A novel carboxyl-terminal protease derived from Paenibacillus lautus CHN26 exhibiting high activities at multiple sites of substrates

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

A novel carboxyl-terminal protease derived from Paenibacillus lautus CHN26 exhibiting high activities at multiple sites of substrates. / Li, Yunxia; Pan, Yingjie; She, Qunxin; Chen, Lanming.

In: B M C Biotechnology, Vol. 13, 89, 2013.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Li, Y, Pan, Y, She, Q & Chen, L 2013, 'A novel carboxyl-terminal protease derived from Paenibacillus lautus CHN26 exhibiting high activities at multiple sites of substrates', B M C Biotechnology, vol. 13, 89. https://doi.org/10.1186/1472-6750-13-89

APA

Li, Y., Pan, Y., She, Q., & Chen, L. (2013). A novel carboxyl-terminal protease derived from Paenibacillus lautus CHN26 exhibiting high activities at multiple sites of substrates. B M C Biotechnology, 13, [89]. https://doi.org/10.1186/1472-6750-13-89

Vancouver

Li Y, Pan Y, She Q, Chen L. A novel carboxyl-terminal protease derived from Paenibacillus lautus CHN26 exhibiting high activities at multiple sites of substrates. B M C Biotechnology. 2013;13. 89. https://doi.org/10.1186/1472-6750-13-89

Author

Li, Yunxia ; Pan, Yingjie ; She, Qunxin ; Chen, Lanming. / A novel carboxyl-terminal protease derived from Paenibacillus lautus CHN26 exhibiting high activities at multiple sites of substrates. In: B M C Biotechnology. 2013 ; Vol. 13.

Bibtex

@article{78f29dc71bfd4165b128367a16b95be9,
title = "A novel carboxyl-terminal protease derived from Paenibacillus lautus CHN26 exhibiting high activities at multiple sites of substrates",
abstract = "Carboxyl-terminal protease (CtpA) plays essential functions in posttranslational protein processing in prokaryotic and eukaryotic cells. To date, only a few bacterial ctpA genes have been characterized. Here we cloned and characterized a novel CtpA. The encoding gene, ctpAp (ctpA of Paenibacillus lautus), was derived from P. lautus CHN26, a Gram-positive bacterium isolated by functional screening. Recombinant protein was obtained from protein over-expression in Escherichia coli and the biochemical properties of the enzyme were investigated.",
author = "Yunxia Li and Yingjie Pan and Qunxin She and Lanming Chen",
year = "2013",
doi = "10.1186/1472-6750-13-89",
language = "English",
volume = "13",
journal = "BMC Biotechnology",
issn = "1472-6750",
publisher = "BioMed Central Ltd.",

}

RIS

TY - JOUR

T1 - A novel carboxyl-terminal protease derived from Paenibacillus lautus CHN26 exhibiting high activities at multiple sites of substrates

AU - Li, Yunxia

AU - Pan, Yingjie

AU - She, Qunxin

AU - Chen, Lanming

PY - 2013

Y1 - 2013

N2 - Carboxyl-terminal protease (CtpA) plays essential functions in posttranslational protein processing in prokaryotic and eukaryotic cells. To date, only a few bacterial ctpA genes have been characterized. Here we cloned and characterized a novel CtpA. The encoding gene, ctpAp (ctpA of Paenibacillus lautus), was derived from P. lautus CHN26, a Gram-positive bacterium isolated by functional screening. Recombinant protein was obtained from protein over-expression in Escherichia coli and the biochemical properties of the enzyme were investigated.

AB - Carboxyl-terminal protease (CtpA) plays essential functions in posttranslational protein processing in prokaryotic and eukaryotic cells. To date, only a few bacterial ctpA genes have been characterized. Here we cloned and characterized a novel CtpA. The encoding gene, ctpAp (ctpA of Paenibacillus lautus), was derived from P. lautus CHN26, a Gram-positive bacterium isolated by functional screening. Recombinant protein was obtained from protein over-expression in Escherichia coli and the biochemical properties of the enzyme were investigated.

U2 - 10.1186/1472-6750-13-89

DO - 10.1186/1472-6750-13-89

M3 - Journal article

C2 - 24161150

VL - 13

JO - BMC Biotechnology

JF - BMC Biotechnology

SN - 1472-6750

M1 - 89

ER -

ID: 91592512