Cell Bio - Enzymes - Part 1

what processes or substrates are enzymes are being used?

Fermentation
Biotransformation
Pharmaceutical Industry

Fermentations

transformation of raw materials such as sugar, starch, etc. in industrial mixtures such as liquors, brewing

Biotransformations

transformation of defined precursors to a desired target product

Pharmaceutical industry

synthesis and modification of antibiotics

protease

degradation of proteins

cellulase

degradation of cellulose

lipase

degradation of lipids

amylase

conversion of starch to glucose

glucose isomerase

production of high glucose syrup

phytase

improve nutrient availability

xylanase

removal of lignin "bio bleaching

amylase (fruit)

removal of fruit starch haze

hydrolase

breakers for biopolymer gels

chymosin

clotting in cheese manufacture

pectinase

increased yields

what does life depend on?

a complex network of chemical reactions

what is a enzyme

special class of protein which has sites that bind and catalyze molecules in a reation

binding sites

very specific for a particular ligand
binding is reversible = there is an equilibrium between the free and bound ligand

Activation Energy

the energy needed to get chemical reactions started

what role do enzymes play on chemical reactions?

they greatly reduce the activation energy

what makes enzymes so important in a reaction

they show a high selectivity and usually catalyze only one specific reaction

most reactions in the body are mediated by what?

enzymes

enzymes

protein catalists that increase the rate of reactions (velocity) without being changed in the process

Substrate

enzyme reactants Glucose is a substrate of the enzyme glucokinase

Synthetase

requires ATP

synthase

no ATP required

Phosphatase

uses water to remove phosphoryl group

Phoshorylase

uses Pi to break a bond and generate a phosphorylated product

Dehydrogenase

NAD+/FAD is an electron acceptor in a redox reaction

oxidase

O2 is the acceptor, and oxygen atoms are not incorporated into substrate

oxygenase

one or both oxygen atoms are incorporated

what are the major classes of enzymes

Oxidoreductases
Transferases
hydrolases
lyases
iosomerases
ligases
polymerases
proteases
kinases
ATPase
synthases
phosphate

Oxidoreductases

catalyze reactions in which one molecule is oxidized while the other is reduced

Transferases

transfer carbon, nitrogen or phosphate containing groups

Hydrolases

enzymes that catalyze a hydrolytic cleavage reaction (nucleases and proteases)

Lyases

catalyze the cleavage of C-C, C-S, and C-N bonds

Isomerases:

catalyze the rearrangement of bonds within a single molecule

Ligases

Join together (ligate) two molecules in an energydependent process (DNA ligase joins two DNA molecules)

Polymerases

catalyze polymerization reactions such as the synthesis of DNA and RNA

Proteases

break down proteins by hydrolyzing bonds between amino acids

Kinases

Catalyze the addition of phosphate groups to molecules

ATPases

Hydrolyze ATP (Na,K ATPase)

Synthases

synthesize molecules in anabolic reactions by condensing two smaller molecules together (ATP synthase)

Phosphatase

catalyze the hydrolytic removal of a phosphate group from a molecule ()

What are the properties of enzymes

Active sites/ specificity
efficient
presence of cofactors
regulation
location in the cell

Active Sites

special pocket called the 'active site' which has a high specificity

Efficiency

reactions catalyzed by enzymes are 103-108 times faster than uncatalyzed reactions

Specificity

enzymes interact with one of few substrates and catalyze only one type of chemical reaction

The presence of cofactors

some enzymes (holoenzymes) require cofactors (Cu2+, Fe2+,etc.)

holoenzyme

E + CF > active

apoenzyme

E - CF > inactive

Regulation

enzyme activity can be regulated

Location in the cell

Many enzymes are located in specific organelles in the cell
this helps the competition for the substrate or enabling more favorable condition

what is the transition state

the bonds are changing
the product is forming