Arpigny and Jaeger classification

Classification of lipolytic enzymes from bacteria as defined originally by Arpigny and Jaeger in 1999 and updated by Jaeger and Eggert in 2002, Hausmann and Jaeger (2010), Kovacic, Babic, Krauss and Jaeger (2019).Note that Family II and Family VIII in this classification are not alpha/beta hydrolases but SGNH hydrolases and beta lactamases respectively and are not represented in ESTHER

Ref Family Esther family Paper Comment
1 Family_I Bacterial_lipase This family correspond to family I.1, I.2, I.3, I.5, I.6, (families I.4 and 1.7 are more related to Lipase_2) of the classification of Arpigny and Jaeger (1999) (the classification was extended by Jaeger and Eggert. (also included in IPR000734). Also close to Lipase_2 (2lip Pseudomonas cepacia lipase is in the same family of scop as 1I6W bacillus subtilis lipase).
1.1 Family I.1 Bacterial_lip_FamI.1 This family corresponds to family I.1 of the classification of Arpigny and Jaeger (1999)
1.2 Family_I.2 Bacterial_lip_FamI.2 This family correspond to family I.2 of the classification of Arpigny and Jaeger (1999)
1.3 Family_I.3 Bacterial_lip_FamI.3 This family corresponds to family I.3 of the classification of Arpigny and Jaeger (1999)
1.4 Family_I.4 Lipase_2 This group of lipases has been called class 2 as they are not clearly related to other lipase families, and includes LipA and LipB from Bacillus subtilis. A novel type of hydrolase was purified from culture fluid of Paucimonas. Biochemical characterization revealed an unusual substrate specificity of the purified enzyme for amorphous poly((R)-3-hydroxyalkanoates PHA and no homologies to any other PHB depolymerase (Arpigny_Jaeger Family IX). Two other subfamilies described in: Arpigny and Jaeger (1999), Jaeger and Eggert (Family I.4 and Family I.7) are included in Lipase_2
1.5 Family_I.5 Bacterial_lip_FamI.5 This family corresponds to family I.5 of the classification of Arpigny and Jaeger (1999)
1.6 Family_I.6 Bacterial_lip_FamI.6 This family corresponds to family I.6 of the classification of Arpigny and Jaeger (1999). These lipases differ from other bacterial lipases. They present high phospholipase A1 activity. The substrate-binding cavity contains two large hydrophobic acyl chain-binding pockets and a shallow and more polar third pocket that is capable of binding either a (short) fatty acid or a phospholipid head-group.
1.7 Family_I.7 Lipase_2 This group of lipases has been called class 2 as they are not clearly related to other lipase families, and includes LipA and LipB from Bacillus subtilis. A novel type of hydrolase was purified from culture fluid of Paucimonas. Biochemical characterization revealed an unusual substrate specificity of the purified enzyme for amorphous poly((R)-3-hydroxyalkanoates PHA and no homologies to any other PHB depolymerase (Arpigny_Jaeger Family IX). Two other subfamilies described in: Arpigny and Jaeger (1999), Jaeger and Eggert (Family I.4 and Family I.7) are included in Lipase_2
1.8 Family_I.8 Bacterial_lip_FamI.8 This family corresponds to family I.6 of the classification of Arpigny and Jaeger (1999). These lipases differ from other bacterial lipases but groups putative psychrophilic esterases/lipases. The closest family is CarbLipBact_2. Features of the new family include: a conserved new active-site pentapeptide motif (LGG(F/L/Y)STG); the likely extra-cytoplasmic localization; the absence of a typical calcium-binding pocket; and the absence of a canonical lid.
2 Family_II Not alpha/beta hydrolase but SGNH hydrolase superfamily. This superfamily includes GDSL-like Lipase/Acylhydrolase family
3 Family_III Polyesterase-lipase-cutinase This family differs substantially from the cutinase acetyl-xylan esterase family. Several cutinases from the genus Thermobifida act on biodegradable plastics such as synthetic polyesters. Not all cutinases can degrade polyester plastics. Aerial plant organs are protected by a cuticle composed of an insoluble polymeric structural compound, cutin, which is a polyester composed of hydroxy and hydroxyepoxy fatty acids. Cutinases are lipases with a specificity for p-nitrophenyl acyl esters with short chain acyl group. This family was extracted from the Bacterial_lipase family which is close to PAF-Acetylhydrolase family. Streptomyces exfoliatus lipase (1JFR) Pseudomonas mendocina lipase (2FX5) are included in this family. This family correspond to family III of the classification of Arpigny et al 1999
4 Family_IV Hormone-sensitive_lipase_like || GTSAGmotif Sequence similarities between hormone-sensitive lipase and prokaryotic enzymes was dicovered by Langin and Holm and Hemila et al.. Corresponds to the Pfam entry Abhydrolase_3. IPR002168 Lipolytic enzyme. For bacterial enzymes this family correspond to family IV of the classification of Arpigny et al 1999
5.1 Family_V.1 ABHD6-Lip PIRSF031982 UCP031982_abhydr This group represents a predicted alpha/beta hydrolase, XabL type. For bacterial enzymes, this family correspond to family V.1 of the classification of Arpigny and Jaeger 1999
5.2 Family_V.2 Carboxymethylbutenolide_lactonase For bacterial enzymes, this family correspond to family V.2 of the classification of Arpigny and Jaeger 1999
5.3 Family_V.3 UCP031982 PIRSF031982 UCP031982_abhydr This group represents a predicted alpha/beta hydrolase, XabL type. For bacterial enzymes, this family correspond to family V.3 of the classification of Arpigny and Jaeger 1999
6 Family_VI LYsophospholipase_carboxylesterase PLP_Cesterase. Abhydrolase_2; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, but different of the family Monoglyceridelipase_lysophospholipase which is part of PF00561 AlphaBeta hydrolase. For bacterial enzymes, this family correspond to family VI of the classification of Arpigny and Jaeger (1999)
7 Family_VII Carb_B_Bacteria This family was extracted from the previous Carboxylesterase COesterase family. Not all bacteria possess esterase with the SEDCLYLN signature. This family corresponds to the Carbohydrate Esterase family CE10 in CAZy - Carbohydrate-Active enZYmes database (CE_10).As bacterial enzymes this family correspond to family VII of the classification of Arpigny et al 1999
8 Family_VIII Not alpha/beta hydrolase but Serine beta-lactamase-like superfamily These enzyme are good acyltrasferases (trans esterases, with high acyl transfer to hydrolysisactivity ratios (AT/H)
9 Family_IX PHAZ7_phb_depolymerase Thermoalkalophilic hydrolase of Paucimonas lemoignei with high specificity for amorphous polyesters of short chain-length hydroxyalkanoic acids. Family IX was introduced by Handrick et al.
10.1 Family_X.1 Bacterial_EstLip_FamX Family of Bacterial lipolytic enzymes. Thermotoga maritima conserved Thermostable Esterase EstD is the first characterized member of this family (thema-TM0336) Levisson et al. 2007 (Family 10 Arpigny and Jaeger 1999)
10.2 Family_X.2 Fungal-Bact_LIP Secretory lipases. Fungal-Bact_LIP is a new family as described by Neugnot et al. and Hube et al. These lipases are expressed and secreted during the infection cycle of these pathogens. In particular, C. albicans has a large number of different lipases, possibly reflecting broad lipolytic activity, which may contribute to the persistence and virulence of C. albicans in human tissue. Bassegoda et al. defined the bacterial members of this family as Family X.2 of updated Bacterial lipases classification (Family 10.2 )
11 Family_XI Lipase_3 Bacterial enzymes of Lipase_3 family belong to family XI of the classification of Arpigny and Jaeger 1999. Family XI was introduced by Lee et al.(2006)
12 Family_XII Bact_LipEH166_FamXII Novel cold-adapted alkaline lipase from an intertidal flat metagenome Kim et al. 2009. Related to Abhydrolase_5 or Lipase_2. Some enzymes contain an extra domain in N- or C-terminal: Bacterial Ig-like domain (group 2) Family XII was introduced by Kim et al. (2009)
13.1 Family_XIII-1 CarbLipBact_1 esterases, lipases, and (possibly) other hydrolases of the alpha/beta hydrolase fold. The Bacillus stearothermophilus member, Est, has been characterized as a carboxylesterase (EC 3.1.1.1) involved in the detoxification of xenobiotics, and the Bacillus sp. member has been characterized as monoacylglycerol lipase. Family XIII was introduced by Ewis et al.(2004) and Liu et al. (2004) This family is composed of two sub families with different sets of salt-bridges important for thermostability Charbonneau et al. (due to simultaneous publication of new families this family was numbered XV but really is a subset of familly XIII. See notice of this paper in Plos One)
13.2 Family_XIII-2 CarbLipBact_2 esterases, lipases, and (possibly) other hydrolases of the alpha/beta hydrolase fold. The Bacillus stearothermophilus member, Est, has been characterized as a carboxylesterase (EC 3.1.1.1) involved in the detoxification of xenobiotics, and the Bacillus sp. member has been characterized as monoacylglycerol lipase. Family XIII was introduced by Ewis et al.(2004) and Liu et al. (2004) This family is composed of two sub families with different sets of salt-bridges important for thermostability Charbonneau et al. (due to simultaneous publication of new families this family was numbered XV but really is a subset of familly XIII. See notice of this paper in Plos One)
14 Family_XIV Bacterial_EstLip_FamXIV As for bacterial enzymes, this family correspond to family XIV of the classification of Arpigny and Jaeger (1999) Family XIV was introduced by Rao et al.(2011)
15 Family_XV Duf_3089 new lipolytic enzyme family defined from isolation and characterization of two esterases from a metagenomic library . Family XV was introduced by Bayer et al.(2010) and Lee et al. (2010) (Charbonneau et al. had defined a family XV but the enzyme described in this paper is really is a subset of familly XIII. See notice of this paper in Plos One)
16 Family_XVI LipSM54-like_FamXVI Family XVI has been extracted from Cocaine_esterase to match the consensu numbering The prototype is Pseudomonas alcaligenes; Lipase LipSM54 PaL (stema-s4tny8) The family is part of the larger Peptidase_S15 family. A family XVI had been defined by Fu et al. (2013) but is not anymore in the consensus numbering
17 Family_XVII Fungal-Bact_LIP Secretory lipases. Fungal-Bact_LIP is a new family as described by Neugnot et al. and Hube et al. These lipases are expressed and secreted during the infection cycle of these pathogens. In particular, C. albicans has a large number of different lipases, possibly reflecting broad lipolytic activity, which may contribute to the persistence and virulence of C. albicans in human tissue. Bassegoda et al. defined the bacterial members of this family as Family X.2 of of updated Bacterial lipases classification (Family 10.2). Castilla et al. Defined a new lipase family (Family XVII) (Family 17) with a novel thermophilic and halophilic esterase from Janibacter sp. R02 as the first member of this subfamily
18 Family_XVIII CarbLipBact_1 Samoylova et al. defined a new lipase family XVIII of updated classification with homologues of esterase estUT1 from Ureibacillus thermosphaericus. It has a typical catalytic triad and the active serine is included in a pentapeptide (GGSVG). The enzyme is specific for short chain fatty acids p-NP esters. This family is not separated yet from CarbLipBact_1 together with Family_XIII.2 in ESTHER
19 Family_XIX Fungal-Bact_LIP Parapouli et al. analysed a new thermostable alkaliphilic lipase LipSm from Stenotrophomonas maltophilia. It lacks the requirement for interfacial activation for small substrates. They created a new family XIX of updated classification for homologues of this enzyme. This family is not separated yet from Fungal-Bact_LIP together with Family_XVII and Family_X.2 in ESTHER