Flashcards in ME02 - ENZYMES : Introduction Deck (104)
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Energy required in order for reaction to occur
Activation Energy
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Determine the direction and equilibrium states of the reaction
Free energy changes
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Catalysts
Enzymes
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Properties of Enzymes
Reaction-specific
Substrate-specific
Stereo-specific
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Description for Enzymes
Increase reaction rates without being consumed or permanently altered
D sugars & L-amino acids
Typically proteins but can also be nucleotides
Affected by pH and temp
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Non-protein catalysts with ribonuclease & peptidyl transferase activity
Ribozymes
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What kind of gene is present in Ribozymes and its function
It contains autocatalytic RNA molecules that can adopt complex structures like proteins
8
Involved in Gene Therapy
Intron and tRNA processing
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Enzymes classified by reaction. Complete table
Class Type of Reaction Example
Hydrolase
Isomerase
Ligase/Polymerase
Lyase
Oxidoreductase
Transferase
Class Type of Reaction Example
Hydrolase Hydrolysis Lipase
Isomerase Rearrangement of atom Phosphoglucoisomerase
within a molecule
Ligase/Polymerase Joining two or more Acetyl-CoA synthetase
chemicals together
Lyase Splitting a chemical into Fructose 1,6-BP Aldolase
smaller parts w/o using water
Oxidoreductase Transfer of electrons or Lactic acid
H atoms from one molecule dehydrogenase
group to another
Transferase Moving a functional group Hexokinase
from one molecule group to another
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IUBMB Number corresponds to
1st number
2nd number
3rd number
4th number
1st number - Major class: Enzymes
2nd number - Subclass: Mechanism
3rd number - Sub-Subclass: Substrate Clase
4th number - Specific Substrate
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Catalyze the oxidation of a substrate with simultaneous reduction of another substrate or coenzyme
Transfer of electrons or H atoms from one molecule to another
Oxidoreductases
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Example of Oxidoreductase
Lactic acid-dehydrogenase - oxidizes lactic acid to form pyruvic acid during FERMENTATION
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Moving a functional group from one substrate/molecule to another
(may be anabolic)
Transferase
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Example of Transferase
Hexokinase - transfers phosphate from ATP to glucose in the first step of glycolysis
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Break single bonds (ester, ether, peptide or glycosidic) by the addition of water
This is Catabolic
Hydrolysis
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Example of Hydrolysis
Lipase - breaks down lipid molecules
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Form or cleave bonds with group elimination non hydrolytically
Splitting a chemical into smaller parts without using water
Lyase
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How does LYASE catalyze cleavage of C-C, C-O, C-N, and other covalent bonds
By atom elimination and generating double bonds
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Example of Lyase
Fructose 1,6-bisphosphate aldolase - splits fructos into G3P and DHAP
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Carry out intramolecular rearrangements
Catalyze geometric or structural changes within a molecule
(Neither catabolic or anabolic)
Isomerase
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Example of Isomerase
Phosphoglucoisomerase - converts glucose 6 phosphate into fructose 6 phosphate during glycolysis
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Link two substrates together usually with the Hydrolysis of ATP
Joining two or more chemicals together coupled with ATP hydrolysis
Ligase or Polymerase
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Example of Ligase/Phosphorylase
Acetyl-CoA synthetase - combines acetate and coenzyme A to form acetyl-CoA for the Krebs Cycle
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ENZYMES THAT HAS Catabolic Reactions
Hydrolases - Lipase
Lyase - Fructose 1,6-Bisphosphate aldolase
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ENZYMES THAT HAS Anabolic Reactions
Transferase - Hexokinase
Ligase/Polymerase - AcetylCoA synthetase
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ENZYMES THAT HAS Neither Catabolic and Anabolic Reactions
Isomerase - Phosphoglucoisomerase
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Where does Catalysis occur
The site on the enzyme where the substrate binds to
at the ACTIVE site
Active Site - cleft or pocket on the enzyme
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Events happening on the Active Site of Enzyme
Desolvation effects
Binds substrates properly for transition state formation
Binds cofactors & prosthetic groups
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Factors for substrates' transition state formation properly
Geometric & Electronic complementarity
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