Structural and functional characterization of mature forms of metalloprotease E495 from Arctic sea-ice bacterium Pseudoalteromonas sp. SM495.

E495 is the most abundant protease secreted by the Arctic sea-ice bacterium Pseudoalteromonas sp. SM495. As a thermolysin family metalloprotease, E495 was found to have multiple active forms in the culture of strain SM495. E495-M (containing only the catalytic domain) and E495-M-C1 (containing the c...

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Autores principales: Hai-Lun He, Jun Guo, Xiu-Lan Chen, Bin-Bin Xie, Xi-Ying Zhang, Yong Yu, Bo Chen, Bai-Cheng Zhou, Yu-Zhong Zhang
Formato: article
Lenguaje:EN
Publicado: Public Library of Science (PLoS) 2012
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Acceso en línea:https://doaj.org/article/5f7e7309ea5247c682967d2f1d4fc420
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