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Probing Enzyme Promiscuity of SGNH Hydrolases


Leščić Ašler, Ivana; Ivić, Nives; Kovačić, Filip; Schell, Sabrina; Knorr, Janina; Krauss, Ulrich; Wilhelm, Susanne; Kojić-Prodić, Biserka; Jaeger, Karl-Erich
Probing Enzyme Promiscuity of SGNH Hydrolases // ChemBioChem, 11 (2010), 15; 2158-2167 doi:10.1002/cbic.201000398 (međunarodna recenzija, članak, znanstveni)


Naslov
Probing Enzyme Promiscuity of SGNH Hydrolases

Autori
Leščić Ašler, Ivana ; Ivić, Nives ; Kovačić, Filip ; Schell, Sabrina ; Knorr, Janina ; Krauss, Ulrich ; Wilhelm, Susanne ; Kojić-Prodić, Biserka ; Jaeger, Karl-Erich

Izvornik
ChemBioChem (1439-4227) 11 (2010), 15; 2158-2167

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
Autotransporter proteins; bacterial SNGH hydrolases; enzyme catalysis; promiscuity; selectivity

Sažetak
Several hydrolases of the SGNH superfamily, including the lipase SrLip from Streptomyces rimosus (Q93MW7), the acyl-CoA thioesterase I TesA from Pseudomonas aeruginosa (Q9HZY8) and the two lipolytic enzymes EstA (from P. aeruginosa, O33407) and EstP (from Pseudomonas putida, Q88QS0), were examined for promiscuity. These enzymes were tested against four chemically different classes of a total of 34 substrates known to be hydrolysed by esterases, thioesterases, lipases, phospholipases, Tweenases and proteases. Furthermore, they were also analysed with respect to their amino acid sequences and structural homology, and their phylogenetic relationship was determined. The Pseudomonas esterases EstA and EstP each have an N-terminal domain with catalytic activity together with a C-terminal autotransporter domain, and so the hybrid enzymes EstAN–EstPC and EstPN–EstAC were constructed by swapping the corresponding N- and C-terminal domains, and their hydrolytic activities were compared. Interestingly, substrate specificity and kinetic measurements indicated a significant influence of the autotransporter domains on the catalytic activities of these enzymes in solution. TesA, EstA and EstP were shown to function as esterases with different affinities and catalytic efficacies towards p-nitrophenyl butyrate. Of all the enzymes tested, only SrLip revealed lipase, phospholipase, esterase, thioesterase and Tweenase activities.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Biologija



POVEZANOST RADA


Projekt / tema
098-1191344-2943 - Protein-ligand međudjelovanja na atomnoj razini (Marija Luić, )

Ustanove
Institut "Ruđer Bošković", Zagreb

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus
  • MEDLINE


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  • MEDLINE
  • BIOBASE
  • Biochemistry & Biophysics Citation Index
  • Cambridge Scientific Abstracts
  • Cambridge Structural Database
  • ChemInform
  • Chemistry Citation Index
  • ChemWeb
  • CSA
  • Current Awareness in Bi


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