Pork liver esterase

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Pork liver esterase ( Sus scrofa )
Isoforms 3 (α, β and γ)
Identifier
Gene name (s) PLE
External IDs
Enzyme classification
EC, category 3.1.1.1 ,  esterase
Response type hydrolysis
Substrate Carboxylic acid ester
Products Carboxylic acid and alcohol

Pig liver esterase ( engl. Pig liver esterase , PLE) is one selected from the liver of pigs recovered enzyme .

description

Pig liver esterase is obtained from pig livers by extraction with organic solvents . It is a slightly brownish powder that can be easily dissolved in water.

The enzyme exists in three isoforms : the α-subunit has a molar mass of 58.2  kDa , the β-subunit has 59.7 kDa and the γ-subunit 61.4 kDa. The pig liver esterase itself consists of three subunits of all three isoenzymes . The main components of the natural product are ααα, ααγ, αγγ and γγγ. The different variants also show a different substrate specificity. Compared to the γ-subunit, the α-subunit has a lower proportion of aspartic acid and a higher proportion of arginine . Since 2001 there has been a recombinantly produced pig liver esterase in addition to pig liver extract.

use

Pig liver esterase is the most common and versatile esterase used in synthetic chemistry. A number of reactions can be carried out stereoselectively with the help of pig liver esterase.

The enzyme can thereby also on a polymeric support, such as polyacrylamide - gels (Eupergit ® are immobilized). The activity of the enzyme is thereby slightly impaired and reaches about 68% of the value of the non-immobilized pig liver esterase.

Inhibitors

Trifluoromethyl ketones, such as, for example, 1,1,1-trifluoro-4-phenylbutan-2-one , are able to inhibit the enzyme.

literature

  • M. Hermann et al .: Alternative pig liver esterase (APLE) - cloning, identification and functional expression in Pichia pastoris of a versatile new biocatalyst. In: J Biotechnol. 133, 2008, pp. 301-310. PMID 18078679 .
  • A. Hummel et al: Isoenzymes of pig-liver esterase reveal striking differences in enantioselectivities. In: Angew Chem Int Ed Engl. 46, 2007, pp. 8492-8494. PMID 17902087 .
  • E. Brüsehaber et al .: Identification of pig liver esterase variants by tandem mass spectroscopy analysis and their characterization. In: Appl Microbiol Biotechnol. 76, 2007, pp. 853-859. PMID 17593363 .
  • RN Patel: Microbial / enzymatic synthesis of chiral drug intermediates. In: Adv Appl Microbiol. 47, 2000, pp. 33-78. PMID 12876794 (Review).
  • S. Niwayama et al: A Novel Chemicoenzymic Rearrangement by Asymmetric Hydrolysis with Pig Liver Esterase. In: JACS. 116, 1994, pp. 3290-3295. doi: 10.1021 / ja00087a015 .
  • LKP Lam et al: Enzymes in organic synthesis. 42. Investigation of the effects of the isozymal composition of pig liver esterase on its stereoselectivity in preparative-scale ester hydrolysis of asymmetric synthetic value. In: JACS. 110, 1988, pp. 4409-4411. doi: 10.1021 / ja00221a049 .
  • RC Augusteyn et al .: On the homology of the active-site peptides of liver carboxylesterases. In: Biochim Biophys Acta . 171, 1969, pp. 128-137. PMID 4884138 .
  • AJ Adler and GB Kistiakowsky: Kinetics of Pig Liver Esterase Catalysis. In: JACS. 84, 1962, pp. 695-703. doi: 10.1021 / ja00864a001 .
  • GB Kistiakowsky and PC Mangelsdorf: The Kinetics of Ester Hydrolysis by Liver Esterase. In: JACS. 78, 1956, pp. 2964-2969. doi: 10.1021 / ja01594a012 .

Web links

Individual evidence

  1. ↑ Carboxylic-ester hydrolase  reaction - R00630 in the Kyoto Encyclopedia of Genes and Genomes.Retrieved November 17, 2009.
  2. ↑ DJ Horgan et al: Carboxylesterases (EC 3.1.1). A large-scale purification of pig liver carboxylesterase. In: Biochemistry 8, 1969, pp. 2000-2006. PMID 5785220 .
  3. ^ E. Heymann and W. Junge: Characterization of the isoenzymes of pig-liver esterase. 1. Chemical Studies. In: Eur J Biochem 95, 1979, pp. 509-518. PMID 446477 .
  4. ^ W. Junge and E. Heymann: Characterization of the Isoenzymes of Pig-Liver Esterase 2. Kinetic Studies. In: Eur J Biochem 95, 1979, pp. 519-525. PMID 446478 .
  5. ↑ a b S. Lange et al .: Cloning, functional expression, and characterization of recombinant pig liver esterase. In: ChemBioChem 2, 2001, pp. 576-582. PMID 11828491 .
  6. ↑ D. Böttcher et al .: Functional expression of the gamma isoenzymes of pig liver carboxyl esterase in Escherichia coli. In: Appl Microbiol Biotechnol 73, 2007, pp. 1282-1289. PMID 16960735 .
  7. ↑ A. Musidlowska-Persson and UT Bornscheuer: Recombinant porcine intestinal carboxylesterase: cloning from the pig liver esterase gene by site-directed mutagenesis, functional expression and characterization. In: Protein Eng 16, 2003, pp. 1139-1145. PMID 14983097 .
  8. ↑ UT Bornscheuer and RJ Kazlauskas: Hydrolases in Organic Synthesis - Regio- and Stereoselective Biotransformations. Wiley-VCH, 2005, ISBN 3-527-31029-0 .
  9. ↑ K. Faber: Biotransformations in Organic Chemistry. Verlag Springer, 2004, ISBN 3-540-20097-5 .
  10. ↑ EJ Toone et al.: Enzymes in Organic Synthesis. 47. An Active Site Model for Interpreting and Predicting the Specificity of Pig Liver Esterase. In: JACS 112, 1990, pp. 4946-4952. doi: 10.1021 / ja00168a047
  11. ↑ LM Zhu and MC Tedford: Application of Pig Liver Esterase (PLE) in Asymmetric Synthesis. In: Tetrahedron 46, 1990, S, 6587-6611. doi: 10.1016 / S0040-4020 (01) 87851-0 .
  12. ↑ HJ Gais et al: Activation of pig liver esterase in organic media with organic polymers: application to the enantioselective acylation of racemic functionalized secondary alcohols. In: J Org Chem 66, 2001, pp. 3384-3396. PMID 11348121
  13. ↑ JM Herdan et al: Enantioselective hydrolysis of racemic esters using pig liver esterase. In: Journal of Molecular Catalysis A: Chemical 107, 1996, pp. 409-414. doi: 10.1016 / 1381-1169 (95) 00241-3 .
  14. ↑ T. Boller et al: EUPERGIT Oxirane Acrylic Beads: How to Make Enzymes Fit for Biocatalysis. In: Org. Process Res. Dev. 6, 2002, pp. 509-519. doi: 10.1021 / op015506w .
  15. ↑ K. L Bäumen et al: Immobilized porcine liver esterase: a convenient reagent for the preparation of chiral building blocks. In: Tetrahedron Letters 26, 1985, pp. 407-410. doi: 10.1016 / S0040-4039 (00) 61896-8 .
  16. ↑ KN Allen and RH Ables: Inhibition of pig liver esterase by trifluoromethyl ketones: modulators of the catalytic reaction alter inhibition kinetics. In: Biochemistry 28, 1989, pp 135-140. doi: 10.1021 / bi00427a020
  17. ^ MA Ashour and BD Hammock: Substituted trifluoroketones as potent, selective inhibitors of mammalian esterases. In: Biochem Pharmacol 36, 1987, pp. & 1869-1879. PMID 3593399 .