Self-catalysis = autocatalysis
Enterokinase: trypsinogen Trypsin
Lactice acid dehydrogenase (LDH) = 5 isoenzymes.
Number of active sites of enzyme affect turnover number
3D shape of molecule β
(1) Spatial sit β tertiary structure Match shape of groove
(2) Bonding fit β present of active site in grooves
Induced fit theory β Koshland (enzyme e active site are more flexible)
Lock & key theory β Fischer
Change in arrangement of polypeptide chain within protein = Denaturation
Michaels constant km =>
Initial velocity V0 =
Carbonic anhydrase = fastest acting enzyme (low Ki, low enzyme inhibition so more active)
Prosthetic group + apoenzyme = Holoenzyme
(non-protein) (Protein)
Enzyme bromeclaim = pineapple
Catalytic efficiency = K cat (turnover no.)/Km.(michalies const)
Evolve O2 from tissue = peroxidase
Histidine decarboxylase = lyase (split) -> fumarase, Aldolase
Sulpha drug inhibit synthesis of folic acid in bacteria
Cyanide kill organism by inhibiting Cytochrome oxidase
Thomas tech β group I r RNA of tetrahymena thermophile could splice itself without help of any protein i.e. RNA can act as Catalyst (enzyme). 1982
1983 β Sydney altman & Norman pace β M/RNA port alone of E coli RNAase enzyme is sufficient for Catalysis, protein is needed for stabilization
1992 β Harry Noller β protein synthesis formation of peptide bond is catalyzed by 235 r RNA & not by protein peptidyl transferase
Calvin Melwin β in cyclotron strongly irritated CO2 & H2 end products were HCOOH, Succinic acid & Oxalic acid
Presence of abundant free O2 on earth today is not conductive to origin of life.
Coacervates - due to Zwitterionic nature, proteins formed colloidal hydrophilic Complexes
Homologous organ β Same origin & difference function β forelimbs of vertebrates, leg in insects, teeth of man, thorn of Bougainvillea & tendril of possiflora
Analogous organ - difference origin but same function β wing of bird, lead of plant & cladode of Ruscus.