Porth Ymchwil

Activity screening of environmental metagenomic libraries reveals novel carboxylesterase families

Allbwn ymchwil: Cyfraniad at gyfnodolyn › Erthygl › adolygiad gan gymheiriaid

StandardStandard

Activity screening of environmental metagenomic libraries reveals novel carboxylesterase families. / Popovic, Anna; Hai, Tran; Tchigvintsev, Anatoly et al.
Yn: Scientific Reports, Cyfrol 7, Rhif 44103, 44103, 03.2017.

Allbwn ymchwil: Cyfraniad at gyfnodolyn › Erthygl › adolygiad gan gymheiriaid

HarvardHarvard

Popovic, A, Hai, T, Tchigvintsev, A, Hajighasemi, M, Nocek, B, Khusnutdinova, AN, Brown, G, Glinos, J, Flick, R, Skarina, T, Chernikova, T, Yim, V, Bruls, T, Le Paslier, D, Yakimov, MM, Joachimiak, A, Ferrer, M, Golyshina, O, Savchenko, A, Golyshin, P & Yakunin, AF 2017, 'Activity screening of environmental metagenomic libraries reveals novel carboxylesterase families', Scientific Reports, cyfrol. 7, rhif 44103, 44103. https://doi.org/10.1038/srep44103

APA

Popovic, A., Hai, T., Tchigvintsev, A., Hajighasemi, M., Nocek, B., Khusnutdinova, A. N., Brown, G., Glinos, J., Flick, R., Skarina, T., Chernikova, T., Yim, V., Bruls, T., Le Paslier, D., Yakimov, M. M., Joachimiak, A., Ferrer, M., Golyshina, O., Savchenko, A., ... Yakunin, A. F. (2017). Activity screening of environmental metagenomic libraries reveals novel carboxylesterase families. Scientific Reports, 7(44103), Erthygl 44103. https://doi.org/10.1038/srep44103

CBE

Popovic A, Hai T, Tchigvintsev A, Hajighasemi M, Nocek B, Khusnutdinova AN, Brown G, Glinos J, Flick R, Skarina T, et al. 2017. Activity screening of environmental metagenomic libraries reveals novel carboxylesterase families. Scientific Reports. 7(44103):Article 44103. https://doi.org/10.1038/srep44103

MLA

Popovic, Anna et al. "Activity screening of environmental metagenomic libraries reveals novel carboxylesterase families". Scientific Reports. 2017. 7(44103). https://doi.org/10.1038/srep44103

VancouverVancouver

Popovic A, Hai T, Tchigvintsev A, Hajighasemi M, Nocek B, Khusnutdinova AN et al. Activity screening of environmental metagenomic libraries reveals novel carboxylesterase families. Scientific Reports. 2017 Maw;7(44103):44103. Epub 2017 Maw 8. doi: 10.1038/srep44103

Author

Popovic, Anna ; Hai, Tran ; Tchigvintsev, Anatoly et al. / Activity screening of environmental metagenomic libraries reveals novel carboxylesterase families. Yn: Scientific Reports. 2017 ; Cyfrol 7, Rhif 44103.

RIS

TY - JOUR

T1 - Activity screening of environmental metagenomic libraries reveals novel carboxylesterase families

AU - Popovic, Anna

AU - Hai, Tran

AU - Tchigvintsev, Anatoly

AU - Hajighasemi, Mahbod

AU - Nocek, Boguslaw

AU - Khusnutdinova, Anna N.

AU - Brown, Greg

AU - Glinos, Julia

AU - Flick, Robert

AU - Skarina, Tatiana

AU - Chernikova, Tatyana

AU - Yim, Veronica

AU - Bruls, Thomas

AU - Le Paslier, Denis

AU - Yakimov, Michail M.

AU - Joachimiak, Andrzej

AU - Ferrer, Manuel

AU - Golyshina, Olga

AU - Savchenko, Alexei

AU - Golyshin, Peter

AU - Yakunin, A. F.

N1 - UK Biotechnology and Biological Sciences Research Council (BBSRC) Grant BB/M029085/1.

PY - 2017/3

Y1 - 2017/3

N2 - Metagenomics has made accessible an enormous reserve of global biochemical diversity. To tap into this vast resource of novel enzymes, we have screened over one million clones from metagenome DNA libraries derived from sixteen different environments for carboxylesterase activity and identified 714 positive hits. We have validated the esterase activity of 80 selected genes, which belong to 17 different protein families including unknown and cyclase-like proteins. Three metagenomic enzymes exhibited lipase activity, and seven proteins showed polyester depolymerization activity against polylactic acid and polycaprolactone. Detailed biochemical characterization of four new enzymes revealed their substrate preference, whereas their catalytic residues were identified using site-directed mutagenesis. The crystal structure of the metal-ion dependent esterase MGS0169 from the amidohydrolase superfamily revealed a novel active site with a bound unknown ligand. Thus, activity-centered metagenomics has revealed diverse enzymes and novel families of microbial carboxylesterases, whose activity could not have been predicted using bioinformatics tools.

AB - Metagenomics has made accessible an enormous reserve of global biochemical diversity. To tap into this vast resource of novel enzymes, we have screened over one million clones from metagenome DNA libraries derived from sixteen different environments for carboxylesterase activity and identified 714 positive hits. We have validated the esterase activity of 80 selected genes, which belong to 17 different protein families including unknown and cyclase-like proteins. Three metagenomic enzymes exhibited lipase activity, and seven proteins showed polyester depolymerization activity against polylactic acid and polycaprolactone. Detailed biochemical characterization of four new enzymes revealed their substrate preference, whereas their catalytic residues were identified using site-directed mutagenesis. The crystal structure of the metal-ion dependent esterase MGS0169 from the amidohydrolase superfamily revealed a novel active site with a bound unknown ligand. Thus, activity-centered metagenomics has revealed diverse enzymes and novel families of microbial carboxylesterases, whose activity could not have been predicted using bioinformatics tools.

U2 - 10.1038/srep44103

DO - 10.1038/srep44103

M3 - Article

VL - 7

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

IS - 44103

M1 - 44103

ER -