Enzymes

Question 1

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

Answer 1

Enzymes

Question 2

Clinically significant enzymes are _____ protein

Answer 2

Intracellular

Question 3

Other substances in the rxn that is converted to product

Answer 3

Substrate

Question 4

number, type, and sequence of amino acids

Answer 4

Primary structure

Question 5

Linear sequence of amino acid

Answer 5

Primary sequence

Question 6

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

Answer 6

Secondary structure

Question 7

Secondary structure are commonly formed arrangements stabilized by _____

Answer 7

Hydrogen bonds

Question 8

overall shape of the protein molecule.

Answer 8

Tertiary structure

Question 9

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

Answer 9

Quaternary structure

Question 10

substance acted upon by the enzyme

Answer 10

Substrate

Question 11

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

Answer 11

Active site

Question 12

cavity other than the active site

Answer 12

Allosteric site

Question 13

Allosteric site is where ____ molecules binds

Answer 13

Regulator

Question 14

cavity other than the active site; binds the regulator molecules

Answer 14

Allosteric site

Question 15

What part of the enzyme does the substrate bind to?

Answer 15

Active site

Question 16

enzymes with same function but exist in different forms

Answer 16

Isozenzyme

Question 17

Example of an isoenzyme

Answer 17

Creatine Kinase

Question 18

Forms of enzymes that were post-transcriptionally modified

Answer 18

Isoforms

Question 19

Isoforms are _____ modified

Answer 19

Post transcriptionally

Question 20

non-CHON molecule necessary for enzyme activity

Answer 20

Cofactors

Question 21

Two types of cofactors

Answer 21

Activator
Coenzyme

Question 22

Inorganic cofactor

Answer 22

Activator

Question 23

Organic cofactor

Answer 23

Coenzyme

Question 24

Coenzyme + enzyme =

Answer 24

Prosthetic group

Question 25

Prosthetic group is made out of

Answer 25

Coenzyme and enzyme

Question 26

Physical properties that differs isoenzymes from one another

Answer 26

Different amino acid composition Electrophoretic mobility Solubility Resistance to inactivation

Question 27

Isoenzyme elevated in AMI

Answer 27

CK-MB

Question 28

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

Answer 28

4-8 hours

Question 29

Most abundant CK isoenzyme

Answer 29

CK-MM

Question 31

Most cathodic CK

Answer 31

CK-MM

Question 32

Most anodic CK isoenzyme

Answer 32

CK-BB

Question 33

coenzyme bound tightly to the enzyme

Answer 33

Prosthetic group

Question 34

enzyme portion that is activated by the prosthetic group

Answer 34

Apoenzyme

Question 35

Prosthetic group + Apoenzyme

Answer 35

Holoenzyme

Question 36

Inactive precursor of an enzyme

Answer 36

Zymogen or Proenzyme

Question 37

IUB

Answer 37

International Union of Biochemistry

Question 38

EC numerical code containing ___ digits separated by decimal points.

Answer 38

Four

Question 39

Enzyme Classification (6)

Answer 39

Oxidoreductases Transferases Hydrolases Lyases Isomerases Ligases

Question 40

catalyze an oxidation– reduction reaction between two substrates

Answer 40

Oxidoreductases

Question 41

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

Answer 41

Transferases

Question 42

catalyze hydrolysis of various chemical bonds.

Answer 42

Hydrolases

Question 43

Catalyze removal of groups from substates without hydrolysis

Answer 43

Lyases

Question 44

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

Answer 44

Isomerases

Question 45

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

Answer 45

Ligases

Question 46

EC code for Lactate dehydrogenase

Answer 46

1.1.1.27

Question 47

Intermediate state formed after reactant exist bur before product is formed

Answer 47

Transition state

Question 48

This should be reached for a product to form

Answer 48

Energy barrier?

Question 49

Energy required to induce the transition state

Answer 49

Activation energy

Question 50

Who discovered the lock and key theory

Answer 50

Emil Fischer

Question 51

Who proposed the induced fit theory

Answer 51

Daniel Koshland

Question 52

Different types of enzyme specificity

Answer 52

Absolute specificity Group specificity Bond specificity Stereoisomeric specificity

Question 53

ability of an enzyme to selectively bind to a particular substrate

Answer 53

Enzyme specificity

Question 54

Factors affecting enzyme activity

Answer 54

Substrate concentration Enzyme concentration pH Temperature Cofactors Inhibitors

Question 55

Temperature increases enzyme activity by promoting what

Answer 55

Molecular collisions