N-acylethanolamine-hydrolyzing acid amidase (Rattus norvegicus) - Revision history

Wu3857: /* Reference */

2019-08-19T23:21:17Z

‎Reference

Wu3857: /* Reference */

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‎Reference

Wu3857: /* Cys Function & Property */

2019-08-10T19:05:54Z

‎Cys Function & Property

Wu3857: /* Cys Function & Property */

2019-08-10T19:05:42Z

‎Cys Function & Property

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|ASAH-like protein, NAAA|[https://www.uniprot.org/uniprot/Q5KTC7 Q5KTC7]|Rattus norvegicus|Cys131|[http://pfam.x..."

2019-08-10T19:05:23Z

Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|ASAH-like protein, NAAA|[https://www.uniprot.org/uniprot/Q5KTC7 Q5KTC7]|Rattus norvegicus|Cys131|[http://pfam.x..."

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{{#invoke:InfoboxforTarget|run|ASAH-like protein, NAAA|[https://www.uniprot.org/uniprot/Q5KTC7 Q5KTC7]|Rattus norvegicus|Cys131|[http://pfam.xfam.org/family/PF02275 Linear amide C-N hydrolases, choloylglycine hydrolase family], Acid ceramidase family|[[:Category:N-acylethanolamine-hydrolyzing acid amidase (Rattus norvegicus)|Ligand list]]|Metabolic enzyme}}
==Summary==

===Protein Function ===
NAAA must operate under acidic conditions (pH ~4.5), and is completely inactivated at a pH of 8. Selective inhibitors of NAAA are ester and amide compounds, such as N-cyclohexanecarbonylpentadecylamine. NAAA is cleaved proteolytically at residue Cys126. NAAA cleaves C-N non-peptide bonds in linear amides, particularly ethanolamides. Its mechanism is quite similar to that of AC, which is further supported by AC's ability to cleave N-acylethanolamines (NAEs), albeit at far lower rates and with different specificities. While mechanistic details are not very well known, catalytic activity of NAAA is thought to be activated by Cys126 and Asp145. 
Fatty acid ethanolamines (FAEs) perform several physiological functions, most notably serving as messengers for pain and inflammation. NAAA's are found primarily in the lysosomal compartment of macrophages, in line with most inflammation-related proteins. They perform FAE hydrolysis, the final step in the signaling cascade for pain and inflammation, yielding an ethanolamine and a fatty acid. While it processes the cleavage of many different substrates, NAAA is most active with the substrate N-palmitoylethanolamine, suggesting that this is one of the key messengers of pain. (From Wikipedia) 
[[File:551-function.jpg|center|500px]]
<div align="center">Mechanism for the hydrolysis of ethanolamides by NAAA</div> 
===Cys Function & Property===
Cys131 is the active site of rat NAAA. 
:[[File:152.png|center|600px]]
<div align="center">Alignment of NAAA from different species</div> 

* Hydrophobic property:
:[[File:552-hydro.png||600px]]
* SASA：
:Cys131: Unknown 

==Protein Sequence==

MGTPAIRAAC HGAHLALALL LLLSLSDPWL WATAPGTPPL FNVSLDAAPE 
LRWLPMLQHY DPDFVRAAVA QVIGDRVPQW ILEMIGEIVQ KVESFLPQPF 
TSEIRGICDY LNLSLAEGVL VNLAYEASAF '''C'''TSIVAQDSQ GRIYHGRNLD 
YPFGNALRKL TADVQFVKNG QIVFTATTFV GYVGLWTGQS PHKFTISGDE 
RDKGWWWENM IAALSLGHSP ISWLIRKTLT ESEDFEAAVY TLAKTPLIAD 
VYYIVGGTSP QEGVVITRDR GGPADIWPLD PLNGAWFRVE TNYDHWEPVP 
KRDDRRTPAI KALNATGQAH LSLETLFQVL SVFPVYNNYT IYTTVMSAAE 
PDKYMTMIRN PS 


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

*Protein structure:
:Unknown 

==Related Pathway==
:Unknown 

==Experimental Evidence==
:Cys-directed Mutation, Homologous Analysis Of Sequence

==Reference==
# Armirotti A, Romeo E, Ponzano S, et al. '''β-Lactones inhibit N-acylethanolamine acid amidase by S-acylation of the catalytic N-terminal cysteine[J].''' ACS medicinal chemistry letters, 2012, 3(5): 422-426. [https://www.ncbi.nlm.nih.gov/pubmed/?term=24900487 24900487] 
# Solorzano C, Zhu C, Battista N, et al. '''Selective N-acylethanolamine-hydrolyzing acid amidase inhibition reveals a key role for endogenous palmitoylethanolamide in inflammation[J].''' Proceedings of the National Academy of Sciences, 2009, 106(49): 20966-20971. [https://www.ncbi.nlm.nih.gov/pubmed/?term=19926854 19926854]

[[Category:Targets|Targets]]
[[Category:Rattus norvegicus|Rattus norvegicus]]
[[Category:Metabolic enzyme|Metabolic enzyme]]
[[Category:Acid ceramidase family|Acid ceramidase family]]

@@ Line 50: / Line 50: @@
 [[Category:Targets]]
-[[Category:Homo sapiens]]
+[[Category:Rattus norvegicus]]
 [[Category:Metabolic enzyme]]
 [[Category:Acid ceramidase family]]

@@ Line 13: / Line 13: @@
 Cys131 is the active site of rat NAAA. <br/>
 :[[File:152.png|center|600px]]
-<div align="center">Alignment of NAAA from different species</div><br/>
+<div align="center">Alignment of NAAA sequences from different species</div><br/>
 * Hydrophobic property:

@@ Line 49: / Line 49: @@
 # Solorzano C, Zhu C, Battista N, et al. '''Selective N-acylethanolamine-hydrolyzing acid amidase inhibition reveals a key role for endogenous palmitoylethanolamide in inflammation[J].''' Proceedings of the National Academy of Sciences, 2009, 106(49): 20966-20971. [https://www.ncbi.nlm.nih.gov/pubmed/?term=19926854 19926854]
-[[Category:Targets|Targets]]
+[[Category:Targets]]
-[[Category:Rattus norvegicus|Rattus norvegicus]]
+[[Category:Homo sapiens]]
-[[Category:Metabolic enzyme|Metabolic enzyme]]
+[[Category:Metabolic enzyme]]
-[[Category:Acid ceramidase family|Acid ceramidase family]]
+[[Category:Acid ceramidase family]]

N-acylethanolamine-hydrolyzing acid amidase (Rattus norvegicus) - Revision history

Wu3857: /* Reference */

Wu3857: /* Reference */

Wu3857: /* Cys Function & Property */

Wu3857: /* Cys Function & Property */

Wu3857: Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|ASAH-like protein, NAAA|[https://www.uniprot.org/uniprot/Q5KTC7 Q5KTC7]|Rattus norvegicus|Cys131|[http://pfam.x..."

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|ASAH-like protein, NAAA|[https://www.uniprot.org/uniprot/Q5KTC7 Q5KTC7]|Rattus norvegicus|Cys131|[http://pfam.x..."