The Enzyme Database

Your query returned 4 entries.    printer_iconPrintable version

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
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]
[EC created 2011]
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, 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, CAS registry number: 99283-61-1
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]
[EC created 1989, modified 2019]
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
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]
[EC created 2009]
Accepted name: polyenoic fatty acid isomerase
Reaction: (5Z,8Z,11Z,14Z,17Z)-icosapentaenoate = (5Z,7E,9E,14Z,17Z)-icosapentaenoate
For diagram of reaction, click here
Other name(s): PFI; eicosapentaenoate cis5,8,11,14,17-eicosapentaenoate cis5-trans7,9-cis14,17 isomerase; (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate Δ8,117,8-isomerase (incorrect); (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate Δ8,117,9-isomerase (trans-double-bond-forming)
Systematic name: (5Z,8Z,11Z,14Z,17Z)-icosapentaenoate Δ8,117,9-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
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]
[EC created 2004]

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