Monoglyceride lipase - Revision history

Wu3857: /* Structural Information */

2019-12-02T02:26:58Z

‎Structural Information

Wu3857 at 02:23, 2 December 2019

2019-12-02T02:23:54Z

Wu3857 at 02:18, 2 December 2019

2019-12-02T02:18:17Z

Wu3857: /* Summary */

2019-12-02T02:14:57Z

‎Summary

Wu3857: /* Cys Function & Property */

2019-12-02T02:14:24Z

‎Cys Function & Property

Wu3857: /* Cys Function & Property */

2019-12-02T02:14:13Z

‎Cys Function & Property

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|MgII, MGL|[https://www.uniprot.org/uniprot/Q8R431 Q8R431]|Rattus norvegicus|Cys208|[http://pfam.xfam.org/family..."

2019-12-02T02:12:43Z

Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|MgII, MGL|[https://www.uniprot.org/uniprot/Q8R431 Q8R431]|Rattus norvegicus|Cys208|[http://pfam.xfam.org/family..."

New page

{| align="left"
| __TOC__
|}
{{#invoke:InfoboxforTarget|run|MgII, MGL|[https://www.uniprot.org/uniprot/Q8R431 Q8R431]|Rattus norvegicus|Cys208|[http://pfam.xfam.org/family/PF12146 Serine aminopeptidase, S33], AB hydrolase superfamily, Monoacylglycerol lipase family|[[:Category:Monoglyceride lipase|Ligand list]]|Metabolic enzyme}}
==Summary==

===Protein Function ===
Monoacylglycerol lipase (MGL) is a cytosolic serine hydrolase that cleaves monoacylglycerols into fatty acid and glycerol through a catalytic mechanism that involves a classical serine-aspartate-histidine triad. MGL is a member of the α/β-hydrolase family of enzymes and is distantly related to microbial lysophospholipases and haloperoxidases. Because of its abundant expression in mammals in lipid-metabolizing tissues, such as white fat and liver, MGL is thought to catalyse the final step of the lipolytic cascade that releases fatty acids from triacylglycerol stores. In the brain, however, a primary role of MGL may be to carry out the hydrolysis and inactivation of the endocannabinoid neurotransmitter, 2-arachidonoyl-sn-glycerol (2-AG). (PMID: 19486005)
 

===Cys Function & Property===
Residues Cys201 and Cys208 are located within the lid domain, wherefrom they might be able to extend their sulphydryl groups towards the substrate-binding site, while residues Cys32 and Cys55 are positioned in two structurally conserved regions: Cys32 in the second beta-strand and Cys55 in a loop before the beginning of the first alpha-helix. Cys301 is not included in the model because it occupies a region of MGL that is not present in the chloroperoxidase template. 
[[File:588-function.png|center|600px]]
<div align="center">The positions of active site and Cysteine reisudes in MGL structure</div>

* Hydrophobic property:
:[[File:588-hydro.png||600px]]
* SASA:
:Unknown 

==Protein Sequence==

MPEASSPRRT PQNVPYQDLP HLVNADGQYL FCRYWKPSGT PKALIFVSHG 
AGEHCGRYDE LAQMLKRLDM LVFAHDHVGH GQSEGERMVV SDFQVFVRDL 
LQHVNTVQKD YPEVPVFLLG HSMGGAISIL AAAERPTHFS GMILISPLIL 
ANPESASTLK VLAAKLLNFV LPNISLGRID SSVLSRNKSE VDLYNSDPLI 
CHAGVKV'''C'''FG IQLLNAVSRV ERAMPRLTLP FLLLQGSADR LCDSKGAYLL 
MESSPSQDKT LKMYEGAYHV LHKELPEVTN SVLHEINTWV SHRIAVAGAR 
CLP 


==Structural Information==
*Known structure with covalent ligand: 
:Unknown 

*Protein structure:
:Unknown 

==Related Pathway==
*[https://www.genome.jp/kegg-bin/show_pathway?ko00561 Glycerolipid metabolism] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko04723 Retrograde endocannabinoid signaling] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko04923 Regulation of lipolysis in adipocytes] 

==Experimental Evidence==
:Cys-directed mutation, Homologous Analysis Of Sequence, Molecular Docking

==Reference==
# King A R, Lodola A, Carmi C, et al. '''A critical cysteine residue in monoacylglycerol lipase is targeted by a new class of isothiazolinone‐based enzyme inhibitors[J].''' British journal of pharmacology, 2009, 157(6): 974-983. [https://www.ncbi.nlm.nih.gov/pubmed/?term=19486005 19486005] 

[[Category:Targets]]
[[Category:Rattus norvegicus]]
[[Category:Metabolic enzyme]]
[[Category:Serine aminopeptidase, S33]]
[[Category:AB hydrolase superfamily]]
[[Category:Monoacylglycerol lipase family]]
[[Category:Glycerolipid metabolism]]
[[Category:Retrograde endocannabinoid signaling]]
[[Category:Regulation of lipolysis in adipocytes]]

@@ Line 35: / Line 35: @@
 *Protein structure:
-:[[File:588-function.png|center|600px]] <br/>
+:[[File:588-function.png|center|400px]] <br/>
 ==Related Pathway==

@@ Line 35: / Line 35: @@
 *Protein structure:
-:Unknown <br/>
+:[[File:588-function.png|center|600px]] <br/>
 ==Related Pathway==

@@ Line 10: / Line 10: @@
 ===Cys Function & Property===
-Residues Cys201 and Cys208 are located within the lid domain, wherefrom they might be able to extend their sulphydryl groups towards the substrate-binding site, while residues Cys32 and Cys55 are positioned in two structurally conserved regions: Cys32 in the second beta-strand and Cys55 in a loop before the beginning of the first alpha-helix. Cys301 is not included in the model because it occupies a region of MGL that is not present in the chloroperoxidase template. <br/>
+Residues Cys201 and Cys208 are located within the lid domain, wherefrom they might be able to extend their sulphydryl groups towards the substrate-binding site, while residues Cys32 and Cys55 are positioned in two structurally conserved regions: Cys32 in the second beta-strand and Cys55 in a loop before the beginning of the first alpha-helix. Cys301 is not included in the model because it occupies a region of MGL that is not present in the chloroperoxidase template. (PMID: 19486005)<br/>
 [[File:588-function.png|center|600px]]
 <div align="center">The positions of active site His269 and cysteine reisudes in MGL structure</div>

@@ Line 12: / Line 12: @@
 Residues Cys201 and Cys208 are located within the lid domain, wherefrom they might be able to extend their sulphydryl groups towards the substrate-binding site, while residues Cys32 and Cys55 are positioned in two structurally conserved regions: Cys32 in the second beta-strand and Cys55 in a loop before the beginning of the first alpha-helix. Cys301 is not included in the model because it occupies a region of MGL that is not present in the chloroperoxidase template. <br/>
 [[File:588-function.png|center|600px]]
-<div align="center">The positions of active site His269 and Cysteine reisudes in MGL structure</div>
+<div align="center">The positions of active site His269 and cysteine reisudes in MGL structure</div>
 * Hydrophobic property:

@@ Line 2: / Line 2: @@
    | __TOC__
    |}
-{{#invoke:InfoboxforTarget|run|MgII, MGL|[https://www.uniprot.org/uniprot/Q8R431 Q8R431]|Rattus norvegicus|Cys208|[http://pfam.xfam.org/family/PF12146 Serine aminopeptidase, S33], AB hydrolase superfamily, Monoacylglycerol lipase family|[[:Category:Monoglyceride lipase|Ligand list]]|Metabolic enzyme}}
+{{#invoke:InfoboxforTarget|run|MgII, MGL|[https://www.uniprot.org/uniprot/Q8R431 Q8R431]|Rattus norvegicus|Cys208|[http://pfam.xfam.org/family/PF12146 Serine aminopeptidase, S33],<br/>AB hydrolase superfamily, Monoacylglycerol lipase family|[[:Category:Monoglyceride lipase|Ligand list]]|Metabolic enzyme}}
 ==Summary==

Monoglyceride lipase - Revision history

Wu3857: /* Structural Information */

Wu3857 at 02:23, 2 December 2019

Wu3857 at 02:18, 2 December 2019

Wu3857: /* Summary */

Wu3857: /* Cys Function & Property */

Wu3857: /* Cys Function & Property */

Wu3857: Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|MgII, MGL|[https://www.uniprot.org/uniprot/Q8R431 Q8R431]|Rattus norvegicus|Cys208|[http://pfam.xfam.org/family..."

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|MgII, MGL|[https://www.uniprot.org/uniprot/Q8R431 Q8R431]|Rattus norvegicus|Cys208|[http://pfam.xfam.org/family..."