Lipases and esterases: a review of their sequences, structure and evolution

Anthonsen, Henrik W.; Baptista, António M.; Drabløs, Finn; Martel, Paulo; Petersen, Steffen B.; Sebastião, M. J.; Vaz, Louis

doi:10.1016/s1387-2656(08)70056-5

Cited by 72 publications

(42 citation statements)

References 109 publications

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“…This catalytic triad is chemically analogous to that originally described in serine proteases such as chymotrypsin [22]. The nucleophilic elbow, b-strand/Ser/a-helix, structural motif including the Gly-X-Ser-X-Gly consensus sequence has been detected mostly in lipases and esterases [23][24][25][26]. Bacillus and Candida antartica B lipases have a variation to Ala-X-Ser-X-Gly and Thr-XSer-X-Gly, respectively.…”

mentioning

confidence: 71%

Digestive Lipases Inhibition: an In vitro Study

Tiss

Miled

Verger

et al. 2004

Lipases and Phospholipases in Drug Development

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IntroductionUnder normal physiological conditions the digestion and absorption of dietary lipids are highly efficient processes. In industrialized countries, the daily human diet intake generally contains an average of 90-120 g of lipids, mostly triacylglycerides (TAG), more than 95% of which are absorbed, due to the action of the stomach, small intestine, liver and pancreas [1,2]. Several steps can be distinguished in the processing of dietary lipids, including their emulsification, hydrolysis and micellization, and lastly, their uptake by the enterocytes. The emulsification of lipids starts in the stomach and is mediated by physical forces and facilitated by the partial lipolysis of the dietary lipids [2]. For a long time, the hydrolysis of dietary TAG was thought to begin in the intestinal lumen and to be catalyzed entirely by pancreatic lipase. The stomach was thought to be a transient storage organ, the role of which was limited to mixing lipids with the other nutrients and dispersing them. In human, it has been now clearly established that the hydrolysis of alimentary TAG begins in the stomach and is catalyzed by human gastric lipase (HGL) [3][4][5] which is able to hydrolyze short and long chain TAG at comparable rates. Under acidic pH conditions, HGL has been shown to be remarkably stable and active, whereas pancreatic lipase irreversibly loses its lipolytic capacity.Human pancreatic lipase (HPL) alone is inactive in vitro on an emulsified TAG substrate in the presence of supramicellar concentrations of bile salts such as those found in the small intestine. Bile salts are amphiphilic molecules that bind to the oil-water interface and prevent pancreatic lipase adsorption, and thus lipolysis, from occurring [3,4]. The inhibition by bile salts can, however, be reversed by the specific pancreatic lipase cofactor colipase [3,[5][6][7], via the formation of a specific 1 : 1 lipase-colipase complex.HPL has been purified from the pancreatic juice by De Caro et al. [8]. In contrast to most other pancreatic enzymes, which are secreted as proenzymes and further activated by proteolytic cleavage in the small intestine, pancreatic lipase is directly secreted as a 50 kDa active enzyme consisting of 449 amino acid residues including a high mannose or complex-type glycan chain N-linked to Asn 166. In vitro, the maximum specific activities, obtained using 4 mM NaTDC and colipase in excess, were 12000 units/mg at pH 8, 6000 units/mg at pH 7.8 and 4600 units/mg at pH 8 using tributyroylglycerol (tributyrin), trioctanoylglycerol and Intralipid TM as substrates, respectively. The cDNA has been cloned [9] and expressed in a baculovirus/insect cells system [10]. The recombinant HPL (rHPL) which was secreted in the culture medium at high level (40 mg/L) was obtained after a one-step purification procedure. The kinetic characterizations have shown that the kinetic and surface behavior of rHPL was similar to that of the native enzyme.Bodmer et al. [11] have cloned, sequenced, and expressed active HGL in yeast. The amino acid seque...

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mentioning

confidence: 71%

Digestive Lipases Inhibition: an In vitro Study

Tiss

Miled

Verger

et al. 2004

Lipases and Phospholipases in Drug Development

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“…This domain has a highly conserved motif, GDGHGYDI, possibly containing conserved catalytic residues of an enzyme family of unknown function. Family members are not very homologous in sequences outside of this motif; such low homology is typical for esterase and lipase families (2,13,24,30).…”

Section: Resultsmentioning

confidence: 99%

Complete Sequences of Four Plasmids ofLactococcus lactissubsp.cremorisSK11 Reveal Extensive Adaptation to the Dairy Environment

Siezen¹,

Renckens²,

Swam

et al. 2005

Appl Environ Microbiol

132

169

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Lactococcus lactis strains are known to carry plasmids encoding industrially important traits. L. lactis subsp. cremoris SK11 is widely used by the dairy industry in cheese making. Its complete plasmid complement was sequenced and found to contain the plasmids pSK11A (10,372 bp), pSK11B (13,332 bp), pSK11L (47,165 bp), and pSK11P (75,814 bp). Six highly homologous repB-containing replicons were found, all belonging to the family of lactococcal theta-type replicons. Twenty-three complete insertion sequence elements segment the plasmids into numerous modules, many of which can be identified as functional units or containing functionally related genes. Plasmid-encoded functions previously known to reside on L. lactis SK11 plasmids were now mapped in detail, e.g., lactose utilization (lacR-lacABCDFEGX), the proteolytic system (prtM-prtP, pepO, pepF), and the oligopeptide permease system (oppDFBCA). Newly identified plasmid-encoded functions could facilitate the uptake of various cations, while the pabA and pabB genes could be essential for folate biosynthesis. A competitive advantage could be obtained by using the putative flavin adenine dinucleotide-dependent D-lactate dehydrogenase and oxalate:formate antiporter for enhanced ATP synthesis, while the activity of the predicted ␣-acetolactate decarboxylase may contribute to the formation of an additional electron sink. Various stress response proteins are plasmid encoded, which could enhance strain robustness. A substantial number of these "adaptation" genes have not been described before on L. lactis plasmids. Moreover, several genes were identified for the first time in L. lactis, possibly reflecting horizontal gene transfer.

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“…Some of these are present in both lactobacilli, either as single copies of orthologues, or as multiple copies (paralogues) belonging to different families. Two families of putative cell-surface hydrolases (CSH-1 and CSH-2) are detected which have sequence characteristics of lipases or esterases (Anthonsen et al, 1995;Wong & Schotz, 2002). It is striking to note that the majority of extracellular proteins with unknown function are not shared by L. plantarum and L. johnsonii, but only occur in one of the two bacteria.…”

Section: Extracellular Proteinsmentioning

confidence: 99%

The complete genomes of Lactobacillus plantarum and Lactobacillus johnsonii reveal extensive differences in chromosome organization and gene content

Boekhorst¹,

Siezen²,

Zwahlen

et al. 2004

Microbiology

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The first comprehensive comparative analysis of lactobacilli was done by comparing the genomes of Lactobacillus plantarum (3?3 Mb) and Lactobacillus johnsonii (2?0 Mb). L. johnsonii is predominantly found in the gastrointestinal tract, while L. plantarum is also found on plants and plant-derived material, and is used in a variety of industrial fermentations. The L. plantarum and L. johnsonii chromosomes have only 28 regions with conservation of gene order, totalling about 0?75 Mb; these regions are not co-linear, indicating major chromosomal rearrangements. Metabolic reconstruction indicates many differences between L. johnsonii and L. plantarum: numerous enzymes involved in sugar metabolism and in biosynthesis of amino acids, nucleotides, fatty acids and cofactors are lacking in L. johnsonii. Major differences were seen in the number and types of putative extracellular proteins, which are of interest because of their possible role in host-microbe interactions. The differences between L. plantarum and L. johnsonii, both in genome organization and gene content, are exceptionally large for two bacteria of the same genus, emphasizing the difficulty in taxonomic classification of lactobacilli.

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Lipases and esterases: a review of their sequences, structure and evolution

Cited by 72 publications

References 109 publications

Digestive Lipases Inhibition: an In vitro Study

Digestive Lipases Inhibition: an In vitro Study

Complete Sequences of Four Plasmids ofLactococcus lactissubsp.cremorisSK11 Reveal Extensive Adaptation to the Dairy Environment

The complete genomes of Lactobacillus plantarum and Lactobacillus johnsonii reveal extensive differences in chromosome organization and gene content

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