TY - JOUR
T1 - On the kinetic distinction of ordered and random bireactant enzyme systems
AU - Frieden, Carl
N1 - Funding Information:
as useful as previously indicated in distinguishing different enzyme mechanisms although these cases would be mechanistically quite distinct. Acknowledgement. This research was supported in part by U.S. Public Health Service Grant AM-13332.
PY - 1976/2/9
Y1 - 1976/2/9
N2 - It is shown that under certain conditions it could be difficult to distinguish kinetically between an ordered or random addition of two substrates to an enzyme. An ordered mechanism in which substrate binding steps are in rapid equilibrium and which includes the formation of an inactive enzyme-second substrate complex from both directions is indistinguishable by initial velocity, product inhibition, or alternate substrate kinetic studies from a mechanism involving random addition of substrates with ternary complex interconversion as the rate limiting step.
AB - It is shown that under certain conditions it could be difficult to distinguish kinetically between an ordered or random addition of two substrates to an enzyme. An ordered mechanism in which substrate binding steps are in rapid equilibrium and which includes the formation of an inactive enzyme-second substrate complex from both directions is indistinguishable by initial velocity, product inhibition, or alternate substrate kinetic studies from a mechanism involving random addition of substrates with ternary complex interconversion as the rate limiting step.
UR - http://www.scopus.com/inward/record.url?scp=0017261726&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(76)91232-8
DO - 10.1016/0006-291X(76)91232-8
M3 - Article
C2 - 1259739
AN - SCOPUS:0017261726
SN - 0006-291X
VL - 68
SP - 914
EP - 917
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -