Family Report for: Bacterial_lip_FamI.2

This family corresponds to family I.2 of the classification of Arpigny and Jaeger (1999)

Title: Lipases for biotechnology
Jaeger KE, Eggert T
Ref: Curr Opin Biotechnol, 13:390, 2002 : PubMed
Abstract


ESTHER: Jaeger_2002_Curr.Opin.Biotechnol_13_390
PubMedSearch: Jaeger 2002 Curr.Opin.Biotechnol 13 390
PubMedID: 12323363

Abstract

Lipases constitute the most important group of biocatalysts for biotechnological applications. The high-level production of microbial lipases requires not only the efficient overexpression of the corresponding genes but also a detailed understanding of the molecular mechanisms governing their folding and secretion. The optimisation of industrially relevant lipase properties can be achieved by directed evolution. Furthermore, novel biotechnological applications have been successfully established using lipases for the synthesis of biopolymers and biodiesel, the production of enantiopure pharmaceuticals, agrochemicals, and flavour compounds.



        

Title: Bacterial lipolytic enzymes: classification and properties
Arpigny JL, Jaeger KE
Ref: Biochemical Journal, 343:177, 1999 : PubMed
Abstract


ESTHER: Arpigny_1999_Biochem.J_343_177
PubMedSearch: Arpigny 1999 Biochem.J 343 177
PubMedID: 10493927

Abstract

Knowledge of bacterial lipolytic enzymes is increasing at a rapid and exciting rate. To obtain an overview of this industrially very important class of enzymes and their characteristics, we have collected and classified the information available from protein and nucleotide databases. Here we propose an updated and extensive classification of bacterial esterases and lipases based mainly on a comparison of their amino acid sequences and some fundamental biological properties. These new insights result in the identification of eight different families with the largest being further divided into six subfamilies. Moreover, the classification enables us to predict (1) important structural features such as residues forming the catalytic site or the presence of disulphide bonds, (2) types of secretion mechanism and requirement for lipase-specific foldases, and (3) the potential relationship to other enzyme families. This work will therefore contribute to a faster identification and to an easier characterization of novel bacterial lipolytic enzymes.