Biochem

Front 1

Enzymes

Back 1

-proteins that are catalysts of biochemical reactions

-typically has a globular shape

-complex 3-D structure

Hint 1

Human pancreatic amylase

Front 2

Enzymes are biological catalyst

Back 2

-Increase the rate of reaction by lowering the energy of activation

-Catalyze nearly all the chemical reactions taking place in the cells of the body

-Have unique three dimensional shapes that fit the shapes of reactants

Hint 2

.

Front 3

Enzymes lower a reactions activation energy

Back 3

Hint 3

.

Front 4

First clear recognition was made by PAYEN and PERSOZ (around 1833)

Back 4

DIASTASE An alcohol precipitate of malt extract contained in a thermolabile substance that converted starch into sugar

Hint 4

Basic concept

Front 5

Basic concept

Back 5

DUCLAUX(1898)

use of -ase

J.B.Sumner (1924-1930)

first to crystallize

Front 6

Basic concept

Back 6

-more than 2500 biochemically important enzyme catalyzed reactions

-characterized by specifically for substrates

Front 7

Effectors

Back 7

Modulates an enzymes activity

-Activators, inhibitors,both, or depending on conditions

SINGLE ENZYME

-small single unit to large multiple units

Hint 7

Basic concept

Front 8

Catalase

Back 8

- found in animal and plant cell

-needed to speed up the breakdown of HYDROGEN PEROXIDE

-breaks it down to OXYGEN and WATER

Hint 8

the word equation for this looks like this

Front 9

Amylase

Back 9

-Found in saliva and in the pancreas

-breaks down enzymes

-breaks STARCH down to MALTOSE

Hint 9

Word equation

Front 10

Potato phosphorylase

Back 10

-synthesis enzyme (builds up)

-builds GLUCOSE-1-PHOSPHATE molecules into STARCH

-the formation of starch is tested using iodine solution

Hint 10

Front 11

Enzymes and Reactions

Back 11

Front 12

Catalytic efficiency

Back 12

High efficiency,10^3 to 10^17 faster than the corresponding uncatalyzed reactions

Front 13

Specificity

Back 13

High specificity, interacting with one or a few specific substrates and catalyzing only one type of chemical reaction

Front 14

Mild reaction conditions

Back 14

37°C, physiological pH, ambient atmospheric pressure

Front 15

Active site

(Part of catalysts)

Back 15

Part of the enzyme where the reactants bind, where the biochemical reactions occurs

Hint 15

basic parts of CATALYST

Front 16

Enzyme active site

Back 16

-amino acid side chains interact,metal ions

-various types of polar, non-polar, ionic interactions

Front 17

Active site

Back 17

Hint 17

Front 18

Lock and Key Model

Back 18

Front 19

Basic enzyme diagram

Back 19

Front 20

Parts of enzyme

-Small nonprotein molecules (subunits)

Back 20

-cofactors (metal ions)

Manganese,zinc, magnesium

-prosthetic group

(Covalently bonded to the enzyme)

Hint 20

Parts of an enzymes

Front 21

Holoenzyme

Back 21

=apoenzyme+nonprotein part

Hint 21

Parts of an enzymes

Front 22

Simple,conjugated

Back 22

Hint 22

Front 23

Cofactors

Back 23

Hint 23

Front 24

Enzymes -Cofactors

Back 24

Metal ions present in trace amounts

Front 25

Metal Ions as cofactors

Back 25

Front 26

Enzyme cofactors

Back 26

Coenzyme -non protein organic, maybe a vitamin

Hint 26

Front 27

Isoenzymes

Back 27

Catalyze the same reaction in different tissues in the body

Front 28

EXAMPLE

Lactate dehydrogenase

Back 28

Converts lactate to pyruvate,(LDH) consists of five isoenzymes

Front 29

Isoenzymes

Back 29

Different forms of an enzyme that catalyze the same reaction in different tissues in the body

-they have slight variations in the amino acid sequences of the subunits of their quaternary structure

Hint 29

Front 30

Classification of enzymes

Back 30

-IUPAC

-EC

-four integer EC number and a name

-common name: usually the principal specific reactant +-ase

-Does not follow any rule

*pepsin

*rhodanese

Front 31

Naming Enzymes

Back 31

Front 32

Classification of Enzymes

Back 32

Front 33

Oxidoreductase, Transferases and Hydrolases

Back 33

Hint 33

Front 34

Lyases, Isomerases and Ligases

Back 34

Hint 34

Front 35

Classification of Enzymes

Back 35

Front 36

Oxidoreductases

Back 36

Catalyze oxidation-reduction reactions.

Front 37

Transferases

Back 37

Catalyze group-transfer reactions

Front 38

Hydrolases

Back 38

Catalyze hydrolysis

Front 39

Lyases

Back 39

Catalyze lysis of a substrate

Front 40

Isomerases

Back 40

Catalyze structural change within a single molecule

Front 41

Ligases

Back 41

Catalyze ligation, or joining, of two substrates

Front 42

Facilitation of proximity

Back 42

Hint 42

Modes of Enhancement of rates of bond cleavage

Front 43

Covalent Catalysis

Back 43

Amino acid side chains: nucleophilic groups

Front 44

Covalent Catalysis: Acetoacetate Decarboxylase

Back 44

Front 45

Modes of Enhancement of rates of bond cleavage/ catalytic mechanisms

Back 45

-General acid-base Catalysis

-Binding Energy

-Metal-ion Catalysis

Front 46

Acid-Base Catalysis

Back 46

Hint 46

Front 47

Binding energy catalysis

(Method for improving the reactant rate)

Back 47

Front 48

Metal ion catalysis(method)

Back 48

Front 49

Modes of Enhancement of rates of bond cleavage/ catalytic mechanisms

Back 49

STRAIN, molecular DISTORTION, and shape change

Hint 49

Front 50

.

Back 50

Front 51

Uses of enzymes

Back 51

Hint 51

Front 52

Cont

Back 52

Hint 52