Enzymes                             acceleraterales
ctity
                                                                                              EnzymeA
                                           n
                                               chinetics                                  E
                                                                                                   µ
Enzymes are          biological catalysts
 Lower
           Es do not alter             ya
                                                                                                SG
                                                                                                         2
 catalyze only thermodynamically
                                            favorable
  reins
 Bindspecificsubstrates catalyze specific reins
                                                highyield
 Subjectto regulation
kinetics
   A            P             V rateofproductformation or reaction consumption per unit time
Rate law                  KCA         whatorder rxn        1storder
                          9
                      rateconstant
Enzyme kinetics
           ki                                 Remember
                       Kz EtP
   Ets              ES                                             k
                                               ko CE
                                                   TES                   i
           k    i
                     p                                           KT
                    Enzymesubstrate
                        complex
        KEE           s       2ndorder rxn
  MichaelisMenten Model
                                                            Allosteric enzymes are an exception
       Vmax
                                                            to MichealsMenten model due to
   n                                  athff
velocity
           r                                                 2 t subunits activesites
                      1                                    Equation
                      i    CD
                                                                                VmaxEs3
  Atlow s                  AthighCs zero                   vofproof.dz
Forderkinetics            order kinetics                                          KartEs
       a Cs               rateindependentof                Derivedfrom
                                                                                  generic enzymecatalyzed xn
                                                            Represents
                                                                             velocity   ofentire r n notjust Ets EES
                                                           Based on      a few assumptions
  Assumption
RapidEquilibrium            Ks KD              Ks   CEfe.gg            k        idks   TAffinity     M
   ki          KZ       dissociation           KD                      K
      ofCES
dissociation             constant
to E ED is              5 conc atwhich
muchfasterthan
conversiontoCE   Ep    501of E exists
                       as ES
aka Krisratelimiting
                                                                           e.s
  s.gs eca             m                       km kztk             i             dkm 4Affinity       M
RateofformationFEES    Michaelis
                            constant                         k
                 of
                                                        Formation
                                                                  rakes
     of
  Rate breakdown CES
                        s atwhichthe              km is Ks
   CES quickly         enzymeis at                      if
  reaches aconstant
                            YzVmax                  K        Kz
Kz Keat ifIfdd         Roat_Vm                  catalytic
                                                                                 Rkat ratalytic      Sec
                                   E   n                         seat
   TurnoverNumber                               Efficiency
                                                                  km                    efficiency
                                       p
    smartness
 convertedto product
                                       II        Effi            ns.wy
                                                                     m      s
                       vma kz Et           n
  in 1unittimeatVmax                           Estimate
                                                         ofhow
  peractive site                               perfectanenzymeis