\|there are HOo types of enzymes — © Extroceiiular = eg: amylase , protease, © ® Tntraceitwar ; Extraceilwar- The enzyme which are the cel! and FuncHon is calle fntrocellwar cell have Hoo Kypes— © Constituive - eg Grycolysis, TCA | @ stimulatory ConsHifulve— the enzyme Which are consrahHyssept and present inthe cell fs called consHit uve en: SHmmularory ~ When the Substrate is present due Fo sHmulation of substrate the specific enzyme ors such type of enzyme are called Stimulakory enzyme. 2-9. lactose degranated, f gluctocidase and pg permiage are enzyme: All prorein are enzyme exceph- Ribozymes + Bl This are not protein Discovery of enzyme first discayered by Edu Buchnner discovered in 18947 thak yeast extn could ferment sugar to alcohol iat The conversion of sugar to a aa ed zymase thi @ scanned with OKEN Scanner|| dimensional structure: molecular Weight j0,000 dalton Fo 10). enzyme accurate rate of reachon and jn the given reaction enzyme exhibit reversibility: e.g. guecinare enzyme comminion recommended the Unir QcHivity ts kKMeWN as Katal. iFisg defined as Molecule of substrate converted to product pei tscatied katal Turn over number Single Maleewle of enzyme | as turn over number of enzyme: enzyme have high degree of specificihy: enzyme are sensiHve ko various environmenke eg. Ferperature , pH enzyme is that enzyme catalyHe acHvi by smal! jon. eg. cofactor. Structure of enzyme. © scanned with OKEN Scanneris secondary structure the most Comm, is right handed this called as helix: *%- helix is Stabilized by hydrogen bond: * There are approximarely 3:6 amino acid are | turn: oe + peech of x helix 054m enzyme clhrarel Syn another form of secondary structure 76 pple also called B sheet ¥ + they OF2 antiparallel t TerHary Structure - this folding ring this Fogether active amino at are digrupt along with chain. e the tertiary structure enzyme is maintair funcHon by using different bond. e.g. diswphate bond hydrogen band hydrofobie bond jonic_ bond @ scanned with OKEN ScannerComplex protein. s enzyme forms of two parks: —jerliy Saas |) protein part catjed apoenzyme. 2) Non protein part cailed cofactor: 1 * the Whole enzyme is called holoenzyme. | ¢ the cofactar may be coenzyme or prosthetic gi Fo enzyme. * They are mainly vitamin ® derivative . 21g. FAD) * prosthetic group is inorganic thermostable, Fil attached to enzyme. * They are usually metal fon. e.g. Ca, an. * | tahibitor mL mMany substance alter the activity of ane combining with ikina Way that influence he Of substrate and Tks turnover number: oul reduce cn enzyme called inhibitor. @ scanned with OKEN Scanneracid Fo lysine. The enzyme has about i947. helical SegmenF- lysozyme has a compactly Folded conformaHon with host OF its hydro phoric group inside the globwar structure [away From Water and irs hydrophilic _R group outside Facing Fhe aqueous mediwn 8 conformation and 40-7). x The active site has six gubseh thal bind various gubstrad or inhibitor and the amino acid residue jocared ot the acHve site are 35, 52, 59, 69,69 and 107. chymotrysin- ahymotrysin is a mammalian digestive enzyme produc in the Small intestine Hhak catalyze Fhe hydrolysis OF proketh- chymotrysin is highly selective in Ths action os it catalyzed the hydrolysis of only those pepride bond that are present on Fhe carboxy! side of amino acld with apomaHc or bulky hydrophobic Q group. A molecule of chymotrysincensist OF 3 Short polypeptide chain of 13431 and 97amino acid Interehaln diswFide bonds “The secondary Structure of chymolrysin consist of several anriparalte) pleated sheet wegion and a title hellx grrucrure - + al @ scanned with OKEN ScannerEnzyme specificity. j «| one of the most important characterisHes of ehzying their speciticthy. the degree of specificity very Dim ay enzyme fn many cases enzyme act on only one Sub shay, land earied oul only one reacton. | In other cases Tr can act an smal) number alasely Telaig substances. 7 | enzyme exhibit A. Absouwlho speclficity , b. Group C. epee optical d- Geametrice) Absolure Specificity some enzyme are capable sf acting on only one gu land an example of Fhis is the enzyme urease thal act only on urea to produce ammonia apd carbon dioxide. Group .specificity. enzyme catalyze all reaction of Structwally related f Group of compound. &g. Hexokinase, factose dehydrog enaus. + enzyme Which catalyzed PhosphoryfaHon of variehy Sugar “optical Another important Fort of Specificity 1s seanin some enzyme Where o certain enzyme Will react with only: — one Of the tO optical isomers of a compound - a @ scanned with OKEN Scanner\ The oxidaHon of the p—amine acid fo the correspon ding keto acid by amino acid oxidase is an example opHcad Specificity: fhe enzyme thal exhibit optical specificity. Some might interconvert the Ho optical isomers of racemase that catalyst’ the tnterconversian behdeen L and D alanine. Geometrical io Geometrical specificity is observed in some enzyme exhibit Specificity toDards the cis and trans Form Anexample of this enzyme fumarase thal catalyze the VV 444 4A LE LSE interconversion Fumarie and malic acid: : rehae Mechanism of acHon of enzyme. “ion The mechanism of acHon of enzyme Das discovered by shorte Michalis and menten. enzyme accurate the Given reachon Without distroying iF SelP. In michalis — menten proposed enzyme and subsh combine Fo gwe enzyme gubstrare complex - The enzyme Substrate complex fo Aree enzyme and product. +S — ES — ETP The free enzyme then combine with fresh molecwe of Substrate Hhig may ¢onHinuos unhl all substrate Molecule are consumed. HoDever, steady Stake condition, is rch dhen fondard reacHon means formarion of ES Complex equal fe bacte Dard reacHon means breakdown of ES complex: — Me @ scanned with OKEN ScannerThis hypothesis proposed by Eni] 1898 according to Pisher catal yHc site o tigid structure. ’ |The substrate mejecule fit tne active Sike of leck $ Key relationship, Fhis made) Was develope explaln Specificity of enzyme. A Recording thig concepy CahalyHe site of enayry Complenentary in structure fo that of subs! buk the Most enzyme active Site fs nor model is nop accepted. 27 e > ‘% By: 7 7 en (FRY ¢ ANE ery 1 Ny 7) of a) Th z Fovyme igubshe 4 anit: Complies | a 8. Induced Fit hypothesig. ve This hypothesis Was Proposed by koshland according Fhig hyp thesia enzyme molecu werain ite original Shape and structure. a featbur ef tis _hypothesia is Fexi bility Site, Mina. @ scanned with OKEN ScannerEnzyme + Substrate Active Site of enzyme: \ The part of the enzyme combining with bh e is the acHve site- | Active site oharacrerisHes Fnclude [+ Pocket or defry in the surface of Khe enzym e Shape of enzyme active site is Complements Shape of the Ggubstrabe- r iF *The enzyme attract and holde the enzyi oon covalent inreracHion- * conformation of the acHye site de of enzyme. @ scanned with OKEN Scanner