The Enzyme Database

Displaying entries 51-84 of 84.

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EC 3.1.1.8     
Accepted name: cholinesterase
Reaction: an acylcholine + H2O = choline + a carboxylate
Other name(s): pseudocholinesterase; butyrylcholine esterase; non-specific cholinesterase; choline esterase II (unspecific); benzoylcholinesterase; choline esterase; butyrylcholinesterase; propionylcholinesterase; BtChoEase
Systematic name: acylcholine acylhydrolase
Comments: Acts on a variety of choline esters and a few other compounds.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9001-08-5
References:
1.  Augustinsson, K.-B. Cholinesterases. A study in comparative enzymology. Acta Physiol. Scand. 15, Suppl. 2 (1948) .
2.  Augustinsson, K.-B. and Olsson, B. Esterases in the milk and blood plasma of swine. 1. Substrate specificity and electrophoresis studies. Biochem. J. 71 (1959) 477–484. [PMID: 13638253]
3.  Koelle, G.B. Cholinesterases of the tissues and sera of rabbits. Biochem. J. 53 (1953) 217–226. [PMID: 13032058]
4.  Nachmansohn, D. and Wilson, I.B. The enzymic hydrolysis and synthesis of acetylcholine. Adv. Enzymol. Relat. Subj. Biochem. 12 (1951) 259–339. [PMID: 14885021]
5.  Sawyer, C.H. Hydrolysis of choline esters by liver. Science 101 (1945) 385–386. [PMID: 17780326]
6.  Strelitz, F. Studies on cholinesterase. 4. Purification of pseudo-cholinesterase from horse serum. Biochem. J. 38 (1944) 86–88. [PMID: 16747753]
[EC 3.1.1.8 created 1961]
 
 
EC 3.1.1.9      
Deleted entry:  benzoylcholinesterase; a side reaction of EC 3.1.1.8 cholinesterase
[EC 3.1.1.9 created 1961, deleted 1972]
 
 
EC 3.1.1.25     
Accepted name: 1,4-lactonase
Reaction: a 1,4-lactone + H2O = a 4-hydroxyacid
Other name(s): γ-lactonase
Systematic name: 1,4-lactone hydroxyacylhydrolase
Comments: The enzyme is specific for 1,4-lactones with 4-8 carbon atoms. It does not hydrolyse simple aliphatic esters, acetylcholine, sugar lactones or substituted aliphatic lactones, e.g. 3-hydroxy-4-butyrolactone; requires Ca2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37278-38-9
References:
1.  Fishbein, W.N. and Bessman, S.P. Purification and properties of an enzyme in human blood and rat liver microsomes catalyzing the formation and hydrolysis of γ-lactones. I. Tissue localization, stoichiometry, specificity, distinction from esterase. J. Biol. Chem. 241 (1966) 4835–4841. [PMID: 4958984]
2.  Fishbein, W.N. and Bessman, S.P. Purification and properties of an enzyme in human blood and rat liver microsomes catalyzing the formation and hydrolysis of γ-lactones. II. Metal ion effects, kinetics, and equilibria. J. Biol. Chem. 241 (1966) 4842–4847. [PMID: 4958985]
[EC 3.1.1.25 created 1972, modified 1981]
 
 
EC 3.1.1.26     
Accepted name: galactolipase
Reaction: 1,2-diacyl-3-β-D-galactosyl-sn-glycerol + 2 H2O = 3-β-D-galactosyl-sn-glycerol + 2 carboxylates
Other name(s): galactolipid lipase; polygalactolipase; galactolipid acylhydrolase
Systematic name: 1,2-diacyl-3-β-D-galactosyl-sn-glycerol acylhydrolase
Comments: Also acts on 2,3-di-O-acyl-1-O-(6-O-α-D-galactosyl-β-D-galactosyl)-D-glycerol, and phosphatidylcholine and other phospholipids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37278-40-3
References:
1.  Helmsing, P.J. Purification and properties of galactolipase. Biochim. Biophys. Acta 178 (1969) 519–533. [DOI] [PMID: 5784904]
2.  Hirayama, O., Matsuda, H., Takeda, H., Maenaka, K. and Takatsuka, H. Purification and properties of a lipid acyl-hydrolase from potato tubers. Biochim. Biophys. Acta 384 (1975) 127–137. [DOI] [PMID: 236765]
[EC 3.1.1.26 created 1972]
 
 
EC 3.1.1.32     
Accepted name: phospholipase A1
Reaction: phosphatidylcholine + H2O = 2-acylglycerophosphocholine + a carboxylate
Systematic name: phosphatidylcholine 1-acylhydrolase
Comments: This enzyme has a much broader specificity than EC 3.1.1.4 phospholipase A2. Requires Ca2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9043-29-2
References:
1.  Gatt, S. Purification and properties of phospholipase A-1 from rat and calf brain. Biochim. Biophys. Acta 159 (1968) 304–316. [DOI] [PMID: 5657461]
2.  Scandella, C.J. and Kornberg, A. A membrane-bound phospholipase A1 purified from Escherichia coli. Biochemistry 10 (1971) 4447–4456. [PMID: 4946924]
3.  van den Bosch, H. Intracellular phospholipases A. Biochim. Biophys. Acta 604 (1980) 191–246. [DOI] [PMID: 6252969]
4.  van den Bosch, H., Aarsman, A.J. and van Deenen, L.L.M. Isolation and properties of a phospholipase A1 activity from beef pancreas. Biochim. Biophys. Acta 348 (1974) 197–209. [DOI] [PMID: 4858811]
[EC 3.1.1.32 created 1972, modified 1976]
 
 
EC 3.1.1.47     
Accepted name: 1-alkyl-2-acetylglycerophosphocholine esterase
Reaction: 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate
Other name(s): 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine acetylhydrolase; alkylacetyl-GPC:acetylhydrolase
Systematic name: 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine acetohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 76901-00-3
References:
1.  Blank, M.L., Lee, T.-C., Fitzgerald, V. and Snyder, F. A specific acetylhydrolase for 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine (a hypotensive and platelet-activating lipid). J. Biol. Chem. 256 (1981) 175–178. [PMID: 7451433]
[EC 3.1.1.47 created 1984]
 
 
EC 3.1.1.49     
Accepted name: sinapine esterase
Reaction: sinapoylcholine + H2O = sinapate + choline
Other name(s): aromatic choline esterase
Systematic name: sinapoylcholine sinapohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 72506-67-3
References:
1.  Nurmann, G. and Strack, D. Sinapine esterase. 1. Characterization of sinapine esterase from cotyledons of Raphanus sativus. Z. Naturforsch. C: Biosci. 34 (1979) 715–720.
[EC 3.1.1.49 created 1984]
 
 
EC 3.1.1.55     
Accepted name: acetylsalicylate deacetylase
Reaction: acetylsalicylate + H2O = salicylate + acetate
Other name(s): aspirin esterase; aspirin esterase; acetylsalicylic acid esterase; aspirin hydrolase
Systematic name: acetylsalicylate O-acetylhydrolase
Comments: Not identical with EC 3.1.1.1 (carboxylesterase), EC 3.1.1.2 (arylesterase), EC 3.1.1.7 (acetylcholinesterase) or EC 3.1.1.8 (cholinesterase). The activity of the liver cytosol enzyme is highest with acetyl esters of aryl alcohols, and thioesters are also hydrolysed; the microsomal enzyme also hydrolyses some other negatively charged esters, with highest activity on esters of salicylate with long-chain alcohols.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 87348-04-7
References:
1.  Ali, B. and Kaur, S. Mammalian tissue acetylsalicylic acid esterase(s): identification, distribution and discrimination from other esterases. J. Pharmacol. Exp. Ther. 226 (1983) 589–594. [PMID: 6875867]
2.  Kim, D.-H., Yang, Y.-S. and Jakoby, W.B. Aspirin hydrolyzing esterases from rat liver cytosol. Biochem. Pharmacol. 40 (1990) 481–487. [DOI] [PMID: 2383281]
3.  White, K.N. and Hope, D.B. Partial purification and characterization of a microsomal carboxylesterase specific for salicylate esters from guinea-pig liver. Biochim. Biophys. Acta 785 (1984) 138–147. [DOI] [PMID: 6704404]
[EC 3.1.1.55 created 1986, modified 1989]
 
 
EC 3.1.1.56     
Accepted name: methylumbelliferyl-acetate deacetylase
Reaction: 4-methylumbelliferyl acetate + H2O = 4-methylumbelliferone + acetate
Other name(s): esterase D
Systematic name: 4-methylumbelliferyl-acetate acylhydrolase
Comments: Acts on short-chain acyl esters of 4-methylumbelliferone, but not on naphthyl, indoxyl or thiocholine esters.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 83380-83-0
References:
1.  Hopkinson, D.A., Mestriner, M.A., Cortner, J. and Harris, H. Esterase D: a new human polymorphism. Ann. Hum. Genet. 37 (1973) 119–137. [DOI] [PMID: 4768551]
[EC 3.1.1.56 created 1986]
 
 
EC 3.1.1.71     
Accepted name: acetylalkylglycerol acetylhydrolase
Reaction: 2-acetyl-1-alkyl-sn-glycerol + H2O = 1-alkyl-sn-glycerol + acetate
Other name(s): alkylacetylglycerol acetylhydrolase
Systematic name: 2-acetyl-1-alkyl-sn-glycerol acetylhydrolase
Comments: Hydrolysis of the acetyl group from the 1-alkyl-2-acetyl and 1-alkyl-3-acetyl substrates occurs at apparently identical rates. The enzyme from Erlich ascites cells is membrane-bound. It differs from lipoprotein lipase (EC 3.1.1.34) since 1,2-diacetyl-sn-glycerols are not substrates. It also differs from EC 3.1.1.47, 1-acetyl-2-alkyl-glycerophosphocholine esterase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Blank, M.L., Smith, Z.L., Cress, E.A., Snyder, F. Characterization of the enzymatic hydrolysis of acetate from alkylacetylglycerols in the de novo pathway of PAF biosynthesis. Biochim. Biophys. Acta 1042 (1990) 153–158. [DOI] [PMID: 2302414]
[EC 3.1.1.71 created 1999]
 
 
EC 3.1.1.90     
Accepted name: all-trans-retinyl ester 13-cis isomerohydrolase
Reaction: an all-trans-retinyl ester + H2O = 13-cis-retinol + a fatty acid
For diagram of retinal and derivatives biosynthesis, click here
Systematic name: all-trans-retinyl ester acylhydrolase, 13-cis-retinol-forming
Comments: All-trans-retinyl esters, which are a storage form of vitamin A, are generated by the activity of EC 2.3.1.135, phosphatidylcholine—retinol O-acyltransferase (LRAT). They can be hydrolysed to 11-cis-retinol by EC 3.1.1.64, retinoid isomerohydrolase (RPE65), or to 13-cis-retinol by this enzyme.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Takahashi, Y., Moiseyev, G., Chen, Y., Farjo, K., Nikolaeva, O. and Ma, J.X. An enzymatic mechanism for generating the precursor of endogenous 13-cis retinoic acid in the brain. FEBS J. 278 (2011) 973–987. [DOI] [PMID: 21235714]
[EC 3.1.1.90 created 2011]
 
 
EC 3.1.1.111     
Accepted name: phosphatidylserine sn-1 acylhydrolase
Reaction: (1) a phosphatidylserine + H2O = a 2-acyl-1-lyso-phosphatidylserine + a fatty acid
(2) a 1-acyl-2-lyso-phosphatidylserine + H2O = glycerophosphoserine + a fatty acid
Glossary: phosphatidylserine = 3-sn-phosphatidyl-L-serine = 1,2-diacyl-sn-glycero-3-phospho-L-serine
glycerophosphoserine = sn-glycero-3-phospho-L-serine
Other name(s): phosphatidylserine-specific phospholipase A1; PS-PLA1; PLA1A (gene name)
Systematic name: 3-sn-phosphatidyl-L-serine sn-1 acylhydrolase
Comments: The enzyme, which has been described from mammals, is specific for phosphatidylserine and 2-lysophosphatidylserine, and does not act on phosphatidylcholine, phosphatidylethanolamine, phosphatidic acid or phosphatidylinositol.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sato, T., Aoki, J., Nagai, Y., Dohmae, N., Takio, K., Doi, T., Arai, H. and Inoue, K. Serine phospholipid-specific phospholipase A that is secreted from activated platelets. A new member of the lipase family. J. Biol. Chem. 272 (1997) 2192–2198. [PMID: 8999922]
2.  Nagai, Y., Aoki, J., Sato, T., Amano, K., Matsuda, Y., Arai, H. and Inoue, K. An alternative splicing form of phosphatidylserine-specific phospholipase A1 that exhibits lysophosphatidylserine-specific lysophospholipase activity in humans. J. Biol. Chem. 274 (1999) 11053–11059. [PMID: 10196188]
3.  Hosono, H., Aoki, J., Nagai, Y., Bandoh, K., Ishida, M., Taguchi, R., Arai, H. and Inoue, K. Phosphatidylserine-specific phospholipase A1 stimulates histamine release from rat peritoneal mast cells through production of 2-acyl-1-lysophosphatidylserine. J. Biol. Chem. 276 (2001) 29664–29670. [PMID: 11395520]
4.  Aoki, J., Nagai, Y., Hosono, H., Inoue, K. and Arai, H. Structure and function of phosphatidylserine-specific phospholipase A1. Biochim. Biophys. Acta 1582 (2002) 26–32. [PMID: 12069807]
[EC 3.1.1.111 created 2019]
 
 
EC 3.1.3.75     
Accepted name: phosphoethanolamine/phosphocholine phosphatase
Reaction: (1) O-phosphoethanolamine + H2O = ethanolamine + phosphate
(2) phosphocholine + H2O = choline + phosphate
Other name(s): PHOSPHO1; 3X11A
Systematic name: phosphoethanolamine phosphohydrolase
Comments: Requires active site Mg2+ but also works, to a lesser extent, with Co2+ and Mn2+. The enzyme is highly specific for phosphoethanolamine and phosphocholine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Houston, B., Seawright, E., Jefferies, D., Hoogland, E., Lester, D., Whitehead, C. and Farquharson, C. Identification and cloning of a novel phosphatase expressed at high levels in differentiating growth plate chondrocytes. Biochim. Biophys. Acta 1448 (1999) 500–506. [DOI] [PMID: 9990301]
2.  Stewart, A.J., Schmid, R., Blindauer, C.A., Paisey, S.J. and Farquharson, C. Comparative modelling of human PHOSPHO1 reveals a new group of phosphatases within the haloacid dehalogenase superfamily. Protein Eng. 16 (2003) 889–895. [DOI] [PMID: 14983068]
3.  Roberts, S.J., Stewart, A.J., Sadler, P.J. and Farquharson, C. Human PHOSPHO1 displays high specific phosphoethanolamine and phosphocholine phosphatase activities. Biochem. J. 382 (2004) 59–65. [DOI] [PMID: 15175005]
[EC 3.1.3.75 created 2004]
 
 
EC 3.1.4.2     
Accepted name: glycerophosphocholine phosphodiesterase
Reaction: sn-glycero-3-phosphocholine + H2O = choline + sn-glycerol 3-phosphate
Other name(s): glycerophosphinicocholine diesterase; glycerylphosphorylcholinediesterase; sn-glycero-3-phosphorylcholine diesterase; glycerolphosphorylcholine phosphodiesterase; glycerophosphohydrolase
Systematic name: sn-glycero-3-phosphocholine glycerophosphohydrolase
Comments: Also acts on sn-glycero-3-phosphoethanolamine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-85-8
References:
1.  Dawson, R.M.C. Liver glycerylphosphorylcholine diesterase. Biochem. J. 62 (1956) 689–693. [PMID: 13315235]
2.  Hayaishi, O. and Kornberg, A. Metabolism of phospholipides by bacterial enzymes. J. Biol. Chem. 206 (1954) 647–663. [PMID: 13143024]
3.  Webster, G.R., Marples, E.A. and Thompson, R.H.S. Glycerylphosphorylcholine diesterase activity in nervous tissue. Biochem. J. 65 (1957) 374–377. [PMID: 13403918]
[EC 3.1.4.2 created 1961, modified 1976]
 
 
EC 3.1.4.3     
Accepted name: phospholipase C
Reaction: a phosphatidylcholine + H2O = 1,2-diacyl-sn-glycerol + phosphocholine
Other name(s): lipophosphodiesterase I; lecithinase C; Clostridium welchii α-toxin; Clostridium oedematiens β- and γ-toxins; lipophosphodiesterase C; phosphatidase C; heat-labile hemolysin; α-toxin
Systematic name: phosphatidylcholine cholinephosphohydrolase
Comments: The bacterial enzyme, which is a zinc protein, also acts on sphingomyelin and phosphatidylinositol; that from seminal plasma does not act on phosphatidylinositol.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9001-86-9
References:
1.  Druzhinina, K.V. and Kritzman, M.G. [Lecithinase from animal tissues.] Biokhimiya 17 (1952) 77–81. [PMID: 13066482] (in Russian)
2.  Little, C. and Otnass, A.-B. The metal ion dependence of phospholipase C from Bacillus cereus. Biochim. Biophys. Acta 391 (1975) 326–333. [DOI] [PMID: 807246]
3.  Sheiknejad, R.G. and Srivastava, P.N. Isolation and properties of a phosphatidylcholine-specific phospholipase C from bull seminal plasma. J. Biol. Chem. 261 (1986) 7544–7549. [PMID: 3086312]
4.  Takahashi, T., Sugahara, T. and Ohsaka, A. Purification of Clostridium perfringens phospholipase C (α-toxin) by affinity chromatography on agarose-linked egg-yolk lipoprotein. Biochim. Biophys. Acta 351 (1974) 155–171. [DOI] [PMID: 4365891]
[EC 3.1.4.3 created 1961]
 
 
EC 3.1.4.4     
Accepted name: phospholipase D
Reaction: a phosphatidylcholine + H2O = choline + a phosphatidate
Other name(s): lipophosphodiesterase II; lecithinase D; choline phosphatase
Systematic name: phosphatidylcholine phosphatidohydrolase
Comments: Also acts on other phosphatidyl esters.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9001-87-0
References:
1.  Astrachan, L. The bond hydrolyzed by cardiolipin-specific phospholipase D. Biochim. Biophys. Acta 296 (1973) 79–88. [DOI] [PMID: 4632675]
2.  Einset, E. and Clark, W.L. The enzymatically catalyzed release of choline from lecithin. J. Biol. Chem. 231 (1958) 703–715. [PMID: 13539005]
3.  Hanahan, D.J. and Chaikoff, I.L. On the nature of the phosphorus-containing lipides of cabbage leaves and their relation to a phospholipide-splitting enzyme contained in these leaves. J. Biol. Chem. 172 (1948) 191–198. [PMID: 18920784]
4.  Tookey, H.L. and Balls, A.K. Plant phospholipase D. I. Studies on cottonseed and cabbage phospholipase D. J. Biol. Chem. 218 (1956) 213–224. [PMID: 13278329]
[EC 3.1.4.4 created 1961]
 
 
EC 3.1.4.12     
Accepted name: sphingomyelin phosphodiesterase
Reaction: a sphingomyelin + H2O = a ceramide + phosphocholine
Glossary: a ceramide = an N-acylsphingosine
Other name(s): neutral sphingomyelinase
Systematic name: sphingomyelin cholinephosphohydrolase
Comments: Has very little activity on phosphatidylcholine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-54-3
References:
1.  Barnholz, Y., Roitman, A. and Gatt, S. Enzymatic hydrolysis of sphingolipids. II. Hydrolysis of sphingomyelin by an enzyme from rat brain. J. Biol. Chem. 241 (1966) 3731–3737. [PMID: 5916388]
2.  Chatterjee, S. and Ghosh, N. Neutral sphingomyelinase from human urine. Purification and preparation of monospecific antibodies. J. Biol. Chem. 264 (1989) 12554–12561. [PMID: 2545711]
3.  Heller, M. and Shapiro, B. Enzymic hydrolysis of sphingomyelin by rat liver. Biochem. J. 98 (1966) 763–769. [PMID: 5911524]
4.  Kanfer, J.N., Young, O.M., Shapiro, D. and Brady, R.O. The metabolism of sphingomyelin. I. Purification and properties of a sphingomyelin-cleaving enzyme from rat liver tissue. J. Biol. Chem. 241 (1966) 1081–1084. [PMID: 5933867]
[EC 3.1.4.12 created 1972]
 
 
EC 3.1.4.38     
Accepted name: glycerophosphocholine cholinephosphodiesterase
Reaction: sn-glycero-3-phosphocholine + H2O = glycerol + phosphocholine
Other name(s): L-3-glycerylphosphinicocholine cholinephosphohydrolase
Systematic name: sn-glycero-3-phosphocholine cholinephosphohydrolase
Comments: No activity on sn-3-glycerophosphoethanolamine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 60063-78-7
References:
1.  Abra, R.M. and Quinn, P.J. A novel pathway for phosphatidylcholine catabolism in rat brain homogenates. Biochim. Biophys. Acta 380 (1975) 436–441. [DOI] [PMID: 166661]
[EC 3.1.4.38 created 1976]
 
 
EC 3.1.4.39     
Accepted name: alkylglycerophosphoethanolamine phosphodiesterase
Reaction: 1-alkyl-sn-glycero-3-phosphoethanolamine + H2O = 1-alkyl-sn-glycerol 3-phosphate + ethanolamine
Other name(s): lysophospholipase D
Systematic name: 1-alkyl-sn-glycero-3-phosphoethanolamine ethanolaminehydrolase
Comments: Also acts on acyl and choline analogues.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 62213-15-4
References:
1.  Wykle, R.L. and Schremmer, J.M. A lysophospholipase D pathway in the metabolism of ether-linked lipids in brain microsomes. J. Biol. Chem. 249 (1974) 1742–1746. [PMID: 4855486]
[EC 3.1.4.39 created 1976]
 
 
EC 3.1.4.41     
Accepted name: sphingomyelin phosphodiesterase D
Reaction: sphingomyelin + H2O = ceramide phosphate + choline
Other name(s): sphingomyelinase D
Systematic name: sphingomyelin ceramide-phosphohydrolase
Comments: Does not act on phosphatidylcholine, but hydrolyses 2-lysophosphatidylcholine to choline and 2-lysophosphatidate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 54992-31-3
References:
1.  Carne, H.R. and Onon, E. Action of Corynebacterium ovis exotoxin on endothelial cells of blood vessels. Nature 271 (1978) 246–248. [PMID: 622164]
2.  Soucek, A., Michalec, C. and Souckov, A. Identification and characterization of a new enzyme of the group phospholipase D isolated from Corynebacterium ovis. Biochim. Biophys. Acta 227 (1971) 116–128. [DOI] [PMID: 5543581]
[EC 3.1.4.41 created 1978]
 
 
EC 3.1.4.46     
Accepted name: glycerophosphodiester phosphodiesterase
Reaction: a glycerophosphodiester + H2O = an alcohol + sn-glycerol 3-phosphate
Other name(s): gene hpd protein; glycerophosphoryl diester phosphodiesterase; IgD-binding protein D
Systematic name: glycerophosphodiester glycerophosphohydrolase
Comments: Broad specificity for glycerophosphodiesters; glycerophosphocholine, glycerophosphoethanolamine, glycerophosphoglycerol and bis(glycerophospho)-glycerol are hydrolysed.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 86280-59-3
References:
1.  Larson, T.J., Ehrmann, M. and Boos, W. Periplasmic glycerophosphodiester phosphodiesterase of Escherichia coli, a new enzyme of the glp regulon. J. Biol. Chem. 258 (1983) 5428–5432. [PMID: 6304089]
[EC 3.1.4.46 created 1986]
 
 
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]
[EC 3.1.4.54 created 2011]
 
 
EC 3.1.6.6     
Accepted name: choline-sulfatase
Reaction: choline sulfate + H2O = choline + sulfate
Systematic name: choline-sulfate sulfohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-59-6
References:
1.  Takebe, I. Isolation and characterization of a new enzyme choline sulfatase. J. Biochem. (Tokyo) 50 (1961) 245–255. [PMID: 13919191]
[EC 3.1.6.6 created 1965]
 
 
EC 3.3.2.2     
Accepted name: lysoplasmalogenase
Reaction: (1) 1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O = an aldehyde + sn-glycero-3-phosphocholine
(2) 1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine + H2O = an aldehyde + sn-glycero-3-phosphoethanolamine
Other name(s): alkenylglycerophosphocholine hydrolase; alkenylglycerophosphoethanolamine hydrolase; 1-(1-alkenyl)-sn-glycero-3-phosphocholine aldehydohydrolase
Systematic name: lysoplasmalogen aldehydohydrolase
Comments: Lysoplasmalogenase is specific for the sn-2-deacylated (lyso) form of plasmalogen and catalyses hydrolytic cleavage of the vinyl ether bond, releasing a fatty aldehyde and sn-glycero-3-phosphocholine or sn-glycero-3-phosphoethanolamine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-65-6
References:
1.  Warner, H.R. and Lands, W.E.M. The metabolism of plasmalogen: enzymatic hydrolysis of the vinyl ether. J. Biol. Chem. 236 (1961) 2404–2409. [PMID: 13783189]
2.  Ellingson, J.S. and Lands, W.E.M. Phospholipid reactivation of plasmalogen metabolism. Lipids 3 (1968) 111–120. [DOI] [PMID: 17805898]
3.  Gunawan, J. and Debuch, H. Liberation of free aldehyde from 1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine (lysoplasmalogen) by rat liver microsomes. Hoppe-Seyler's Z. Physiol. Chem. 362 (1981) 445–452. [PMID: 7239443]
4.  Arthur, G., Page, L., Mock, T. and Choy, P.C. The catabolism of plasmenylcholine in the guinea pig heart. Biochem. J. 236 (1986) 475–480. [PMID: 3753461]
5.  Wu, L.C., Pfeiffer, D.R., Calhoon, E.A., Madiai, F., Marcucci, G., Liu, S. and Jurkowitz, M.S. Purification, identification, and cloning of lysoplasmalogenase, the enzyme that catalyzes hydrolysis of the vinyl ether bond of lysoplasmalogen. J. Biol. Chem. 286 (2011) 24916–24930. [DOI] [PMID: 21515882]
[EC 3.3.2.2 created 1972, modified 1976, (EC 3.3.2.5 created 1984, incorporated 2016), modified 2016]
 
 
EC 3.4.24.69     
Accepted name: bontoxilysin
Reaction: Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP), synaptosome-associated protein of 25 kDa (SNAP25) or syntaxin. No detected action on small molecule substrates
Other name(s): botulinum neurotoxin; BoNT
Comments: This zinc enzyme, produced by Clostridium botulinum, occurs as forms A-G that differ in specificity of action on the proteins of the neuroexocytosis apparatus [1-5]. The 150-kDa proenzymes of bontoxilysin are processed to disulfide-linked subunits of 100 and 50 kDa, the latter being responsible for the endopeptidase activities. Weakly inhibited by captopril, and phosphoramidon. Toxicity is due to action at the neuromuscular junctions that blocks release of acetylcholine, causing flaccid paralysis, in contrast to the spastic paralysis caused by tentoxilysin. In peptidase family M27 (tentoxilysin family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 107231-12-9
References:
1.  Schiavo, G., Rossetto, O., Catsicas, S., Polverino De Laureto, P., DasGupta, B.R., Benfenati, F. and Montecucco, C. Identification of the nerve-terminal targets of botulinum neurotoxins serotypes A, D and E. J. Biol. Chem. 268 (1993) 23784–23787. [PMID: 8226912]
2.  Schiavo, G., Santucci, A., DasGupta, B.R., Mehta, P.P., Jontes, J., Benfenati, F., Wilson, M.C. and Montecucco, C. Botulinum neurotoxins serotypes A and E cleave SNAP-25 at distinct COOH-terminal peptide bonds. FEBS Lett. 335 (1993) 99–103. [DOI] [PMID: 8243676]
3.  Schiavo, G., Shone, C.C., Rossetto, O., Alexander, F.C.G. and Montecucco, C. Botulinum neurotoxin serotype F is a zinc endopeptidase specific for VAMP/synaptobrevin. J. Biol. Chem. 268 (1993) 11516–11519. [PMID: 8505288]
4.  Schiavo, G., Malizio, C., Trimble, W.S., Polverino De Laureto, P., Milan, G., Sugiyama, H., Johnson, E.A. and Montecucco, C. Botulinum G neurotoxin cleaves VAMP/synaptobrevin at a single Ala-Ala peptide bond. J. Biol. Chem. 269 (1994) 20213–20216. [PMID: 8051110]
5.  Montecucco, C. and Schiavo, G. Mechanism of action of tetanus and botulinum neurotoxins. Mol. Microbiol. 8 (1994) 1–13. [DOI] [PMID: 7527117]
6.  Schiavo, G. and Montecucco, C. Tetanus and botulism neurotoxins. Methods Enzymol. 248 (1995) 643–652. [PMID: 7674951]
[EC 3.4.24.69 created 1995]
 
 
EC 3.5.1.13     
Accepted name: aryl-acylamidase
Reaction: an anilide + H2O = a carboxylate + aniline
Other name(s): AAA-1; AAA-2; brain acetylcholinesterase (is associated with AAA-2); pseudocholinesterase (associated with arylacylamidase)
Systematic name: aryl-acylamide amidohydrolase
Comments: Also acts on 4-substituted anilides.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-18-7
References:
1.  Nimmo-Smith, R.H. Aromatic N-deacylation by chick-kidney mitochondria. Biochem. J. 75 (1960) 284–293. [PMID: 14427286]
[EC 3.5.1.13 created 1965]
 
 
EC 3.5.1.109     
Accepted name: sphingomyelin deacylase
Reaction: (1) an N-acyl-sphingosylphosphorylcholine + H2O = a fatty acid + sphingosylphosphorylcholine
(2) a D-glucosyl-N-acylsphingosine + H2O = a fatty acid + D-glucosyl-sphingosine
Glossary: sphingomyelin = N-acyl-sphingosylphosphorylcholine
D-glucosyl-N-acylsphingosine = glucosylceramide
Other name(s): SM deacylase; GcSM deacylase; glucosylceramide sphingomyelin deacylase; sphingomyelin glucosylceramide deacylase; SM glucosylceramide GCer deacylase; SM-GCer deacylase; SMGCer deacylase
Systematic name: N-acyl-sphingosylphosphorylcholine amidohydrolase
Comments: The enzyme is involved in the sphingolipid metabolism in the epidermis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hara, J., Higuchi, K., Okamoto, R., Kawashima, M. and Imokawa, G. High-expression of sphingomyelin deacylase is an important determinant of ceramide deficiency leading to barrier disruption in atopic dermatitis. J. Invest. Dermatol. 115 (2000) 406–413. [DOI] [PMID: 10951276]
2.  Higuchi, K., Hara, J., Okamoto, R., Kawashima, M. and Imokawa, G. The skin of atopic dermatitis patients contains a novel enzyme, glucosylceramide sphingomyelin deacylase, which cleaves the N-acyl linkage of sphingomyelin and glucosylceramide. Biochem. J. 350 (2000) 747–756. [PMID: 10970788]
3.  Ishibashi, M., Arikawa, J., Okamoto, R., Kawashima, M., Takagi, Y., Ohguchi, K. and Imokawa, G. Abnormal expression of the novel epidermal enzyme, glucosylceramide deacylase, and the accumulation of its enzymatic reaction product, glucosylsphingosine, in the skin of patients with atopic dermatitis. Lab. Invest. 83 (2003) 397–408. [PMID: 12649340]
[EC 3.5.1.109 created 2011]
 
 
EC 3.6.1.53     
Accepted name: Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase
Reaction: (1) CDP-choline + H2O = CMP + phosphocholine
(2) ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate
Other name(s): Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase; ADPRibase-Mn
Systematic name: CDP-choline phosphohydrolase
Comments: Requires Mn2+. Unlike EC 3.6.1.13, ADP-ribose diphosphatase, it cannot utilize Mg2+. ADP-D-ribose, CDP-choline, CDP-ethanolamine and ADP are substrates for this enzyme but ADP-D-glucose, UDP-D-glucose, CDP-D-glucose, CDP, CMP and AMP are not hydrolysed [2]. The mammalian enzyme hydrolyses cyclic ADP-ribose to 1-(5-phospho-β-D-ribosyl)-AMP with ~100-fold lower efficiency than ADP-D-ribose [3]. In rat, the enzyme is found predominantly in thymus and spleen.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Canales, J., Pinto, R.M., Costas, M.J., Hernández, M.T., Miró, A., Bernet, D., Fernández, A. and Cameselle, J.C. Rat liver nucleoside diphosphosugar or diphosphoalcohol pyrophosphatases different from nucleotide pyrophosphatase or phosphodiesterase I: substrate specificities of Mg2+-and/or Mn2+-dependent hydrolases acting on ADP-ribose. Biochim. Biophys. Acta 1246 (1995) 167–177. [DOI] [PMID: 7819284]
2.  Canales, J., Fernández, A., Ribeiro, J.M., Cabezas, A., Rodrigues, J.R., Cameselle, J.C. and Costas, M.J. Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase: a novel metallophosphoesterase family preferentially expressed in rodent immune cells. Biochem. J. 413 (2008) 103–113. [DOI] [PMID: 18352857]
3.  Canales, J., Fernandez, A., Rodrigues, J.R., Ferreira, R., Ribeiro, J.M., Cabezas, A., Costas, M.J. and Cameselle, J.C. Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn(2+)-dependent ADP-ribose/CDP-alcohol pyrophosphatase. FEBS Lett. 583 (2009) 1593–1598. [DOI] [PMID: 19379742]
4.  Rodrigues, J.R., Fernandez, A., Canales, J., Cabezas, A., Ribeiro, J.M., Costas, M.J. and Cameselle, J.C. Characterization of Danio rerio Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase, the structural prototype of the ADPRibase-Mn-like protein family. PLoS One 7:e42249 (2012). [DOI] [PMID: 22848751]
[EC 3.6.1.53 created 2008]
 
 
EC 3.6.3.1      
Transferred entry: phospholipid-translocating ATPase. Now EC 7.6.2.1, P-type phospholipid transporter
[EC 3.6.3.1 created 2000 (EC 3.6.3.13 created 2000, incorporated 2001), deleted 2018]
 
 
EC 4.1.1.42     
Accepted name: carnitine decarboxylase
Reaction: carnitine = 2-methylcholine + CO2
Other name(s): carnitine carboxy-lyase
Systematic name: carnitine carboxy-lyase (2-methylcholine-forming)
Comments: Requires ATP.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37237-38-0
References:
1.  Khairallah, E.A. and Wolf, G. Carnitine decarboxylase. The conversion of carnitine to β-methylcholine. J. Biol. Chem. 242 (1967) 32–39. [PMID: 6016331]
[EC 4.1.1.42 created 1972]
 
 
EC 4.3.1.7     
Accepted name: ethanolamine ammonia-lyase
Reaction: ethanolamine = acetaldehyde + NH3
Other name(s): ethanolamine deaminase
Systematic name: ethanolamine ammonia-lyase (acetaldehyde-forming)
Comments: A cobalamin protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9054-69-7
References:
1.  Bradbeer, C. The clostridial fermentations of choline and ethanolamine. 1. Preparation and properties of cell-free extracts. J. Biol. Chem. 240 (1965) 4669. [PMID: 5846987]
2.  Bradbeer, C. The clostridial fermentations of choline and ethanolamine. II. Requirement for a cobamide coenzyme by an ethanolamine deaminase. J. Biol. Chem. 240 (1965) 4675–4681. [PMID: 5846988]
3.  Kaplan, B.H. and Stadtman, E.R. Ethanolamine deaminase, a cobamide coenzyme-dependent enzyme. I. Purification, assay, and properties of the enzyme. J. Biol. Chem. 243 (1968) 1787–1793. [PMID: 4297225]
[EC 4.3.1.7 created 1972]
 
 
EC 4.3.99.4     
Accepted name: choline trimethylamine-lyase
Reaction: choline = trimethylamine + acetaldehyde
Other name(s): cutC (gene name)
Systematic name: choline trimethylamine-lyase (acetaldehyde-forming)
Comments: The enzyme utilizes a glycine radical to break the C-N bond in choline. Found in choline-degrading anaerobic bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Craciun, S. and Balskus, E.P. Microbial conversion of choline to trimethylamine requires a glycyl radical enzyme. Proc. Natl. Acad. Sci. USA 109 (2012) 21307–21312. [DOI] [PMID: 23151509]
[EC 4.3.99.4 created 2013]
 
 
EC 5.2.1.3      
Deleted entry: retinal isomerase. Now known to be catalysed by a pathway involving EC 1.1.1.300, NADP-retinol dehydrogenase; EC 2.3.1.135, phosphatidylcholine—retinol O-acyltransferase; EC 3.1.1.64, retinoid isomerohydrolase; and EC 1.1.1.315, 11-cis-retinol dehydrogenase.
[EC 5.2.1.3 created 1961, modified 1976, deleted 2011]
 
 
EC 7.6.2.1     
Accepted name: P-type phospholipid transporter
Reaction: ATP + H2O + phospholipid[side 1] = ADP + phosphate + phospholipid[side 2]
Other name(s): Mg2+-ATPase (ambiguous); flippase (ambiguous); aminophospholipid-transporting ATPase (ambiguous); phospholipid-translocating ATPase (ambiguous); phospholipid-transporting ATPase (ambiguous)
Systematic name: ATP phosphohydrolase (P-type, phospholipid-flipping)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. Different forms of the enzyme move phospholipids such as phosphatidylcholine, lyso-phosphatidylcholine, phosphatidylserine, phosphatidylethanolamine, phosphatidyglycerol, sphingomyelin and glucosylceramide from one membrane face to the other (‘flippase’).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Morris, M.B., Auland, M.E., Xu, Y.H. and Roufogalis, B.D. Characterization of the Mg2+-ATPase activity of the human erythrocyte membrane. Biochem. Mol. Biol. Int. 31 (1993) 823–832. [PMID: 8136700]
2.  Vermeulen, W.P., Briede, J.J. and Rolofsen, B. Manipulation of the phosphatidylethanolamine pool in the human red cell membrane affects its Mg2+-ATPase activity. Mol. Membr. Biol. 13 (1996) 95–102. [PMID: 8839453]
3.  Suzuki, H., Kamakura, M., Morii, M. and Takeguchi, N. The phospholipid flippase activity of gastric vesicles. J. Biol. Chem. 272 (1997) 10429–10434. [DOI] [PMID: 9099684]
4.  Auland, M.E., Roufogalis, B.D., Devaux, P.F. and Zachowski, A. Reconstitution of ATP-dependent aminophospholipid translocation in proteoliposomes. Proc. Natl. Acad. Sci. USA 91 (1994) 10938–10942. [DOI] [PMID: 7971987]
5.  Alder-Baerens, N., Lisman, Q., Luong, L., Pomorski, T. and Holthuis, J.C. Loss of P4 ATPases Drs2p and Dnf3p disrupts aminophospholipid transport and asymmetry in yeast post-Golgi secretory vesicles. Mol. Biol. Cell 17 (2006) 1632–1642. [DOI] [PMID: 16452632]
6.  Lopez-Marques, R.L., Poulsen, L.R., Hanisch, S., Meffert, K., Buch-Pedersen, M.J., Jakobsen, M.K., Pomorski, T.G. and Palmgren, M.G. Intracellular targeting signals and lipid specificity determinants of the ALA/ALIS P4-ATPase complex reside in the catalytic ALA α-subunit. Mol. Biol. Cell 21 (2010) 791–801. [DOI] [PMID: 20053675]
7.  Jensen, M.S., Costa, S.R., Duelli, A.S., Andersen, P.A., Poulsen, L.R., Stanchev, L.D., Gourdon, P., Palmgren, M., Günther Pomorski, T. and Lopez-Marques, R.L. Phospholipid flipping involves a central cavity in P4 ATPases. Sci. Rep. 7:17621 (2017). [PMID: 29247234]
[EC 7.6.2.1 created 2000 as EC 3.6.3.1 (EC 3.6.3.13 created 2000, incorporated 2001), transferred 2018 to EC 7.6.2.1]
 
 


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