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

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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Bibliographic Details
Main Authors: Hai-Lun He, Jun Guo, Xiu-Lan Chen, Bin-Bin Xie, Xi-Ying Zhang, Yong Yu, Bo Chen, Bai-Cheng Zhou, Yu-Zhong Zhang
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2012-01-01
Series:PLoS ONE
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22523598/pdf/?tool=EBI

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https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22523598/pdf/?tool=EBI

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