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Understanding promiscuous amidase activity of an esterase from Bacillus subtilis
Univ Greifswald, Dept Biotechnol & Enzyme Catalysis.
Univ Greifswald, Dept Biotechnol & Enzyme Catalysis.
KTH, Skolan för bioteknologi (BIO), Biokemi.
KTH, Skolan för bioteknologi (BIO), Biokemi.
Vise andre og tillknytning
2008 (engelsk)Inngår i: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 9, nr 1, s. 67-69Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Water works. Bacillus subtilis esterase BS2 is a promiscuous esterase that shows amidase activity. This amidase activity was shown to depend on a hydrogen-bond network with the substrate amide hydrogen (indicated by arrow). When this stabilising hydrogen bond network was removed by a point mutation, the amide activity was significantly lowered in comparison with the esterase activity. (Figure Presented)

sted, utgiver, år, opplag, sider
2008. Vol. 9, nr 1, s. 67-69
Emneord [en]
amidases, Bacillus subtilis, catalysis, esterases, molecular modeling
HSV kategori
Identifikatorer
URN: urn:nbn:se:kth:diva-14181DOI: 10.1002/cbic.200700521ISI: 000252292200013PubMedID: 18022973Scopus ID: 2-s2.0-38149041619OAI: oai:DiVA.org:kth-14181DiVA, id: diva2:331473
Merknad
QC 20100722Tilgjengelig fra: 2010-07-22 Laget: 2010-07-22 Sist oppdatert: 2020-05-11bibliografisk kontrollert
Inngår i avhandling
1. Enzyme substrate solvent interactions: a case study on serine hydrolases
Åpne denne publikasjonen i ny fane eller vindu >>Enzyme substrate solvent interactions: a case study on serine hydrolases
2008 (engelsk)Doktoravhandling, med artikler (Annet vitenskapelig)
Abstract [en]

Reaction rates and selectivities were measured for transacylation of fatty acid esters in solvents catalysed by Candida antarctica lipase B and by cutinase from Humicola insolens. With these enzymes classical water-based enzymology can be expanded to many different solvents allowing large variations in interaction energies between the enzymes, the substrates and the surrounding. Further ,hydrolysis reactions catalysed by Bacillus subtilis esterase 2 were investigated.

Thermodynamics analyses revealed that the enzyme contribution to reaction rate acceleration compared to acid catalysis was purely entropic. On the other hand, studies of differences in activation entropy and enthalpy between enantiomers and between homologous esters showed that high substrate specificity was favoured by enthalpic stabilisation.

Solvent was found to have a profound effect on enzyme catalysis, affecting both reaction rate and selectivity. Differences in substrate solubility will impact enzyme specificity since substrate binding is an equilibrium between enzyme-bound substrate and substrate in free solution. In addition, solven tmolecules were found to act as enzyme inhibitors, showing both competitive and non-competitive behaviour.

In several homologous data series enthalpy-entropy compensation relationships were encountered. A possible extrathermodynamic relationship between enthalpy and entropy can easily be lost under co-varying errors propagated from the experiments. From the data in this thesis, one instance was found of a real enthalpy-entropy compensation that could be distinguished from statistical errors, while other examples could not be verified.

sted, utgiver, år, opplag, sider
Stockholm: KTH, 2008. s. 43
Serie
Trita-BIO-Report, ISSN 1654-2312 ; 2008:15
Emneord
lipase, esterase, specificity
HSV kategori
Identifikatorer
urn:nbn:se:kth:diva-4867 (URN)978-91-7415-094-0 (ISBN)
Disputas
2008-09-05, Stockholm, 13:00 (engelsk)
Opponent
Veileder
Merknad
QC 20100722Tilgjengelig fra: 2008-09-10 Laget: 2008-09-05 Sist oppdatert: 2011-07-07bibliografisk kontrollert

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