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Butylmalonate is a transition state analogue for aminocylase I
Author(s) -
Röhm Klaus-Heinrich
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80718-5
Subject(s) - kinetics , reaction rate constant , chemistry , dissociation (chemistry) , dissociation constant , molecular mechanics , steady state (chemistry) , yield (engineering) , catalysis , transition state analog , stereochemistry , thermodynamics , crystallography , computational chemistry , molecular dynamics , biochemistry , active site , physics , receptor , quantum mechanics
Butylmalonate (butyl propanedioic acid) is a slow‐binding inhibitor of porcine renal aminoacylase I (EC 3.5.1.14), causing transients of activity with half‐times of more than 10 min. At 25°C and pH 7.0, the dissociation rate of the complex is approximately 6 × 10 −4 s −1 , while the rate constant of complex formation is in the order of 20 M −1 ·s −1 . In good agreement with these data, steady‐state kinetics yield an estimated inhibition constant around 100 μM. Molecular mechanics calculations showed that conformation and charge distribution of butylmalonate are strikingly similar to those of the putative transition state of aminoacylase catalysis.