Chemistry Ch 19 Enzymes & Vitamins

Front 1

A protein or other molecule that acts as a catalyst for a biological reaction

Back 1

Enzyme

Front 2

A pocket in an enzyme with the specific shape and chemical makeup necessary to bind a substrate

Back 2

Active site

Front 3

A reactant in an enzyme-catalyzed reaction

Back 3

Substrate

Front 4

A nonprotein part of an enzyme that is essential to the enzyme's catalytic activity; a metal ion or a coenzyme

Back 4

Cofactor

Front 5

An organic molecule that acts as an enzyme cofactor

Back 5

Coenzyme

Front 6

The maximum number of substrate molecules acted upon by one molecule of enzyme per unit time(second)

Back 6

Turnover number

Front 7

Which enzyme has the the highest turnover number?

Back 7

Catalase

Front 8

What does Catalase catalyze?

Back 8

Decomposition of H2O2 to H2O and O2

Front 9

What is an example of an enzyme with a slow turnover number?

Back 9

Papain = Hydrolysis of peptide bonds

Front 10

An enzyme lacking its cofactor is a/an?

Back 10

apoenzyme

Front 11

An apoenzyme and its cofactor is called?

Back 11

holoenzyme

Front 12

What are the most useful enzyme assays done to diagnose a heart attack (MI)

Back 12

CPK = creatine phosphokinase
AST = aspartate transaminas
LDH = lactate dehydrogenase

Front 13

A compound that becomes an active enzyme after undergoing a chemical change

Back 13

Zymogen

Front 14

Name 3 zymogens produced in the pancreas to digest protein in small intestines

Back 14

Typsinogen
Chymotrypsinogen
Procelatase

Front 15

What makes the zymogen an active enzyme?

Back 15

An extra segment is snipped away from the end of the polypeptide

Front 16

What is Catalase specific for?

What rxns is this?

Back 16

the decomposition of hydrogen peroxide

oxidoreductases

Front 17

Give an example of an Absolute specificity

Back 17

Urease = breaks down urea to CO2 and NH3

Front 18

Give an example of a Stereochemical specificity

Back 18

Muscle lactate dehydrogenase only works on L-lactic acid, NOT on the D isomer

Fumarase adds water to fumaric acid and not to cis isomer maleic

Front 19

Give an example of group specificity

Back 19

Trypsin splits proteins on the carboxly side of lysine and arginine A.A.

Front 20

Give an example of linkage specifictiy

Back 20

Lipase acts on the carboxlyic ester bond in all fats and oils

Front 21

Give an example of constitution specificity

Back 21

Trypsin

Front 22

Explain Absolute specificity

Back 22

Only one substrate/ or type of reaction

Front 23

Explain Stereochemical specificity

Back 23

Only works on one of two stereoisomers

Front 24

Explain Group specificity

Back 24

works on different molecules containing the same structural features

Front 25

Explain Linkage specificity

Back 25

acts on a particular kind of bond

Front 26

Give an example of Oxidoreductases RXNS

Back 26

Lactate dehydrogenase

Front 27

Give an example of Transferases RXNS

Back 27

transaminases

Front 28

Give an example of Hydrolases RXNS

Back 28

sucrase

Front 29

Give an example of Lyases RXNS

Back 29

pyruvate decarboxylase

Front 30

Give an example of Isomerases RXNS

Back 30

phosphoglucose isomerase

Front 31

Give an example of Ligases RXNS

Back 31

DNA polymerases

Front 32

ENZYME KINETICS

at very low [S] ???

Back 32

-->ignore denominator
-->The curve falls off as [S} increases

Front 33

ENZYME KINETICS

At very high [S]???

Back 33

-->Km can be ignored, [S] terms cancel out
-->

Front 34

What does Km stand for?

Back 34

Michaielis constant,specific for E-S