Literature DB >> 6460615

Lack of evidence for a tetrahedral intermediate in the hydrolysis of nitroanilide substrates by serine proteinases. Subzero-temperature stopped-flow experiments.

J L Markley, F Travers, C Balny.   

Abstract

We have used a stopped-flow apparatus to reinvestigate reports, based on the observation of "burst" kinetics, of an intermediate prior to the acyl-enzyme complex in hydrolysis reactions of anilides catalyzed by trypsin and elastase [M. W. Hunkapiller, M. D. Forgac and J. H. Richards (1976) Biochemistry 15, 5581-5588; D. D. Petkov (1978) Biochim. Biophys. Acta, 523, 538-541; A. L. Fink and P. Meehan (1979) Proc. Natl Acad. Sci. USA, 76, 1566-1569; P. Compton and A. L. Fink (1980) Biochem. Biophys. Res. Commun. 93, 427-431]. We studied the hydrolysis of several anilide substrates by bovine and porcine trypsin and porcine elastase between -30 degrees C and 20 degrees C. In no case did we record true "burst" kinetics. We show that confusion spectral changes can arise from incomplete mixing, thermal gradients, or heterogeneity of the substrate. We conclude that there is no solid spectroscopic evidence at present for the existence of a tetrahedral intermediate in the hydrolysis of amides by serine proteinases. The substrate N-acetyl-L-alanyl-L-prolyl-L-alanine 4-nitroanilide is a mixture of two isomers trans and cis about the L-alanyl-L-propyl peptide bond. It appears that elastase hydrolysis the cis isomer more rapidly than the trans isomer and this could lead to false "burst" kinetics. We describe the construction of the stopped-flow apparatus designed for cryoenzymology used for this work that has novel features and is adaptable to a variety of spectrophotometers. Solutions can be handled under anaerobic conditions. A window allows the drive syringes to be observed or exposed to light for photochemical experiments. The apparatus operates over the temperature range -35 degrees C to + 25 degrees C. The dead time is under 5 ms. A recording system is described that permits one to follow reactions over a wide time scale covering half-time of the order of several milliseconds to hours.

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Year:  1981        PMID: 6460615     DOI: 10.1111/j.1432-1033.1981.tb05726.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  7 in total

1.  Thermodynamics of the two step formation of horseradish peroxidase compound I.

Authors:  C Balny; F Travers; T Barman; P Douzou
Journal:  Eur Biophys J       Date:  1987       Impact factor: 1.733

2.  Activation volume and energetic properties of the binding of CO to hemoproteins.

Authors:  R Lange; I Heiber-Langer; C Bonfils; I Fabre; M Negishi; C Balny
Journal:  Biophys J       Date:  1994-01       Impact factor: 4.033

3.  Cryoenzymology of trypsin. A detailed kinetic study of the trypsin-catalysed hydrolysis of N-alpha-benzyloxycarbonyl-L-lysine p-nitrophenyl ester at low temperatures.

Authors:  J P Malthouse; A I Scott
Journal:  Biochem J       Date:  1983-12-01       Impact factor: 3.857

4.  Kinetics of electron transfer between cardiac cytochromes c1 and c.

Authors:  C H Kim; C Balny; T E King
Journal:  Proc Natl Acad Sci U S A       Date:  1984-04       Impact factor: 11.205

Review 5.  Current problems in mechanistic studies of serine and cysteine proteinases.

Authors:  L Polgár; P Halász
Journal:  Biochem J       Date:  1982-10-01       Impact factor: 3.857

6.  Cryobaroenzymic studies as a tool for investigating activated complexes: creatine kinase.ADP.Mg.nitrate.creatine as a model.

Authors:  C Balny; F Travers; T Barman; P Douzou
Journal:  Proc Natl Acad Sci U S A       Date:  1985-11       Impact factor: 11.205

7.  Chemical synthesis and papain-catalysed hydrolysis of N-alpha-benzyloxycarbonyl-L-lysine p-nitroanilide.

Authors:  N E Mackenzie; J P Malthouse; A I Scott
Journal:  Biochem J       Date:  1985-03-01       Impact factor: 3.857

  7 in total

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