Cloning of the bovine pancreatic cholesterol esterase/lysophospholipase

Kyger, Erich M.; Wiegand, Roger C.; Lange, Louis G.

doi:10.1016/0006-291x(89)91811-1

Cited by 91 publications

(40 citation statements)

References 7 publications

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“…In glutactin, a 1,023-amino acid residue glycoprotein located in basement membranes of Drosophila, it is the N-terminal segment that is homologous to esterases. Although the sequence identity of these three nonhydrolytic proteins with other proteins in this Shimada et al, 1990Shimada et al, 1989Kawaguchi et al, 1989Longhi et al, 1992Schumacher et al, 1986Sikorav et al, 1987Rachinsky et al, 1990Doctor et al, 1990Soreq et al, 1990Hall and Spierer, 1986Hall and Malcolm, 1991Lockridge et al, 1987Rachinsky et al, 1990Jbilo and Chatonnet, 1990Robbi et al, 1990Munger et al, 1992Long et al, 1991Korza and Ozols, 1988Ozols, 1989Ovnic et al, 1991Long et al, 1988Takagi et al, 1988Oakeshott et al, 1987Collet et al, 1990Hanzlik et al, 1989Mouches et al, 1990Han et al, 1987Kissel et al, 1989 Hui andKissel, 1990;Nilsson et al, 1990;Baba et al, 1991Kyger et al, 1989Rubino et al, 1989Bomblies et al, 1990 de la Escalera et al ., 1990Olson et al, 1990Mercken et al, 1985 family is within 16-28%, there is no evolutionary pressure to maintain the geometry of the active site. One may, therefore, predict that their 3D structures will show more divergence from GCL and TcAChE than other proteins in this group.…”

Section: Resultsmentioning

confidence: 98%

Relationship between sequence conservation and three‐dimensional structure in a large family of esterases, lipases, and related proteins

et al. 1993

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Based on the recently determined X-ray structures of Torpedo californica acetylcholinesterase and Geotrichum candidum lipase and on their three-dimensional superposition, an improved alignment of a collection of 32 related amino acid sequences of other esterases, lipases, and related proteins was obtained. On the basis of this alignment, 24 residues are found to be invariant in 29 sequences of hydrolytic enzymes, and an additional 49 are well conserved. The conservation in the three remaining sequences is somewhat lower. The conserved residues include the active site, disulfide bridges, salt bridges, and residues in the core of the proteins. Most invariant residues are located at the edges of secondary structural elements. A clear structural basis for the preservation of many of these residues can be determined from comparison of the two X-ray structures.

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Section: Resultsmentioning

confidence: 98%

Relationship between sequence conservation and three‐dimensional structure in a large family of esterases, lipases, and related proteins

et al. 1993

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“…The properties of the cod enzyme were similar to mammalian carboxylester lipases, and antibodies directed against cod lipase cross-reacted specifically with a selection of mammalian carboxylester lipases. The absence of a colipase-dependent lipase in fish indicates that the role of carboxylester lipase in lipid digestion is not restricted to hydrolysis of cholesterol esters or vitamin esters, but this enzyme is also physiologically important for triacylglyceride and wax ester digestion.Sequence studies on human [ l l , 121, rat [13], rabbit [14] and bovine pancreatic carboxylester lipases [15] show that these enzymes belong to the esterase B (or cholinesterase) family. These lipases bear no sequence identity to pancreatic triacylglycerol hydrolase (colipase dependent), apart from the active serine GXSXG consensus sequence, common to all serine esterases 1161.…”

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confidence: 99%

“…Sequence studies on human [ l l , 121, rat [13], rabbit [14] and bovine pancreatic carboxylester lipases [15] show that these enzymes belong to the esterase B (or cholinesterase) family. These lipases bear no sequence identity to pancreatic triacylglycerol hydrolase (colipase dependent), apart from the active serine GXSXG consensus sequence, common to all serine esterases 1161.…”

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confidence: 99%

Pancreatic Carboxylester Lipase from Atlantic Salmon (Salmo salar)

Gjellesvik¹,

Lorens²,

Male³

1994

European Journal of Biochemistry

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We report the isolation and characterization of a 1795-bp cDNA fragment encoding Atlantic salmon pancreatic carboxylester lipase from salmon pancreas mRNA. The nearly full-length cDNA contained a 540-amino-acid open-reading frame, encompassing the mature protein (by similarity to mammalian carboxylester lipase enzymes). The salmon carboxylester lipase primary structure shared 58% identity with mammalian carboxylester lipases, lacking the proline-rich C-terminal repeats found in human and rat carboxylester lipases. Congruent with other esterase B type enzymes, the salmon carboxylester lipase contained a canonical serine-esterase catalytic triad motif consisting of serine, histidine and aspartic acid. Computer-assisted modelling of the tertiary structure for salmon carboxylester lipase was conducted using acetylcholine esterase (Torpedo californica) as a template structure. The model, in conjunction with sequence comparisons and available enzymological data, has been used to locate putative bile-salt-binding and lipid-binding sites. The carboxylester lipase enzymes contain a unique, highly conserved insert region that may be associated with bile-salt binding. In the model structure, this region is located close to the active site, and contains a tyrosine residue with an adjacent carboxylester-lipase-conserved arginine. These traits have previously been predicted for the non-specific (regarding bile-salt hydroxylation) bile-salt-binding site in carboxylester lipase enzymes. At this site, a dihydroxy or trihydroxy bile-salt molecule may bind the tyrosine via hydrophobic interactions, the anionic bile-salt head group may bind the arginine, while hydrogen bonding between the bile-salt 12u hydroxy group and an adjacent aspargine residue is possible. The model does not contain an active site 'lid' structure as found in other lipases. The carboxylester lipase structural homolog to the 'flap' of the lipases from Geotrichum candidum and Candida rugosa contains a carboxylester-lipase-conserved deletion that renders this region unable to cover the active site. Instead, the shortening of this loop leads to solvent exposure of the carboxylester lipase insert region, an additional indication of the functional importance of this region.Carboxylester lipase (also bile-salt-dependent lipase and cholesterol esterase) is one of the lipases secreted from the vertebrate pancreas [l, 21. In mammals, this enzyme is considered important for cholesterol ester and vitamin ester digestion [3], and in triacylglyceride digestion in conjunction with other digestive lipases [4, 51. The enzyme exhibits strict dependence on bile-salts for hydrolytic activity on insoluble lipid substrates.In teleosts, most studies conclude that the major, if not the only pancreatic lipolytic enzyme, is of the carboxylester lipase type [6-91. This was shown in cod (Gadus morhua), where the enzyme also has been purified and characterized Correspondence to D. R. Gjellesvik, WS Biotec-Mackzymal, Strandgata 3, N-9008 TromsG, NorwayAbbreviations. ClHgBzOH, p-chloromercu...

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“…A number of proteins have been shown to present homology with the common domain of cholinesterases (ChoEases). In addition to serine hydrolases such as carboxylesterases (16)(17)(18)(19)(20)(21)(22)(23), pancreatic lysophospholipase or cholesterol esterase (24,25), and lipase from Geotrichum candidum (26), this family includes noncatalytic proteins; the C-terminal domain of bovine (27), rat (28), and human (29) thyroglobulins (4,30,31); and two Drosophila proteins that seem to be involved in cellular interactions, glutactin (32) and neurotactin (33,34).…”

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Cholinesterase-like domains in enzymes and structural proteins: functional and evolutionary relationships and identification of a catalytically essential aspartic acid.

Krejci

Duval

Chatonnet

et al. 1991

Proc. Natl. Acad. Sci. U.S.A.

133

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Primary sequences of cholinesterases and related proteins have been systematically compared. The cholinesterase-like domain of these proteins, about 500 amino acids, may fulfill a catalytic and a structural function. We identified an aspartic acid residue that is conserved among esterases and lipases (Asp-397 in Torpedo acetylcholinesterase) but that had not been considered to be involved in the catalytic mechanism. Site-directed mutagenesis demonstrated that this residue is necessary for activity. Analysis of evolutionary relationships shows that the noncatalytic members of the family do not constitute a separate subgroup, suggesting that loss of catalytic activity occurred independently on several occasions, probably from bifunctional molecules. Cholinesterases may thus be involved in cell-cell interactions in addition to the hydrolysis of acetylcholine. This would explain their specific expression in well-defined territories during embryogenesis before the formation of cholinergic synapses and their presence in noncholinergic tissues.

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Cloning of the bovine pancreatic cholesterol esterase/lysophospholipase

Cited by 91 publications

References 7 publications

Relationship between sequence conservation and three‐dimensional structure in a large family of esterases, lipases, and related proteins

Relationship between sequence conservation and three‐dimensional structure in a large family of esterases, lipases, and related proteins

Pancreatic Carboxylester Lipase from Atlantic Salmon (Salmo salar)

Cholinesterase-like domains in enzymes and structural proteins: functional and evolutionary relationships and identification of a catalytically essential aspartic acid.

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