Přehled o publikaci
2020
EnzymeMiner: automated mining of soluble enzymes with diverse structures, catalytic properties and stabilities
HON, Jiří; Simeon BORKO; Jan ŠTOURAČ; Zbyněk PROKOP; Jaroslav ZENDULKA et al.Basic information
Original name
EnzymeMiner: automated mining of soluble enzymes with diverse structures, catalytic properties and stabilities
Authors
HON, Jiří; Simeon BORKO; Jan ŠTOURAČ; Zbyněk PROKOP; Jaroslav ZENDULKA; David BEDNÁŘ; Tomas MARTINEK and Jiří DAMBORSKÝ
Edition
Nucleic Acids Research, Oxford, Oxford University Press, 2020, 0305-1048
Other information
Language
English
Type of outcome
Article in a journal
Country of publisher
United Kingdom of Great Britain and Northern Ireland
Confidentiality degree
is not subject to a state or trade secret
References:
Marked to be transferred to RIV
Yes
RIV identification code
RIV/00216224:14310/20:00117412
Organization
Přírodovědecká fakulta – Repository – Repository
UT WoS
EID Scopus
Keywords in English
PROTEIN; SEARCH
Links
EF17_043/0009632, research and development project. LM2015047, research and development project. LM2018140, research and development project. 814418, interní kód Repo. 857560, interní kód Repo.
Changed: 16/2/2023 04:23, RNDr. Daniel Jakubík
Abstract
In the original language
Millions of protein sequences are being discovered at an incredible pace, representing an inexhaustible source of biocatalysts. Despite genomic databases growing exponentially, classical biochemical characterization techniques are time-demanding, cost-ineffective and low-throughput. Therefore, computational methods are being developed to explore the unmapped sequence space efficiently. Selection of putative enzymes for biochemical characterization based on rational and robust analysis of all available sequences remains an unsolved problem. To address this challenge, we have developed EnzymeMiner-a web server for automated screening and annotation of diverse family members that enables selection of hits for wet-lab experiments. EnzymeMiner prioritizes sequences that are more likely to preserve the catalytic activity and are heterologously expressible in a soluble form in Escherichia coli. The solubility prediction employs the in-house SoluProt predictor developed using machine learning. EnzymeMiner reduces the time devoted to data gathering, multi-step analysis, sequence prioritization and selection from days to hours. The successful use case for the haloalkane dehalogenase family is described in a comprehensive tutorial available on the EnzymeMiner web page.