Enzyme

By: Engr. Vera Marie L. Lanaria

What are enzymes?

Proteins that are capable of catalyzing a reaction in which various substrate are converted to products through the formation of an intermediate enzyme-substrate complex. Organic catalysts

Source of enzyme?

They are produced by living cells (animals, plants, microorganisms) and are absolutely essential as catalyst in biochemical reactions

Function of an enzyme?

As a catalyst, it will increase the rate of reaction without themselves undergoing permanent chemical changes. The catalytic ability of enzymes is due to its particular protein structure

Advantages..

very efficient catalysts environmentally acceptable act under mild conditions highly specific

Disadvantages.

provided by nature in only one enantiomeric form require narrow operation parameters display their highest activities in water prone to inhibition phenomena may cause allergies may be expensive

Nomenclature of Enzymes

Originally enzymes were given nondescriptive names such as: rennin: curding of milk to start cheesemaking process pepsin: hydrolyzes proteins at acidic pH trypsin: hydrolyzes proteins at alkaline pH

Later, it was improved by adding the suffix ase to the name of the substrate with which the enzymes functions, or to the reaction that is catalyzed. Example: lactase: lactose glucose + galactose lipase: fat fatty acids + glycerol maltase: maltose glucose urease: urea + water 2NH3 + CO2 cellobiase: cellobiose glucose

Reaction which is catalyzed + ase Ex. glucose isomerase: glucose fructose glucose oxidase: D-glucose + O2 + H2O gluconic acid lactic acid dehydrogenase: lactic acid pyruvic acid

New Scheme in Nomenclature

By 1964, the International Enzyme Commission suggested that enzymes will be categorize into 6 major classes: 1) oxidoreductases 2) transferases 3) hydrolases 4) lyases 5) isomerases 6) ligases

EC 1 Oxidoreductases

Involved in redox reactions in which hydrogen, oxygen atoms or electrons are transferred between molecules Ex. EC 1.1.3.4 Glucose Oxidase -D-glucose + O2 D-glucose-1, 5-lactone + hydrogen peroxide

EC 2 Transferases

Catalyze the transfer of an atom or group of atoms between two molecules, but excluding such transfers classified in the other groups (e.g. oxidoreductases and hydrolases) or: transfer functional groups such as amino groups, a phosphate group, or a two-carbon group (acetyl), between molecules Ex. EC 2.6.1.1 Aspartate Aminotransferases L-aspartate: 2-oxoglutarate aminotransferases

EC 3 Hydrolases

Involved in hydrolytic reactions and their reversal Ex. EC 3.4.23.4 Chymosin (also known as rennin) k-casein + H2O para-k-casein + caseino macropeptide

EC 4 Lyases

Involved in elimination reactions in which a group of atoms is removed from the substrate, often leaving double bonds Ex. EC 4.3.1.3 Histidine Ammonia-Lyase L-histidine urocanate + ammonia

EC 5 Isomerases

Catalyze molecular isomerizations Rearrange the atoms within a molecule but do not add or remove anything Include epimerases, racemases, and intramolecular transferases Ex. EC 5.3.1.5 Xylose Isomerases -D-glucopyranose -D-fructofuranose

EC 6 Ligases

Involved in the formation of a covalent bond joining two molecules together, coupled with the hydrolysis of a nucleoside triphosphate Ex. EC 6.3.2.3 Glutathione Synthetase ATP + L-glutamyl-L-cysteine + glycine ADP + phosphate + glutathione

Units of Enzyme Activity

Katal - the amount of enzyme needed to produce 1 mole of product per second under standard conditions U - the amount of enzyme needed to produce 1 mole of product per minute under standard conditions 1 Kat = 60,000,000 U

Assignment

Cite at least five specific enzymes and find its application. Research on the different types of amino acids, its names and structures.

Thank you for your attention!