list of transferases?
What are the list of transferases?
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This class of enzyme catalyzes the hydrolysis of various bonds with the addition of water.
This class of enzyme catalyzes the hydrolysis of various bonds with the addition of water.
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List of Hydrolases
List of Hydrolases
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This class of enzyme catalyzes the removal of groups from substrates without hydrolysis in which the product contains double bonds.
This class of enzyme catalyzes the removal of groups from substrates without hydrolysis in which the product contains double bonds.
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This class of enzyme hydrolyzes bonds by elimination with the formation of a double bond.
This class of enzyme hydrolyzes bonds by elimination with the formation of a double bond.
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List of Lyases
List of Lyases
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This class of enzyme catalyzes the interconversion of geometric, optical or positional isomers within a molecule.
This class of enzyme catalyzes the interconversion of geometric, optical or positional isomers within a molecule.
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Lists of Isomerases
Lists of Isomerases
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This class of enzyme catalyzes the joining of two substrate molecules coupled with breaking of the pyrophosphate bond in ATP
This class of enzyme catalyzes the joining of two substrate molecules coupled with breaking of the pyrophosphate bond in ATP
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List of Ligases
List of Ligases
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Study Notes
Enzymes and Proteins
- Specific biologic proteins that catalyze biochemical reactions without being altered or consumed are enzymes.
- Plasma-specific enzymes are synthesized primarily in the liver and other key organs.
- Cofactors are essential nonprotein entities that bind to enzymes before reactions can occur.
Types of Cofactors
- Coenzymes: Nonprotein organic molecules that assist enzymes by acting as second substrates.
- Activators: Inorganic ions that modify enzyme spatial configuration, enabling proper substrate binding.
- Metalloenzymes: Enzymes containing inorganic metal ions crucial for their catalytic activity.
Binding and Active Sites
- The binding site is a region in the enzyme consisting of amino acid sequences that determine its specificity for substrates.
- The active site includes both the binding site and the catalytic site.
Isoforms and Isoenzymes
- Isoforms are variants of enzymes that may perform similar functions but can differ in activity or stability.
- Isoenzymes are different enzyme forms that catalyze the same reaction but differ in kinetic or physical properties.
- The presence of isoforms can significantly affect enzyme activity and physiological functions.
Enzyme Classification and Functionality
- The Enzyme Commission (EC) classifies enzymes based on the types of reactions they catalyze.
- Enzymes are often effective even in small concentrations due to their ability to speed up reactions without being consumed.
- Enzymes can exhibit absolute specificity, reacting only with particular substrates, or relative specificity, reacting with similar functional groups.
Specific Classes of Enzymes
- Oxidoreductases: Catalyze oxidation-reduction reactions, involving electron transfer between substrates.
- Transferases: Facilitate the transfer of functional groups from one molecule to another.
- Hydrolases: Catalyze hydrolysis reactions, breaking bonds through the addition of water.
- Lyases: Remove substrates to form double bonds without hydrolysis.
- Isomerases: Interconvert geometric, optical, or positional isomers.
- Ligases: Catalyze the joining of two substrate molecules, involving ATP hydrolysis.
Enzyme Properties
- Enzymes’ molecular weights typically range significantly, reflecting diverse structures and functions.
- Changes in enzyme concentration can serve as sensitive diagnostic markers for tissue damage or disease states.
- Active site characteristics define an enzyme's specificity and influence its catalytic efficiency.
Biochemical Reactions and Enzyme Diversity
- Reactions that modify proteins include phosphorylation, glycosylation (adding carbohydrates), and cleavage into smaller components.
- The term 'stereoisomer specific' implies an enzyme's ability to act selectively on specific stereoisomers.
- Enzymes like amylase and creatine kinase show specific tissue localization, critical for understanding their roles in metabolism and pathology.
Additional Key Points
- Enzymatic reactions involving coenzymes illustrate the collaborative nature of biomolecules in metabolic processes.
- Isomerases and ligases play pivotal roles in more complex biosynthetic pathways, contributing to cellular metabolism and energy transfer.
- Understanding enzyme mechanisms and their varying isoforms aids in therapeutic development and biochemical research.
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Test your knowledge on specific biologic proteins that catalyze biochemical reactions without being consumed or changed.