Bayer_2010_J.Mol.Microbiol.Biotechnol_18_181

Reference

Title : Indication for a new lipolytic enzyme family: isolation and characterization of two esterases from a metagenomic library - Bayer_2010_J.Mol.Microbiol.Biotechnol_18_181
Author(s) : Bayer S , Kunert A , Ballschmiter M , Greiner-Stoeffele T
Ref : J Molecular Microbiology Biotechnol , 18 :181 , 2010
Abstract :

We have isolated several novel esterase genes from a sheep rumen metagenomic library using the activity-based cluster screening approach as a highly efficient screening technology. The two most remarkable esterase genes, designated estGK1 and estZ3, were further examined. Sequence analysis of estGK1 and estZ3 revealed that they encoded proteins covering 322 and 317 amino acids, respectively. Both proteins were biochemically characterized. EstGK1 and EstZ3 have only minor overall sequence similarity to known esterases. We propose that, together with other hypothetical enzymes, they constitute a new family of lipolytic enzymes. EstGK1 harbors the catalytic serine in the conserved pentapeptide GHSQG, which is typical for lipases, whereas EstZ3 and several other hypothetical proteins contain the pentapeptide SHSQG, a new variation of the conserved motif in lipolytic enzyme families.

PubMedSearch : Bayer_2010_J.Mol.Microbiol.Biotechnol_18_181
PubMedID: 20530969
Gene_locus related to this paper: 9bact-d5l5q1 , 9bact-d5l5q2

Related information

Gene_locus 9bact-d5l5q1    9bact-d5l5q2
Family 9bact-d5l5q1    9bact-d5l5q2    Duf_3089

Citations formats

Bayer S, Kunert A, Ballschmiter M, Greiner-Stoeffele T (2010)
Indication for a new lipolytic enzyme family: isolation and characterization of two esterases from a metagenomic library
J Molecular Microbiology Biotechnol 18 :181

Bayer S, Kunert A, Ballschmiter M, Greiner-Stoeffele T (2010)
J Molecular Microbiology Biotechnol 18 :181