Oxidation Reaction in Microbial Cell

ONDATION - REDUCTION REACTIONS (a) - X In many a CO impound loses d electronic nydrogen one (ie, 2 hychogen atoms); thex rxns are com called clehydrogenation Cy me enzymes that Cat alyn one called dehy urogenuises In some, but not all bio. oxudation a Larben covalently band a to an O2 atom. The enzymes thut (atal 7 these oxidations one generally called oxidases. of Me 02 atom is curved directlyfoon m moleular O2 oxyginaxes ( X Every oxidatn must be awampamea by a reacure", in who an e- aceptor arquines the electrons removed by oxidate on 2n + 2e - ( thz - cn- (=0 iP (Mz- C - CEO 0- 2n+ +2e- O Lautan Lautate Pynivate dehydrogenine An oxidain reduce rxn; In this clehydrogenan Q es ala organ ons (me equivalent of 2 by chogenatons) one removed C-2 q lartate an alishol, to form pynivate, a ketone in cells the rxn is (atalyzia by lautati dehydrogman as me e's eve trank red tha Colcutor called 'nuolinarmde adenine amnules This cofator rxn is freely reversible ) pymorate can be fwm

ANTOONN is, /SOMERDATON LECIMINATION smoker common type of cellular rxn is an intramdeuver arrangement, m Which antron of e results in transport double bondy, rearra- dauble bonds Y Pr ey cremenzary is the forman of fruiture 6 phaphate from pnorphate i on r 49 5-01 H / 0 or O" comerance H on on U H on onono O Glu-6phospmen Inutox 6 pherphate this previously were saturatia (as in the enolase Tumunat of water introduces a (=C bond b/w 2 carbons rxn) Q1 o- 110 O- essolare 11- 110 C O - H2O no-cm O - cm o- 2 -phosphoglyceral A simple transporter of ac=C bond ocuse doing metabols. of me common fatty and Olic and 18 9 alcout WA C=0 S - COA Boudatn 3 Acety 1- COA (34ycues 12 H cle a3 c=0 Docleceno.yl CoA S- COA H Dodecenoy! C=O trans D2 S- WA Oodenny H COA B oual (h cucles) 6 Autul -COA

Olivic and as olloys LOA (A 17 example mere. an additional enzym enoyl-coA the Gomerax reposit request the double bond convesting (II 180 men to comer ,a normal in commidiate in p cridatn 12-h CIRCUP TRAVER be ACTIONS is Dr transfer of aye glyusys, up phosphory groups from mulleophill to another is common in uning cells Pul group changer generally / none me addut Tanwa phile to me curbony Camon of an aye gray to ferm 9 terrated mamediate o p- R- C C :X- R y P Y Y Tetrahecral intermediate PHOSPHORYL GROUP TRANSFER (a' t when a multrophile attake the elerophilic Phosphonya in AT P, a relatively stable pentaio valent Stirution ; forma as a rxn intermediate with departure of the learn group (ADP) the transfer of a phorphony go up is comp lite The large family of enzymes that catalyne pharphony gra transfers wim ATP as donor one called kinches ( meek Kanein to more) Henokman for eg: moves a phosphony from ATP to glinose ip 10 0 Adenine - Rebose - O-P- O- - O- P.K 11 o no-R 6 6. Gluose (ATP IP Adenin - Rebose - 0- - O- - O t IP O_ 6 - O-R O 0 (ADP) Gloose -6 Phosphale a phorphas enter

FACTORS AFFETTING AB ENZYME CATA LYSCS A to - suben all cone A+B m - Temp - pr AG C+D progress 01 7vr me mymer a inemical rvn in when Am AB' 4 lower the Energy of activation ; This B are figureran converted to use of The wanner sa adic complex 11 represented by The colored me represents the course of the rxn in me misera The emyme us autovatn D. energy received to reach 11 by Ea. of am lime enzyme Note mat The Ea is num lower in tatagled mxr Hyperbolic ame Vmax km 2 Vmax 2 V=Vman +S tm= substract coni Vmar recur a by me 2 km-15 enym to operate as nalfit more K velour in Vman- - The rate of rhman conc. toro dust formatn when Enzyme aring at th max velowey - Vmar. the emymil saturates cu insurance operatry as fan as possible Michaels menton Encliss This The dependence wive fitts M michaeles mentor eauam green Mefig. of emmone activity upon substicate conc. in when relates mm veroull (v) u me sebsonale conc. (5) ung the max velourful the men all unsam (km) Enume actually vones greatly w Hth changes in environmental and As wil be emphanzed of later, substrate conc. are usually withn (active, one The mon important beng me sebser ate low

Cells At very low submare come an enzyme makes slowey bw2 11 seldom contacts a subsidiate mclene to 11 more suchtrate molecules are present, an encyme senscrate 5 more open, us me rvn velouly Cuncains to in term of m rating product tomatr) 1) greate memor chen ver substi an wri Thus mirate of an enum cates rxn Tres win substrate wno Eventually former of in in substract conc. donot result in cl greater rose velouie hur me available enzyme moleules are hinang Missison amesting It to produce as r capity as possible. 10, the enume " saturatia, conc, are is a hyperbala 1) unful to know me substandin conc. am encyme needs fun un adequately Usually me Michaelis constant me substrate conc. rearned for the encyre to achieve ha maximal velouty, is used to as a meanne of the appear apporent affinity 9 an enzyme for in substrate The Low the km value, the when the substrate conc at which an enym Catalynn HS rxn. stage 1- Proteins polysawharides upids aminoau as menosawhands awyerol fattyauds Nmy DTP NADH rage 2 NADH pynivate FADN2 ONADH Autul wA urate stage 3 oxa Hometale remyon Aconimate AT throughout ma was NADH NADH= 3XA1P3) Fung Ava Inachinghic were and FADM = 9 PADU2 2ATP response everyone Isoutrau Inversary dehology w A CO2 GTP/ASP, IAP L Kelogutagabe 2 deliver 10Q =12 CO2 company ATP Glum n trargen us tounnomes Chain O2