EC |
3.1.4.54 |
Accepted name: |
N-acetylphosphatidylethanolamine-hydrolysing phospholipase D |
Reaction: |
N-acylphosphatidylethanolamine + H2O = N-acylethanolamine + a 1,2-diacylglycerol 3-phosphate |
Other name(s): |
NAPE-PLD; anandamide-generating phospholipase D; N-acyl phosphatidylethanolamine phospholipase D; NAPE-hydrolyzing phospholipase D |
Systematic name: |
N-acetylphosphatidylethanolamine phosphatidohydrolase |
Comments: |
This enzyme is involved in the biosynthesis of anandamide. It does not hydrolyse phosphatidylcholine and phosphatidylethanolamine [1]. No transphosphatidation [1]. The enzyme contains Zn2+ and is activated by Mg2+ or Ca2+ [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Okamoto, Y., Morishita, J., Tsuboi, K., Tonai, T. and Ueda, N. Molecular characterization of a phospholipase D generating anandamide and its congeners. J. Biol. Chem. 279 (2004) 5298–5305. [DOI] [PMID: 14634025] |
2. |
Wang, J., Okamoto, Y., Morishita, J., Tsuboi, K., Miyatake, A. and Ueda, N. Functional analysis of the purified anandamide-generating phospholipase D as a member of the metallo-β-lactamase family. J. Biol. Chem. 281 (2006) 12325–12335. [DOI] [PMID: 16527816] |
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[EC 3.1.4.54 created 2011] |
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EC |
3.5.1.60 |
Accepted name: |
N-(long-chain-acyl)ethanolamine deacylase |
Reaction: |
N-(long-chain-acyl)ethanolamine + H2O = a long-chain carboxylate + ethanolamine |
Other name(s): |
NAAA (gene name); N-acylethanolamine amidohydrolase; acylethanolamine amidase |
Systematic name: |
N-(long-chain-acyl)ethanolamine amidohydrolase |
Comments: |
This lysosomal enzyme acts best on palmitoyl ethanolamide, with lower activity on other N-(long-chain-acyl)ethanolamines. It is only active at acidic pH. Unlike EC 3.5.1.99, fatty acid amide hydrolase, it does not act on primary amides such as oleamide, and has only a marginal activity with anandamide. The enzyme is translated as an inactive proenzyme, followed by autocatalytic cleavage into two subunits that reassociate to form an active heterodimeric complex. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 99283-61-1 |
References: |
1. |
Ueda, N., Yamanaka, K. and Yamamoto, S. Purification and characterization of an acid amidase selective for N-palmitoylethanolamine, a putative endogenous anti-inflammatory substance. J. Biol. Chem. 276 (2001) 35552–35557. [PMID: 11463796] |
2. |
Ueda, N., Yamanaka, K., Terasawa, Y. and Yamamoto, S. An acid amidase hydrolyzing anandamide as an endogenous ligand for cannabinoid receptors. FEBS Lett. 454 (1999) 267–270. [PMID: 10431820] |
3. |
West, J.M., Zvonok, N., Whitten, K.M., Wood, J.T. and Makriyannis, A. Mass spectrometric characterization of human N-acylethanolamine-hydrolyzing acid amidase. J. Proteome Res. 11 (2012) 972–981. [PMID: 22040171] |
4. |
Zhao, L.Y., Tsuboi, K., Okamoto, Y., Nagahata, S. and Ueda, N. Proteolytic activation and glycosylation of N-acylethanolamine-hydrolyzing acid amidase, a lysosomal enzyme involved in the endocannabinoid metabolism. Biochim. Biophys. Acta 1771 (2007) 1397–1405. [PMID: 17980170] |
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[EC 3.5.1.60 created 1989, modified 2019] |
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EC |
3.5.1.99 |
Accepted name: |
fatty acid amide hydrolase |
Reaction: |
(1) anandamide + H2O = arachidonic acid + ethanolamine (2) oleamide + H2O = oleic acid + NH3 |
Glossary: |
anandamide = (5Z,8Z,11Z,14Z)-N-(2-hydroxyethyl)icosa-5,8,11,14-tetraenamide |
Other name(s): |
FAAH; oleamide hydrolase; anandamide amidohydrolase |
Systematic name: |
fatty acylamide amidohydrolase |
Comments: |
Integral membrane protein, the enzyme is responsible for the catabolism of neuromodulatory fatty acid amides, including anandamide and oleamide, occurs in mammalia. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Boger, D.L., Fecik, R.A., Patterson, J.E., Miyauchi, H., Patricelli, M.P. and Cravatt, B.F. Fatty acid amide hydrolase substrate specificity. Bioorg. Med. Chem. Lett. 10 (2000) 2613–2616. [DOI] [PMID: 11128635] |
2. |
Patricelli, M.P., Lashuel, H.A., Giang, D.K., Kelly, J.W. and Cravatt, B.F. Comparative characterization of a wild type and transmembrane domain-deleted fatty acid amide hydrolase: identification of the transmembrane domain as a site for oligomerization. Biochemistry 37 (1998) 15177–15187. [DOI] [PMID: 9790682] |
3. |
Patricelli, M.P. and Cravatt, B.F. Characterization and manipulation of the acyl chain selectivity of fatty acid amide hydrolase. Biochemistry 40 (2001) 6107–6115. [DOI] [PMID: 11352748] |
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[EC 3.5.1.99 created 2009] |
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EC |
5.3.3.13 |
Accepted name: |
polyenoic fatty acid isomerase |
Reaction: |
(5Z,8Z,11Z,14Z,17Z)-icosapentaenoate = (5Z,7E,9E,14Z,17Z)-icosapentaenoate |
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For diagram of reaction, click here |
Other name(s): |
PFI; eicosapentaenoate cis-Δ5,8,11,14,17-eicosapentaenoate cis-Δ5-trans-Δ7,9-cis-Δ14,17 isomerase; (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate Δ8,11-Δ7,8-isomerase (incorrect); (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate Δ8,11-Δ7,9-isomerase (trans-double-bond-forming) |
Systematic name: |
(5Z,8Z,11Z,14Z,17Z)-icosapentaenoate Δ8,11-Δ7,9-isomerase (trans-double-bond-forming) |
Comments: |
The enzyme from the red alga Ptilota filicina catalyses the isomerization of skip dienes (methylene-interrupted double bonds) in a broad range of fatty acids and fatty-acid analogues, such as arachidonate and γ-linolenate, to yield a conjugated triene. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 159002-84-3 |
References: |
1. |
Wise, M.L., Hamberg, M. and Gerwick, W.H. Biosynthesis of conjugated fatty acids by a novel isomerase from the red marine alga Ptilota filicina. Biochemistry 33 (1994) 15223–15232. [PMID: 7803384] |
2. |
Wise, M.L., Soderstrom, K., Murray, T.F. and Gerwick, W.H. Synthesis and cannabinoid receptor binding activity of conjugated triene anandamide, a novel eicosanoid. Experientia 52 (1996) 88–92. [PMID: 8575565] |
3. |
Wise, M.L., Rossi, J. and Gerwick, W.H. Binding site characterization of polyenoic fatty-acid isomerase from the marine alga Ptilota filicina. Biochemistry 36 (1997) 2985–2992. [DOI] [PMID: 9062129] |
4. |
Zheng, W., Wise, M.L., Wyrick, A., Metz, J.G., Yuan, L. and Gerwick, W.H. Polyenoic fatty-acid isomerase from the marine red alga Ptilota filicina: protein characterization and functional expression of the cloned cDNA. Arch. Biochem. Biophys. 401 (2002) 11–20. [DOI] [PMID: 12054482] |
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[EC 5.3.3.13 created 2004] |
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