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Title 

The slow and tight binding of MR-387A to aminopeptidase N

Authors 

Myung Chul ChungHyo Kon ChunHo Jae LeeChoong Hwan LeeSu-Il KimYung Hee Kho

Publisher 

The Korean Society for Applied Microbiology

Issue Date 

1996

Citation 

Journal of Microbiology and Biotechnology, vol. 6, no. 4, pp. 250-254

Keywords 

aminopeptidase Nkinetic parameterMR-387Aslow and tight binding

Abstract 

MR-387A [(2S,3-R)-2-hydroxy-3-amino-4-phenylbutanoyl-L-valyl-L-prolyl-(2,4-trans)-L-4- hydroxyproline] reversibly inhibits aminopeptidase N (EC 3.4.11.2) in a process that is remarkable for its unusual degree of time dependence. The time required to inactivate the enzyme by 50% (t1/2) for establishing steady-state levels of EI* complex was approximately 5 minutes. This indicates that the inhibition is a slow-binding process. In dissociation experiments of EI* complex, enzymic activity was regained slowly in a quadratic equation, indicating that the inhibition of aminopeptidase N by MR-387A is tight-binding and reversible. Thus, the binding of MR-387A by aminopeptidase N is slow and tight, with Ki (for initial collision complex, EI) and K1* (for final tightened complex, EI*) of 2.2 × 10-8 M (from Lineweaver-Burk plot) and 4.4×10-10 M (from rate constants), respectively. These data indicate that MR-387 A and aminopeptidase N are bound approximately 200-fold more tightly in the final EI* complex than in the initial collision EI complex.

ISSN 

1017-7825

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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