A proposed update for the classification and description of bacterial lipolytic enzymes

Institute of Medical Microbiology, University hospital RWTH Aachen, Aachen, Germany
DOI
10.7287/peerj.preprints.27725v1
Subject Areas
Biochemistry, Biotechnology, Computational Biology, Microbiology
Keywords
lipase, lipolytic enzymes, carboxylesterase, alpha-beta fold, esterase, hydrolase
Copyright
© 2019 Hitch et al.
Licence
This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ Preprints) and either DOI or URL of the article must be cited.
Cite this article
Hitch TCA, Clavel T. 2019. A proposed update for the classification and description of bacterial lipolytic enzymes. PeerJ Preprints 7:e27725v1

Abstract

Bacterial lipolytic enzymes represent an important class of proteins: they provide their host species with access to additional resources and have multiple applications within the biotechnology sector. Since the formalisation of lipolytic enzymes into families and subfamilies, advances in molecular biology have led to the discovery of lipolytic enzymes unable to be classified via the existing system. Utilising sequence-based comparison methods, we have integrated these novel families within the classification system proposed by Arpigny and Jaeger (1999) and recently updated by Kovacic et al (2019) so that it now consists of 35 families and 11 true lipase subfamilies. Representative sequences for each family and subfamily have been defined as well as methodology for accurate comparison of novel sequences against the reference proteins, facilitating the future assignment of novel proteins. Both the code and protein sequences required for integration of additional families are available at: https://github.com/thh32/Lipase_reclassification

Author Comment

This is a submission to PeerJ for review.

Supplemental Information

Similarity of reported novel lipolytic proteins against the accepted type proteins for each lipolytic family

Both enzymes and the similarity scores of interest are in bold when high (>60%) similarity was identified.

DOI: 10.7287/peerj.preprints.27725v1/supp-1

Pairwise comparison of similarity between novel lipolytic proteins

Both enzymes and the similarity scores of interest are in bold when high (>60%) similarity was identified.

DOI: 10.7287/peerj.preprints.27725v1/supp-2

Annotation of each studied lipolytic protein against the genome database

For each protein its publication date and isolation source were reported. Genome annotation was conducted at two levels of strictness and taxonomy of matches reported at both the family and genus level. Taxonomy was assigned using both the NCBI taxonomic assignments and the GTDB method.

DOI: 10.7287/peerj.preprints.27725v1/supp-3

BLAST based assignment of taxonomy for lipolytic enzymes without a genome match

For each protein the top 10 sequence matches reported against the NR database are reported, including the source organism for each matching sequence.

DOI: 10.7287/peerj.preprints.27725v1/supp-4