Lipase

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Line 72: Line 72:
**[[1hpl]] – hLip – horse <br />
**[[1hpl]] – hLip – horse <br />
**[[1hlg]] – hLip – human - gastric<br />
**[[1hlg]] – hLip – human - gastric<br />
-
**[[3jw8]], [[3hju]] – mono-glyceride hLip<br />
 
**[[1jmy]] – hBSSL <br />
**[[1jmy]] – hBSSL <br />
**[[1akn]] – cBSSL – cattle <br />
**[[1akn]] – cBSSL – cattle <br />
Line 81: Line 80:
**[[1gpl]] – Lip – Guinea pig<br />
**[[1gpl]] – Lip – Guinea pig<br />
**[[3zpx]] – Lip – ''Ustilago maydis''<br />
**[[3zpx]] – Lip – ''Ustilago maydis''<br />
 +
**[[4l3w]] – Lip catalytic domain – bread mold<br />
 +
**[[4zrd]], [[4zre]] – Lip1 (mutant) – dandruff fungus<br />
*Prokaryote lipase:
*Prokaryote lipase:
Line 86: Line 87:
**[[3guu]], [[1lbs]], [[1lbt]], [[1tca]], [[1tcb]], [[1tcc]] – CaLipA – ''Candida antarctica''<br />
**[[3guu]], [[1lbs]], [[1lbt]], [[1tca]], [[1tcb]], [[1tcc]] – CaLipA – ''Candida antarctica''<br />
**[[2veo]] – CaLipA – closed state<br />
**[[2veo]] – CaLipA – closed state<br />
-
**[[4k6g]] – CaLipB<br />
+
**[[4k6g]], [[4zv7]], [[3w9b]], [[5a6v]], [[5a71]] – CaLipB<br />
**[[3icv]], [[4k5q]], [[4k6h]], [[4k6k]] – CaLipB (mutant) <br />
**[[3icv]], [[4k5q]], [[4k6h]], [[4k6k]] – CaLipB (mutant) <br />
**[[1gz7]], [[1lpm]], [[1lps]]– CrLip 2 – ''Candida rugosa'' - closed state<br />
**[[1gz7]], [[1lpm]], [[1lps]]– CrLip 2 – ''Candida rugosa'' - closed state<br />
Line 97: Line 98:
**[[2fx5]] – Lip – ''Pseudomonas mendocina''<br />
**[[2fx5]] – Lip – ''Pseudomonas mendocina''<br />
**[[1yzf]] – Lip – ''Enterococcus faecalis''<br />
**[[1yzf]] – Lip – ''Enterococcus faecalis''<br />
-
**[[1dt3]], [[1dt5]], [[1dte]], [[1du4]], [[1ein]], [[1tib]], [[4dyh]], [[4ea6]], [[4flf]], [[4gbg]], [[4gwl]] - TlLip - ''Thermomyces lanuginose''<br />
+
**[[1dt3]], [[1dt5]], [[1dte]], [[1du4]], [[1ein]], [[1tib]], [[4dyh]], [[4ea6]], [[4flf]], [[4gbg]], [[4gwl]], [[4zgb]] - TlLip - ''Thermomyces lanuginose''<br />
 +
**[[5ap9]] – TlLip (mutant)<br />
**[[1jfr]] – Lip – ''Streptomyces exfoliates''<br />
**[[1jfr]] – Lip – ''Streptomyces exfoliates''<br />
 +
**[[5mal]] – Lip – ''Streptomyces rimosus''<br />
**[[1oil]] – BcLip - ''Burkholderia cepacia''<br />
**[[1oil]] – BcLip - ''Burkholderia cepacia''<br />
**[[2lip]] – BcLip – open state<br />
**[[2lip]] – BcLip – open state<br />
Line 112: Line 115:
**[[3lip]], [[3a6z]] - Lip - ''Pseudomonas cepacia'' – open state<br />
**[[3lip]], [[3a6z]] - Lip - ''Pseudomonas cepacia'' – open state<br />
**[[1qge]], [[1tah]] – Lip – ''Pseudomonas glumae''<br />
**[[1qge]], [[1tah]] – Lip – ''Pseudomonas glumae''<br />
-
**[[2w22]] – Lip – ''Geobacillus thermocatenulatus''<br />
+
**[[2w22]] – GtLip – ''Geobacillus thermocatenulatus''<br />
-
**[[1ji3]], [[1ku0]], [[4fmp]] – Lip – ''Bacillus stearothermophilus''<br />
+
**[[5ce5]] – GtLip (mutant)<br />
 +
**[[1ji3]], [[1ku0]], [[4fmp]], [[4x6u]]– BstLip – ''Bacillus stearothermophilus''<br />
 +
**[[4x71]], [[4x7b]], [[4x85]] – BstLip (mutant)<br />
**[[1ah7]] - Lip – ''Bacillus cereus''<br />
**[[1ah7]] - Lip – ''Bacillus cereus''<br />
-
**[[2qxt]], [[2qxu]], [[1isp]], [[1i6w]], [[4fdm]] - BsLip – ''Bacillus subtilis''<br />
+
**[[2qxt]], [[2qxu]], [[1isp]], [[1i6w]], [[4fdm]], [[5ct5]], [[5ct6]] - BsLip – ''Bacillus subtilis''<br />
-
**[[3d2a]], [[3d2b]], [[3d2c]], [[1t2n]], [[1t4m]], [[3qmm]], [[3qzu]], [[4fkb]] - BsLip (mutant) <br />
+
**[[3d2a]], [[3d2b]], [[3d2c]], [[1t2n]], [[1t4m]], [[3qmm]], [[3qzu]], [[4fkb]], [[5ct8]] - BsLip (mutant) <br />
**[[2ory]] – Lip – ''Photobacterium lypoliticum''<br />
**[[2ory]] – Lip – ''Photobacterium lypoliticum''<br />
**[[2z5g]], [[2dsn]] – GzLip T1 – ''Geobacillus zalihae''<br />
**[[2z5g]], [[2dsn]] – GzLip T1 – ''Geobacillus zalihae''<br />
Line 125: Line 130:
**[[3uue]], [[3uuf]] – Lip – ''Malassezia globosa''<br />
**[[3uue]], [[3uuf]] – Lip – ''Malassezia globosa''<br />
**[[4hs9]] – Lip – ''Proteus mirabilis''<br />
**[[4hs9]] – Lip – ''Proteus mirabilis''<br />
 +
**[[4opm]] – Lip – ''Acinetobacter baumannii''<br />
 +
**[[5ah0]] – Lip – ''Pelosinus fermentans''<br />
 +
**[[5ah1]] – Lip – ''Clostridium botulinum''<br />
 +
**[[5ch8]] – Lip (mutant) – ''Penicillium cyclopium''<br />
*Lipase/colipase complexes. The colipase is a co-enzyme whose binding to lipase optimizes the enzymatic activity
*Lipase/colipase complexes. The colipase is a co-enzyme whose binding to lipase optimizes the enzymatic activity
Line 150: Line 159:
*Lipase + inhibitors
*Lipase + inhibitors
-
**[[3jwe]], [[3pe6]] - mono-glyceride hLip + SAR629 – covalent inhibitor<br />
 
**[[3l1h]] – EstE5(LIPE)+FeCl3 – noninvasive inhibitor<br />
**[[3l1h]] – EstE5(LIPE)+FeCl3 – noninvasive inhibitor<br />
**[[3l1i]], [[3l1j]] - EstE5(LIPE)+CuSO4 – noninvasive inhibitor<br />
**[[3l1i]], [[3l1j]] - EstE5(LIPE)+CuSO4 – noninvasive inhibitor<br />
Line 173: Line 181:
**[[4kjx]] - TlLip + nitrobenzaldehyde + lauric acid<br />
**[[4kjx]] - TlLip + nitrobenzaldehyde + lauric acid<br />
**[[4n8s]] - TlLip + nitrobenzaldehyde + ethylacetoacetate<br />
**[[4n8s]] - TlLip + nitrobenzaldehyde + ethylacetoacetate<br />
 +
**[[4s0x]] – TlLip + lauric acid<br />
*Lipase conjugated with analogs to its reaction intermediates
*Lipase conjugated with analogs to its reaction intermediates
Line 191: Line 200:
**[[4ke7]], [[4ke8]], [[4ke9]] – BaMAGL + ligand<br />
**[[4ke7]], [[4ke8]], [[4ke9]] – BaMAGL + ligand<br />
**[[4ke6]], [[4kea]] – BaMAGL (mutant) + ligand<br />
**[[4ke6]], [[4kea]] – BaMAGL (mutant) + ligand<br />
-
**[[3jwe]], [[3pe6]] – hMAGL + inhibitor<br />
+
**[[3jwe]], [[3pe6]], [[4uuq]] – hMAGL + inhibitor<br />
 +
**[[4zwn]] – yMAGL – yeast<br />
 +
**[[4zxf]] – yMAGLip + substrate analog<br />
*Lipase with substrate bound at active site
*Lipase with substrate bound at active site

Revision as of 08:31, 4 July 2017

Structure of Pancreatic Lipase (PDB entry 1akn)

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3D Structures of Lipase

Updated on 04-July-2017

References

  1. [1] 1HPL PDB SUM
  2. [2] A cross-linked complex between horse pancreatic lipase and colipase
  3. [3] History of Lipids
  4. [4] 1HPL PDB
  5. http://www.pdb.org/pdb/explore/explore.do?structureId=1HPL
  6. http://www.pdb.org/pdb/explore/remediatedSequence.do?structureId=1HPL
  7. http://www.springerlink.com/content/g5h1613440115701/fulltext.pdf
  8. Fundamentals of Biochemistry...
  9. Thomas, A. etc. "Role of the Lid Hydrophobicity Pattern in Pancreatic Lipase Activity", The Journal of Biological Chemistry, 2005 September 22; 270 (48): 40074-40083.
  10. "Colipase". Wikipedia: The Free Encyclopedia. 5 July 2011 [5]
  11. "Colipase Residues..."
  12. Fundamentals of Biochemistry...
  13. Crandall,W., Lowe, M. "Colipase Residues Glu64 and Arg65 Are Essential for Normal Lipase-mediated Fat Digestion in the Presence of Bile Salt Micelles" Journal of Biological Chemistry, 2001, (276) 12505-12512
  14. van Tilbeurgh H, etc."Structure of the pancreatic lipase-procolipase complex", 1992 Sep 10;359(6391):159-62. PMID:1522902.[6]
  15. http://www.pdb.org/pdb/explore/explore.do?structureId=1ETH
  16. http://www.nature.com/nature/journal/v362/n6423/abs/362814a0.html
  17. Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L, Silman I. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science. 1991 Aug 23;253(5022):872-9. PMID:1678899
  18. Ollis DL, Cheah E, Cygler M, Dijkstra B, Frolow F, Franken SM, Harel M, Remington SJ, Silman I, Schrag J, et al.. The alpha/beta hydrolase fold. Protein Eng. 1992 Apr;5(3):197-211. PMID:1409539
  19. Bourne Y, Martinez C, Kerfelec B, Lombardo D, Chapus C, Cambillau C. Horse pancreatic lipase. The crystal structure refined at 2.3 A resolution. J Mol Biol. 1994 May 20;238(5):709-32. PMID:8182745 doi:http://dx.doi.org/10.1006/jmbi.1994.1331
  20. [7] 1LPB PDB SUM
  21. "Pancreatic lipase". Wikipedia: The Free Encyclopedia. 7 Nov 2011 [8]
  22. Kordik, C., Reitz, A. "Pharmacological Treatment of Obesity: Therapeutic Strategies" Journal of Medicinal Chemistry, 1999 (42).
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