University:
Swansea University
Course:
PM134 | Microbiology
Academic year:

2023
Views:

412

Pages:

4
Author:

Sanjeev K

EC Numbere Enzymes core classified into six different groups according to the reaction being catalyzed. Enzyme The Nomenclature was determined by the commission in 1961 (with the in 1992), hence all enzymes latest-cupdads having caused assigned an "Ec" number. Ec numbers are four digits for example a.b.c.d, where a clas b Sublass desouber the rean. c Sub-Subclass d Sub-Sub-Sublas. - used to distinguish bo diff-enzymes of the same function based on the actral Substrade in the rean. Ex For Alcohd. NAD+ oxidoreductare. Ecno: = ١٠١٠١٠١٠ Six classes EC 1- 1-Oxidoreductasce Catalyze the transfo of H/Oxygen atoms or I from one. Substract to anotha, also called oxidases, dehydrogenaso, Since there are redox' reane Or reductase. an I donor (acceptor is also required to complete the rean. eg- pyruvatet NADH + H Ladade + NAD+ Ec. 2. Tranferales LDH - Catalyze group transfor reans, luding Oxidoreductares (which excluding transfer hydrogen (oxygen and are. EC1) A-X + B B-X+A eg Apartate + Carbamaylstesphate EC 3. Hydrolase Aspantate (arbamoylaspartate + phosphate Catalyze hyctrolytic. Reaction. Includes lipares, Peptidases/ proteases. estorases, nitrilaser, A-X+H₂OX-OH + HA ag-Glu-6-phosphate + H₂O gastos ghuse-6-phosphotoge glucose + pi EC 4. Leyares Latalyze non hydrolytic (covered in Ec3) removal of functional gp from substrates, often creating a double bond in the product; or the reverse reaction, ie, bond. addn of function gps os across a double A-BA-B+X-Y. egL-malate fumarate Includes decarboxylase and aldolases Synthases in the addn direction. fumarate + H₂O in the removal direction, and EC 5. Isomerases Catalyzes isomerization reans. trans isomerizations. , including racemizations and cis eg. L-alanine Ec 6. Ligases Alanine yalemase. D-alanine. Catalyzes the synther's of various (mostly (-x) bonde, coupled with the breakdown of energy-containing substrates, us ATP. , usually eg: Glutamate + NHATP Glutamine synthetas Glutamine + ADP+ Pi Carbon atome encountered Oxdn states, depending Shares electron. in biochemistry can exist in five on the ademens with which loorbon CH2-CH Alkane Alcohol -CH2-CH애 0 -CH2- H(R) Aldehyde. (Ketone) -CH₂- -OH Carboxylic acid 0=c=0 Carbon dioxide. Oxan-Redni reactione free energy changes ore associated In many biological Oxdne, a compound loses two electrons and kowo hydrogen ions (that is, hoo hydrogen atoms); there. reactione core commonly called dehydrogenatione and the enzymes that Catalyse them are called dehydrogenaser. some, but not all biological Oxdne, a Carbon atom becomes covalently bonded to an oxygen aton. The enzymes that Catalyze there oxdne are generally called oxidave gen atom is derived or if the oxygen (02), oxygenase directly from moleculas oryg 701 Every oxdn must be acompanied by a redn, in which an e acceptor acquires the electrons removed CH3-CH- by oxdn. lactate lactata Pyruvate Dehydrogenase fig- oxdn redn rean. Lactate oxdn •pyruvate Here, in this dehydrogenation, 2 es and a Hydrogen ion (the equivalence of two hydrogen atomes) are removed from C-2 of lactate, an alcohol, to form pyruvate, a ketone. In cells, the reaction is catalyzed by lactate dehydrogenase, and the Is are transferred to a cofactor called nikotinamide adenine dinucleotide. This reaction is fully reversible. Pyruvate can be reduced by Ies from the cofactors.