Substrate positioning in chitinase A, a processive chito-biohydrolase from<i>Serratia marcescens</i>

Norberg, Anne Line; Dybvik, Anette I.; Zakariassen, Henrik; Mormann, Michael; Peter‐Katalinić, Jasna; Eijsink, Vincent G. H.; Sørlie, Morten

doi:10.1016/j.febslet.2011.06.002

Cited by 25 publications

(55 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…lignolyticus SCF1. Phylogenetic analysis has shown that ECENHK_07430 and the synthetic Enterobacter chitinases are associated with the well-characterized Chitinase A in Serratia marcescens [62,63] (Figure 5), which has been demonstrated to control several important plant pathogenic fungi including Botrytis spp., Rhizoctonia solani, Fusarium oxysporum f. sp. cyclaminis and Sclerotinia spp.…”

Section: Resultsmentioning

confidence: 99%

Comparative Genome Analysis of Enterobacter cloacae

et al. 2013

View full text Add to dashboard Cite

The Enterobacter cloacae species includes an extremely diverse group of bacteria that are associated with plants, soil and humans. Publication of the complete genome sequence of the plant growth-promoting endophytic E. cloacae subsp. cloacae ENHKU01 provided an opportunity to perform the first comparative genome analysis between strains of this dynamic species. Examination of the pan-genome of E. cloacae showed that the conserved core genome retains the general physiological and survival genes of the species, while genomic factors in plasmids and variable regions determine the virulence of the human pathogenic E. cloacae strain; additionally, the diversity of fimbriae contributes to variation in colonization and host determination of different E. cloacae strains. Comparative genome analysis further illustrated that E. cloacae strains possess multiple mechanisms for antagonistic action against other microorganisms, which involve the production of siderophores and various antimicrobial compounds, such as bacteriocins, chitinases and antibiotic resistance proteins. The presence of Type VI secretion systems is expected to provide further fitness advantages for E. cloacae in microbial competition, thus allowing it to survive in different environments. Competition assays were performed to support our observations in genomic analysis, where E. cloacae subsp. cloacae ENHKU01 demonstrated antagonistic activities against a wide range of plant pathogenic fungal and bacterial species.

show abstract

Section: Resultsmentioning

confidence: 99%

Comparative Genome Analysis of Enterobacter cloacae

et al. 2013

View full text Add to dashboard Cite

show abstract

“…Although the Phe and Trp residues confer aromaticity, the bulky side chain (increased surface area) of Trp facilitates more interactions with the incoming substrate (14). The Trp also might assist in correct positioning and guiding of the sugar molecule into the active site (37). The increased TG by F64W for 60 min and then a gradual decrease may be because the sugar molecules with higher DP will possibly have more interactions with the Trp residue.…”

Section: Relative Tg Activitymentioning

confidence: 99%

Transglycosylation by Chitinase D from Serratia proteamaculans Improved through Altered Substrate Interactions

Madhuprakash

Tanneeru

Purushotham

et al. 2012

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: SpChiD, a family 18 glycosyl hydrolase, transglycosylates chitooligosaccharides. Results: Transglycosylation of SpChiD was improved in terms of the quantity of TG products produced and the extended duration of TG. Conclusion:The new findings unravel possibilities of modulating chitinases for improved transglycosylation. Significance: Variants of SpChiD can be used to develop a bio-process for large scale production of longer chain chitooligosaccharides.

show abstract

“…The situation beyond subsite +2 for HCHT, AMCase, and ChiA, is less clear. Still, chito-oligosaccharide degradation by ChiA clearly show substrate binding affinity in a subsite +3 that has been linked to its endo-activity [21].…”

Section: Introductionmentioning

confidence: 99%

Analysis of productive binding modes in the human chitotriosidase

et al. 2013

Self Cite

View full text Add to dashboard Cite

a b s t r a c tHuman chitotriosidase (HCHT) is a family 18 chitinase that is an innate part of the immune system. We have mapped preferred productive binding modes of chito-oligosaccharide substrates to HCHT and the data show that HCHT has strong binding affinity in the +3 subsite. Moreover, HCHT shows anomer-specific binding affinities in subsites +2 and +3. These features could endorse HCHT with higher endo-activity and a higher transglycosylation potential.

show abstract

Substrate positioning in chitinase A, a processive chito-biohydrolase fromSerratia marcescens

Cited by 25 publications

References 37 publications

Comparative Genome Analysis of Enterobacter cloacae

Comparative Genome Analysis of Enterobacter cloacae

Transglycosylation by Chitinase D from Serratia proteamaculans Improved through Altered Substrate Interactions

Analysis of productive binding modes in the human chitotriosidase

Contact Info

Product

Resources

About