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CC Lec > Enzymes > Flashcards

Enzymes Flashcards

1
Q

specific proteins that catalyze biochemical reaction without altering the equilibrium point of the reaction or being consumed or changed in composition.

A

Enzymes

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2
Q

Clinically significant enzymes are _____ protein

A

Intracellular

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3
Q

Other substances in the rxn that is converted to product

A

Substrate

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4
Q

number, type, and sequence of amino acids

A

Primary structure

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5
Q

Linear sequence of amino acid

A

Primary sequence

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6
Q

commonly formed arrangements stabilized by hydrogen bonds between nearby amino acids within the protein molecule.

A

Secondary structure

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7
Q

Secondary structure are commonly formed arrangements stabilized by _____

A

Hydrogen bonds

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8
Q

overall shape of the protein molecule.

A

Tertiary structure

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9
Q

results from the interaction of more than one protein molecule, or protein subunits, referred to as multimer, that functions as a single unit.

A

Quaternary structure

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10
Q

substance acted upon by the enzyme

A

Substrate

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11
Q

water free cavity, where the substrate interacts
with particular charged amino acid residues

A

Active site

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12
Q

cavity other than the active site

A

Allosteric site

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13
Q

Allosteric site is where ____ molecules binds

A

Regulator

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14
Q

cavity other than the active site; binds the regulator molecules

A

Allosteric site

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15
Q

What part of the enzyme does the substrate bind to?

A

Active site

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16
Q

enzymes with same function but exist in different forms

A

Isozenzyme

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17
Q

Example of an isoenzyme

A

Creatine Kinase

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18
Q

Forms of enzymes that were post-transcriptionally modified

A

Isoforms

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19
Q

Isoforms are _____ modified

A

Post transcriptionally

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20
Q

non-CHON molecule necessary for enzyme activity

A

Cofactors

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21
Q

Two types of cofactors

A

Activator
Coenzyme

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22
Q

Inorganic cofactor

A

Activator

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23
Q

Organic cofactor

24
Q

Coenzyme + enzyme =

A

Prosthetic group

25
Q

Prosthetic group is made out of

A

Coenzyme and enzyme

26
Q

Physical properties that differs isoenzymes from one another

A

Different amino acid composition
Electrophoretic mobility
Solubility
Resistance to inactivation

27
Q

Isoenzyme elevated in AMI

28
Q

CK-MB is elevated ___ hours after the onset heart attack

29
Q

Most abundant CK isoenzyme

31
Q

Most cathodic CK

32
Q

Most anodic CK isoenzyme

33
Q

coenzyme bound tightly to the enzyme

A

Prosthetic group

34
Q

enzyme portion that is activated by the
prosthetic group

35
Q

Prosthetic group + Apoenzyme

A

Holoenzyme

36
Q

Inactive precursor of an enzyme

A

Zymogen or Proenzyme

37
Q

IUB

A

International Union of Biochemistry

38
Q

EC numerical code containing ___ digits separated by decimal points.

39
Q

Enzyme Classification (6)

A

Oxidoreductases
Transferases
Hydrolases
Lyases
Isomerases
Ligases

40
Q

catalyze an oxidation– reduction reaction between two substrates

A

Oxidoreductases

41
Q

catalyze the transfer of a group other than hydrogen from one substrate to anothe

A

Transferases

42
Q

catalyze hydrolysis of various chemical bonds.

A

Hydrolases

43
Q

Catalyze removal of groups from substates without hydrolysis

44
Q

catalyze the interconversion of geometric, optical, or positional isomers..

A

Isomerases

45
Q

Catalyze the joining of two substrate molecules couples with breaking of pyrophosphate bond in ATP

46
Q

EC code for Lactate dehydrogenase

47
Q

Intermediate state formed after reactant exist bur before product is formed

A

Transition state

48
Q

This should be reached for a product to form

A

Energy barrier?

49
Q

Energy required to induce the transition state

A

Activation energy

50
Q

Who discovered the lock and key theory

A

Emil Fischer

51
Q

Who proposed the induced fit theory

A

Daniel Koshland

52
Q

Different types of enzyme specificity

A

Absolute specificity
Group specificity
Bond specificity
Stereoisomeric specificity

53
Q

ability of an enzyme to selectively bind to a particular substrate

A

Enzyme specificity

54
Q

Factors affecting enzyme activity

A

Substrate concentration
Enzyme concentration
pH
Temperature
Cofactors
Inhibitors

55
Q

Temperature increases enzyme activity by promoting what

A

Molecular collisions

CC Lec (3 decks)

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