Clinchem2: Enzyme

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○ A soecific biologic protein that catalyze biochemical reactions without altering the equilibrium point of the raction or being consumed or changed in composition.

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Enzyme

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○ Enzyme that contains a specific amino a id sequence.

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primary structure

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○ The resultant polypeptide chain twisting.

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secondary structure

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folds

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tertiary structure

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○ Contains more than one polypeptide unit.

○ Refes ti the spatial relationship between the subunits.

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Quaternary structure

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○ Often a water-free cavity where the substance which the enzyme acts interacts with particular charged amino acid residues.

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Active site

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○ A cavity other than the active site.

○ May bind regulator molecule and thereby be significant to the basic enzyme structure.

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Allosteric site

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○ An enzyme is subjected to posttranslational modification.

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Isoform

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○ A non protein molecule that is necessary for enzyme activity.

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cofactor

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○ Organic cofactor.

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coenzyme

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○ Enzyme bound tightly to coenzyme.

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prosthetic grou

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○ Digestive enzyme that are originally secreted from the organ of production in a structurally inactive form.

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Proenzyme or Zymogen

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○ Assigns a systematic name to each enzyme, defining the substrate acted on, the reaction catalyzed, and, possibly, the name of any coenzyme involved in the reaction.

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IUB

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§ Catalyze an oxidation-reduction reaction between two substrates.

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Oxidoreductase

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§ Catalyze the transfer of a group other than hydrogen from one substrate to another.

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Transferases

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§ Catalyze hydrolysis of various bonds.

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Hydrolase

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§ Catalyze removal of groups from substrates without hydrolysis

§ Product contains double bond

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Lyases

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§ Catalyze the interconversion of geometric, optical or positional isomers.

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Isomerases

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§ Catalyzes the joining of two substrateolecules, coupled with breaking of the phosphate bond in ATP or a similar compound.

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Ligases

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○ In the EC code number it represents the subclass and subsubclass of the enzyme, respectively the divisions that are made according to criteria specific to the enzymes in the class.

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2nd and 3rd digit

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○ In the EC code number it represents the subclass and subsubclass of the enzyme, respectively the divisions that are made according to criteria specific to the enzymes in the class.

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2nd and 3rd digit

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○ The serial number specific to each enzyme in a subsub class.

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Final number

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○ In the EC code number it represents the subclass and subsubclass of the enzyme, respectively the divisions that are made according to criteria specific to the enzymes in the class.

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2nd and 3rd digit

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○ The serial number specific to each enzyme in a subsub class.

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Final number

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○ If the free or kinetic energy is HIGHER for reactants than for products.

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spontaneous chemical reaction

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○ In the EC code number it represents the subclass and subsubclass of the enzyme, respectively the divisions that are made according to criteria specific to the enzymes in the class.

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2nd and 3rd digit

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○ The serial number specific to each enzyme in a subsub class.

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Final number

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○ If the free or kinetic energy is HIGHER for reactants than for products.

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spontaneous chemical reaction

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○ Is the enrgy required to raise all molecules in 1 mol of a compound at a certain temperature to the transition state at the peak of the enrgy barrier.

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Actovation energy

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○ In the EC code number it represents the subclass and subsubclass of the enzyme, respectively the divisions that are made according to criteria specific to the enzymes in the class.

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2nd and 3rd digit

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○ The serial number specific to each enzyme in a subsub class.

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Final number

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○ If the free or kinetic energy is HIGHER for reactants than for products.

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spontaneous chemical reaction

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○ Is the enrgy required to raise all molecules in 1 mol of a compound at a certain temperature to the transition state at the peak of the enrgy barrier.

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Actovation energy

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○ A physical binding of a substrate to the active site of the enzyme.

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Enzyme substrate complex

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○ In the EC code number it represents the subclass and subsubclass of the enzyme, respectively the divisions that are made according to criteria specific to the enzymes in the class.

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2nd and 3rd digit

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○ The serial number specific to each enzyme in a subsub class.

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Final number

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○ If the free or kinetic energy is HIGHER for reactants than for products.

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spontaneous chemical reaction

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○ Is the enrgy required to raise all molecules in 1 mol of a compound at a certain temperature to the transition state at the peak of the enrgy barrier.

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Actovation energy

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○ A physical binding of a substrate to the active site of the enzyme.

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Enzyme substrate complex

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○ Meaning that the enzyme combine with only one substrate and catalyze only the one corresponding reaction.

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Absolute specificity

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○ In the EC code number it represents the subclass and subsubclass of the enzyme, respectively the divisions that are made according to criteria specific to the enzymes in the class.

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2nd and 3rd digit

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○ The serial number specific to each enzyme in a subsub class.

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Final number

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○ If the free or kinetic energy is HIGHER for reactants than for products.

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spontaneous chemical reaction

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○ Is the enrgy required to raise all molecules in 1 mol of a compound at a certain temperature to the transition state at the peak of the enrgy barrier.

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Actovation energy

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○ A physical binding of a substrate to the active site of the enzyme.

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Enzyme substrate complex

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○ Meaning that the enzyme combine with only one substrate and catalyze only the one corresponding reaction.

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Absolute specificity

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○ They combine with all the substrate containing a particular chemical group, such as phosphate ester.

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Group specific

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○ In the EC code number it represents the subclass and subsubclass of the enzyme, respectively the divisions that are made according to criteria specific to the enzymes in the class.

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2nd and 3rd digit

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○ The serial number specific to each enzyme in a subsub class.

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Final number

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○ If the free or kinetic energy is HIGHER for reactants than for products.

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spontaneous chemical reaction

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○ Is the enrgy required to raise all molecules in 1 mol of a compound at a certain temperature to the transition state at the peak of the enrgy barrier.

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Actovation energy

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○ A physical binding of a substrate to the active site of the enzyme.

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Enzyme substrate complex

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○ Meaning that the enzyme combine with only one substrate and catalyze only the one corresponding reaction.

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Absolute specificity

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○ They combine with all the substrate containing a particular chemical group, such as phosphate ester.

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Group specific

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○ Enzymes specific to chemical bonds.

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bond specificity

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○ In the EC code number it represents the subclass and subsubclass of the enzyme, respectively the divisions that are made according to criteria specific to the enzymes in the class.

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2nd and 3rd digit

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○ Hypothesized the role of substrate comcentration in the formation of the ES complex.

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Michaelis Meneten

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○ The recation rate is directly proportional to substrate concentration.

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First order kinetics

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○ When the reaction rate depends only on enzyme concentration.

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Zero order kinetics

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○ A constant for a specific enzyme and substrate under defined reaction conditions and is an expression of the relationship between the velocity of an enzymatic reaction and substrate concentration.

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Michaelis Menten concstnat

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○ Specifically the substrate concentration at which the enzyme yields half the possible maximum velocity.

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Michaelis Menten concstnat

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○ A double reciprocal plot of the Michaelis-Menten constant, which yoelds a straight line.

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Line weaver burk plot

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○ Rate pf denaturation.

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40-50

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• Nonprotein entities that must bind to a particular enzyme before a reaction occurs.

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cofactor

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○ Function by alternating the spatial configuration pf the enzyme for proper substrate binding, linking susbtrate to the enzyme or coenzyme or undergoing oxidation reduction.

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Actovator

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○ Serves as second substrate for enzymatic reaction.

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Coenzyme

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○ The serial number specific to each enzyme in a subsub class.

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Final number

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○ Physically bind to the active site of an enzyme and compete with the substrate for the active site.

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competitive inhibitor

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○ Binds the enzyme at a place other thepan the actove site and may be reversible in that some naturally present metabolic substances combine reversibly with certain enzyme.

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Non competitive inhibitor

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○ The inhibitor bind to the ES complex increasimg sibstrate comcentration.

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uncompetitive inhibitor

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○ Commonly a metallic ion, may bund enzyme simultaneously in noncompetitive inhibition.

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substrate and inhibitor

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two general methods used to measure the extent of an enzyme recation

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fized time and continous monitoring or kinetic assay

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reactants combined proceeds at designated time reaction then stops and a measurement is made

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Fixed rime mehod

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multiple measurements usually of ABS change are made during recation at a specific time

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continuous monitoring and kinetic assay

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units used to report enzyme level

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activity units

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as the amount of enzyme that will catalayze the reagtion of 1umol of substrate per minute under specified conditions

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International unit

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provide resolution of isoenzymes and isoform

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electrophoretic technique

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○ If the free or kinetic energy is HIGHER for reactants than for products.

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spontaneous chemical reaction

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may be a reagent when lactate or pyruvate concentration are evaluated

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Lactate dehydrogenase

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chemically bonded to absorbent sucha as agarose or ceratin type of cellulose

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Immobilized enzyme

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○ Is the enrgy required to raise all molecules in 1 mol of a compound at a certain temperature to the transition state at the peak of the enrgy barrier.

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Actovation energy

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○ A physical binding of a substrate to the active site of the enzyme.

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Enzyme substrate complex

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○ Meaning that the enzyme combine with only one substrate and catalyze only the one corresponding reaction.

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Absolute specificity

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○ They combine with all the substrate containing a particular chemical group, such as phosphate ester.

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Group specific

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○ Enzymes specific to chemical bonds.

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bond specificity

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○ Refers to the enzyme that predominantly combine with only one optical isomer of a certain compound.

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stereoisomer specificity

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• One of the mjaor influence in which the rate of an enzymatic reaction proceeds and whether the forward or reverse reaction occurs.

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substrate concentration