Flashcards in Chapter 4 Definitions/Concepts Deck (53)
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1
Cofactors
Nonprotein portions of an enzyme required for action
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Coenzyme
An organic cofactor required for enzyme activity
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Apoenzyme
An enzyme lacking its cofactor, coenzyme or prosthetic groups
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Holoenzyme
Apoenzyme and its cofactor, coenzyme or prosthetic groups. Essentially everything needed for catalytic activity
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Metalloenzyme
Apoenzyme and it's metal iron cofactor
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Prosthetic group
Tightly bound coenzyme
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Stereospecificity
The arrangement of the substrate atoms in three-dimensional space
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Active Site
Region on the enzyme that is directly responsible for interacting with the reacting molecules
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Proenzyme or Zymogen
An enzyme in its inactive form
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Six basic enzyme types
Oxidoreductases
Transferases
Hydrolase's
Lyases
Isomerases
Ligases or Synthertases
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Oxidoreductases
Redox reactions
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Transferases
The transfer groups of atoms
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Hydrolases
Hydrolysis
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Lyases
Addition to a double bond or information of a double bond
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Isomerases
The isomerization of molecules
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Ligases or Synthertases
The joining of two molecules
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Oxidation
The loss of one or more electrons, gain of oxygen or loss of hydrogen
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Reduction
Gain of one or more electrons, loss of oxygen or gain of hydrogen
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Aminotransferase
Transfers an amino group
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Phosphotransferase
Transfers of phosphoryl group
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Phosphatase
Catalyzes the hydrolysis of a monophosphate ester
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Peptidase
Catalyzes the hydrolysis of a peptide bond
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Deaminase
Aids in the removal of ammonia
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Decarboxylase
Catalyzes the loss of CO2
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Pyruvate carboxylase
Catalyzes the formation of a C-C bond
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Acetyl CoA Synthetase
Catalyzed formation of a C-S bond
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Enzyme-substrate complex
The substrate in some way binds to the enzymes active site
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Endergonic
Non spontaneous and energy is absorbed
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Michaelis constant
The substrate concentration producing a rate of one half the maximum velocity
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