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Two novel deep-sea sediment metagenome-derived esterases: residue 199 is the determinant of substrate specificity and preference

Overview of attention for article published in Microbial Cell Factories, January 2018
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Title
Two novel deep-sea sediment metagenome-derived esterases: residue 199 is the determinant of substrate specificity and preference
Published in
Microbial Cell Factories, January 2018
DOI 10.1186/s12934-018-0864-4
Pubmed ID
Authors

Ying-Yi Huo, Shu-Ling Jian, Hong Cheng, Zhen Rong, Heng-Lin Cui, Xue-Wei Xu

Abstract

The deep-sea environment harbors a vast pool of novel enzymes. Owing to the limitations of cultivation, cultivation-independent has become an effective method for mining novel enzymes from the environment. Based on a deep-sea sediment metagenomics library, lipolytic-positive clones were obtained by activity-based screening methods. Two novel esterases, DMWf18-543 and DMWf18-558, were obtained from a deep-sea metagenomic library through activity-based screening and high-throughput sequencing methods. These esterases shared 80.7% amino acid identity with each other and were determined to be new members of bacterial lipolytic enzyme family IV. The two enzymes showed the highest activities toward p-nitrophenyl (p-NP) butyrate at pH 7.0 and 35-40 °C and were found to be resistant to some metal ions (Ba2+, Mg2+, and Sr2+) and detergents (Triton X-100, Tween 20, and Tween 80). DMWf18-543 and DMWf18-558 exhibited distinct substrate specificities and preferences. DMWf18-543 showed a catalytic range for substrates of C2-C8, whereas DMWf18-558 presented a wider range of C2-C14. Additionally, DMWf18-543 preferred p-NP butyrate, whereas DMWf18-558 preferred both p-NP butyrate and p-NP hexanoate. To investigate the mechanism underlying the phenotypic differences between the esterases, their three-dimensional structures were compared by using homology modeling. The results suggested that residue Leu199 of DMWf18-543 shortens and blocks the substrate-binding pocket. This hypothesis was confirmed by the finding that the DMWf18-558-A199L mutant showed a similar substrate specificity profile to that of DMWf18-543. This study characterized two novel homologous esterases obtained from a deep-sea sediment metagenomic library. The structural modeling and mutagenesis analysis provided insight into the determinants of their substrate specificity and preference. The characterization and mechanistic analyses of these two novel enzymes should provide a basis for further exploration of their potential biotechnological applications.

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Mendeley readers

The data shown below were compiled from readership statistics for 24 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 24 100%

Demographic breakdown

Readers by professional status Count As %
Student > Master 8 33%
Researcher 3 13%
Student > Ph. D. Student 3 13%
Student > Doctoral Student 1 4%
Student > Bachelor 1 4%
Other 3 13%
Unknown 5 21%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 6 25%
Agricultural and Biological Sciences 6 25%
Pharmacology, Toxicology and Pharmaceutical Science 1 4%
Business, Management and Accounting 1 4%
Immunology and Microbiology 1 4%
Other 2 8%
Unknown 7 29%

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 01 February 2018.
All research outputs
#7,810,980
of 12,448,635 outputs
Outputs from Microbial Cell Factories
#526
of 906 outputs
Outputs of similar age
#192,043
of 339,125 outputs
Outputs of similar age from Microbial Cell Factories
#1
of 1 outputs
Altmetric has tracked 12,448,635 research outputs across all sources so far. This one is in the 23rd percentile – i.e., 23% of other outputs scored the same or lower than it.
So far Altmetric has tracked 906 research outputs from this source. They receive a mean Attention Score of 3.7. This one is in the 32nd percentile – i.e., 32% of its peers scored the same or lower than it.
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