Literature DB >> 7851747

Characterization of a chitinase gene (chiA) from Serratia marcescens BJL200 and one-step purification of the gene product.

M B Brurberg1, V G Eijsink, I F Nes.   

Abstract

The nucleotide sequence of the chiA gene from Serratia marcescens strain BJL200 was determined. The gene was found to encode a protein of 563 amino acid residues, with a typical N-terminal signal peptide of 23 residues, that is cleaved off during export. The gene exhibited striking differences with two previously characterized chiA genes of S. marcescens in the region corresponding to amino acid residues 410-467 of the gene product. Periplasmic fractions of an Escherichia coli strain harbouring the cloned gene were used as starting material for the development of a fast, one-step purification protocol for the chitinase that is based on hydrophobic interaction chromatography.

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Year:  1994        PMID: 7851747     DOI: 10.1111/j.1574-6968.1994.tb07315.x

Source DB:  PubMed          Journal:  FEMS Microbiol Lett        ISSN: 0378-1097            Impact factor:   2.742


  15 in total

1.  The third chitinase gene (chiC) of Serratia marcescens 2170 and the relationship of its product to other bacterial chitinases.

Authors:  K Suzuki; M Taiyoji; N Sugawara; N Nikaidou; B Henrissat; T Watanabe
Journal:  Biochem J       Date:  1999-11-01       Impact factor: 3.857

2.  Slow Off-rates and Strong Product Binding Are Required for Processivity and Efficient Degradation of Recalcitrant Chitin by Family 18 Chitinases.

Authors:  Mihhail Kurašin; Silja Kuusk; Piret Kuusk; Morten Sørlie; Priit Väljamäe
Journal:  J Biol Chem       Date:  2015-10-14       Impact factor: 5.157

3.  Molecular cloning and purification of an endochitinase from Serratia marcescens (Nima).

Authors:  Alejandro Ruiz-Sanchez; Ramon Cruz-Camarillo; Ruben Salcedo-Hernandez; Jorge E Ibarra; Jose Eleazar Barboza-Corona
Journal:  Mol Biotechnol       Date:  2005-10       Impact factor: 2.695

4.  Aromatic residues in the catalytic center of chitinase A from Serratia marcescens affect processivity, enzyme activity, and biomass converting efficiency.

Authors:  Henrik Zakariassen; Berit Bjugan Aam; Svein J Horn; Kjell M Vårum; Morten Sørlie; Vincent G H Eijsink
Journal:  J Biol Chem       Date:  2009-02-25       Impact factor: 5.157

5.  Genetic analysis of the chitinase system of Serratia marcescens 2170.

Authors:  T Watanabe; K Kimura; T Sumiya; N Nikaidou; K Suzuki; M Suzuki; M Taiyoji; S Ferrer; M Regue
Journal:  J Bacteriol       Date:  1997-11       Impact factor: 3.490

6.  The predominant molecular state of bound enzyme determines the strength and type of product inhibition in the hydrolysis of recalcitrant polysaccharides by processive enzymes.

Authors:  Silja Kuusk; Morten Sørlie; Priit Väljamäe
Journal:  J Biol Chem       Date:  2015-03-12       Impact factor: 5.157

7.  A trimodular bacterial enzyme combining hydrolytic activity with oxidative glycosidic bond cleavage efficiently degrades chitin.

Authors:  Sophanit Mekasha; Tina Rise Tuveng; Fatemeh Askarian; Swati Choudhary; Claudia Schmidt-Dannert; Axel Niebisch; Jan Modregger; Gustav Vaaje-Kolstad; Vincent G H Eijsink
Journal:  J Biol Chem       Date:  2020-05-12       Impact factor: 5.157

8.  Chemical organization of the cell wall polysaccharide core of Malassezia restricta.

Authors:  Thomas Stalhberger; Catherine Simenel; Cécile Clavaud; Vincent G H Eijsink; Roland Jourdain; Muriel Delepierre; Jean-Paul Latgé; Lionel Breton; Thierry Fontaine
Journal:  J Biol Chem       Date:  2014-03-13       Impact factor: 5.157

9.  Molecular and biochemical characterization of an endochitinase (ChiA-HD73) from Bacillus thuringiensis subsp. kurstaki HD-73.

Authors:  J Eleazar Barboza-Corona; Dora M Reyes-Rios; Rubén Salcedo-Hernández; Dennis K Bideshi
Journal:  Mol Biotechnol       Date:  2007-12-14       Impact factor: 2.695

10.  Sequence and structural analysis of the chitinase insertion domain reveals two conserved motifs involved in chitin-binding.

Authors:  Hai Li; Lesley H Greene
Journal:  PLoS One       Date:  2010-01-13       Impact factor: 3.240

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