Purification and characterization of a novel lipase from the digestive glands of a primitive animal: The scorpion

Zouari, Nacim; Miled, Nabil; Chérif, Slim; Mejdoub, Hafedh; Gargouri, Youssef

doi:10.1016/j.bbagen.2005.08.005

Cited by 36 publications

(35 citation statements)

References 28 publications

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“…The lipase is a glycoprotein with a molecular mass of 44.8 kDa, which is similar to that for other lipases from the redclaw crayfish Cherax quadricarinatus (López-López et al 2003), squid Ommastrephes bartramii (Sukarno et al 1996), and scorpion S. maurus (Zouari et al 2005). Within the conserved domain identified in the deduced amino acid sequence of pvl, a catalytic triad and a lid were identified, which shared similarity in residues to those seen in other lipases, and the level of similarity seen here and the catalytic properties of the pure lipase supports pvl encoding a lipase protein with novel biotechnological applications.…”

Section: Discussionmentioning

confidence: 80%

“…Other glycosylated lipases have been described in invertebrates such as the scorpion S. maurus (Zouari et al 2005). However, lipases shown a different degree of glycosylation which differs among species (Rathelot et al 1981).…”

Section: Discussionmentioning

confidence: 99%

“…The pH for maximum activity of digestive lipases in the scorpion is between 8.5 and 9 (Zouari et al 2005), which is related to the ionization properties of histidine (pKa=6.5) and the fact that the amino acid residues of the catalytic triad (Ser, His and Asp) (Roussel et al 1999) play an important role in the charge relay system involving the catalytic triad and the Residues of catalytic (shaded triangle) and pattern of α/β-hydrolase structure (asterisk) are indicated. The peptide sequences obtained by mass spectrometry are boxed.…”

Section: Discussionmentioning

confidence: 99%

“…Lipases from crab Carcinus mediterraneus (Slim et al 2007), scorpion Scorpio maurus (Zouari et al 2005), and squid Todarodes pacificus (Park et al 2008) have been purified. Some biochemical characteristics are similar to those found in mammalian digestive lipases: molecular masses of ∼40-50 kDa with an alkaline pI between 6.8 and 7.8 (Moreau et al 1992;Miled et al 2000).…”

Section: Introductionmentioning

confidence: 99%

“…However, only a few specific inhibitors have been identified, such as tetrahydrolipstatin and di-isopropyl fluorophosphate. These inhibitors are used to characterize digestive enzymes from the scorpion S. maurus (Zouari et al 2005) and crab C. mediterraneus (Slim et al 2007) as serine lipases.…”

Section: Introductionmentioning

confidence: 99%

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Purification and Biochemical Characterization of Digestive Lipase in Whiteleg Shrimp

2010

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Section: Discussionmentioning

confidence: 80%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Purification and Biochemical Characterization of Digestive Lipase in Whiteleg Shrimp

2010

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Biochemical characterization, cloning and molecular modeling of a digestive lipase from red seabream (Pagrus major): Structural explanation of the interaction deficiency with colipase and lipidic interface

Smichi¹,

Fendri²,

Triki-Fendri

et al. 2017

Engineering in Life Sciences

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Biochemical characterization, cloning and molecular modeling of a digestive lipase from red seabream (Pagrus major): Structural explanation of the interaction deficiency with colipase and lipidic interfaceRed seabream digestive lipase (RsDL) was purified from fresh pyloric caeca. Pure RsDL has an apparent molecular mass of 50 kDa. The RsDL is more active on shortchain triacylglycerols (TC 4 ), and enzymatic activity decreases when medium (TC 8 ) or long-chain (olive oil) triacylglycerols were used as substrates. The specific activities of RsDL are very weak as compared to those obtained with classical pancreatic lipases. No colipase was detected in the red seabream pyloric caeca. Furthermore, the RsDL was not activated by a mammal colipase. Similar results were reported for annular seabream lipase. In order to explain structurally the discrepancies between sparidae and mammal lipases, genes encoding mature RsDL and five other lipases from sparidae fish species were cloned and sequenced. Phylogenetic studies indicated the closest homology of sparidae lipases to bird pancreatic ones. Structural models were built for annular seabream and RsDL under their closed and open forms using mammal pancreatic lipases as templates. Several differences were noticed when analyzing the amino acids corresponding to those involved in HPL binding to colipase. This is likely to prevent interaction between the fish lipase and the mammalian colipase and may explain the fact that mammalian colipase is not effective in activating sparidae lipases. In addition, several hydrophobic residues, playing a key role in anchoring pancreatic lipase onto the lipid interface, are replaced by polar residues in fish lipases. This might explain the reason why the latter enzymes display weak activity levels when compared to mammalian pancreatic lipases.Abbreviations: AsDL, annular seabream digestive lipase; DL, digestive lipase; DPLRP1, dog pancreatic lipase related protein 1; GhDL, gilthead seabream digestive lipase; HPL, human pancreatic lipase; HPLRP1, human pancreatic lipase related protein 1; HPLRP2, human pancreatic lipase related protein 2; PCR, polymerase chain reaction; PL, pancreatic lipase; PPL, porcine pancreatic lipase; PPLRP2, porcine pancreatic lipase related protein 2; RP, related pancreatic lipase; RsDL, red seabream digestive lipase; RT, reverse transcription; SpDL, Saupe digestive lipase; SsDL, striped seabream digestive lipase; TPL, turkey pancreatic lipase; WsDL, white seabream digestive lipase

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Ion-Exchange Chromatography

Sheehan

2008

Springer Protocols Handbooks

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Purification and characterization of a novel lipase from the digestive glands of a primitive animal: The scorpion

Cited by 36 publications

References 28 publications

Purification and Biochemical Characterization of Digestive Lipase in Whiteleg Shrimp

Purification and Biochemical Characterization of Digestive Lipase in Whiteleg Shrimp

Biochemical characterization, cloning and molecular modeling of a digestive lipase from red seabream (Pagrus major): Structural explanation of the interaction deficiency with colipase and lipidic interface

Ion-Exchange Chromatography

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