EC |
3.1.4.1 |
Accepted name: |
phosphodiesterase I |
Reaction: |
Hydrolytically removes 5′-nucleotides successively from the 3′-hydroxy termini of 3′-hydroxy-terminated oligonucleotides |
Other name(s): |
5′-exonuclease; 5′-phosphodiesterase; 5′-nucleotide phosphodiesterase; oligonucleate 5′-nucleotidohydrolase; 5′ nucleotide phosphodiesterase/alkaline phosphodiesterase I; 5′-NPDase; 5′-PDase; 5′-PDE; 5’NPDE; alkaline phosphodiesterase; nucleotide pyrophosphatase/phosphodiesterase I; orthophosphoric diester phosphohydrolase; PDE I; phosphodiesterase (ambiguous); exonuclease I |
Systematic name: |
oligonucleotide 5′-nucleotidohydrolase |
Comments: |
Hydrolyses both ribonucleotides and deoxyribonucleotides. Has low activity towards polynucleotides. A 3′-phosphate terminus on the substrate inhibits hydrolysis. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9025-82-5 |
References: |
1. |
Khorana, G.H. Phosphodiesterases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 5, Academic Press, New York, 1961, pp. 79–94. |
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[EC 3.1.4.1 created 1961] |
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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] |
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[EC 3.1.4.2 created 1961, modified 1976] |
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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] |
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[EC 3.1.4.3 created 1961] |
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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] |
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[EC 3.1.4.4 created 1961] |
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EC
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3.1.4.5
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Transferred entry: | deoxyribonuclease. Now EC 3.1.21.1, deoxyribonuclease I
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[EC 3.1.4.5 created 1961, deleted 1978] |
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EC
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3.1.4.6
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Transferred entry: | deoxyribonuclease II. Now EC 3.1.22.1, deoxyribonuclease II
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[EC 3.1.4.6 created 1961, deleted 1978] |
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EC
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3.1.4.7
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Transferred entry: | micrococcal nuclease. Now EC 3.1.31.1, micrococcal nuclease
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[EC 3.1.4.7 created 1961, deleted 1978] |
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EC
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3.1.4.8
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Transferred entry: | Aspergillus oryzae ribonuclease. Now EC 3.1.27.3, ribonuclease T1
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[EC 3.1.4.8 created 1961, transferred 1965 to EC 2.7.7.26, reinstated 1972, deleted 1978] |
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EC
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3.1.4.9
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Transferred entry: | nucleate endonuclease. Now EC 3.1.30.2, Serratia marcescens nuclease
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[EC 3.1.4.9 created 1965, deleted 1978] |
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EC
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3.1.4.10
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Transferred entry: | 1-phosphatidylinositol phosphodiesterase. Now EC 4.6.1.13, phosphatidylinositol diacylglycerol-lyase. As there is no hydrolysis of the inositol 1,2-cyclic phosphate formed, previous classification of the enzyme as a hydrolase was incorrect
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[EC 3.1.4.10 created 1972, modified 1976, deleted 2002] |
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EC |
3.1.4.11 |
Accepted name: |
phosphoinositide phospholipase C |
Reaction: |
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol |
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For diagram of myo-inositol-phosphate biosynthesis, click here |
Other name(s): |
triphosphoinositide phosphodiesterase; phosphoinositidase C; 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase; monophosphatidylinositol phosphodiesterase; phosphatidylinositol phospholipase C; PI-PLC; 1-phosphatidyl-D-myo-inositol-4,5-bisphosphate inositoltrisphosphohydrolase |
Systematic name: |
1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate inositoltrisphosphohydrolase |
Comments: |
These enzymes form some of the cyclic phosphate Ins(cyclic1,2)P(4,5)P2 as well as Ins(1,4,5)P3. They show activity towards phosphatidylinositol, i.e., the activity of EC 4.6.1.13, phosphatidylinositol diacylglycerol-lyase, in vitro at high [Ca2+]. Four β-isoforms regulated by G-proteins, two γ-forms regulated by tyrosine kinases, four δ-forms regulated at least in part by calcium and an ε-form, probably regulated by the oncogene ras, have been found. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 63551-76-8 |
References: |
1. |
Downes, C.P. and Michell, R.H. The polyphosphoinositide phosphodiesterase of erythrocyte membranes. Biochem. J. 198 (1981) 133–140. [PMID: 6275838] |
2. |
Thompson, W. and Dawson, R.M.C. The triphosphoinositide phosphodiesterase of brain tissue. Biochem. J. 91 (1964) 237–243. [PMID: 4284484] |
3. |
Rhee, S.G. and Bae, Y.S. Regulation of phosphoinositide-specific phospholipase C isozymes. J. Biol. Chem. 272 (1997) 15045–15048. [DOI] [PMID: 9182519] |
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[EC 3.1.4.11 created 1972, modified 2002] |
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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] |
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[EC 3.1.4.12 created 1972] |
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EC |
3.1.4.13 |
Accepted name: |
serine-ethanolaminephosphate phosphodiesterase |
Reaction: |
serine phosphoethanolamine + H2O = serine + ethanolamine phosphate |
Other name(s): |
serine ethanolamine phosphodiester phosphodiesterase; SEP diesterase |
Systematic name: |
serine-phosphoethanolamine ethanolaminephosphohydrolase |
Comments: |
Acts only on those phosphodiesters that have ethanolamine as a component part of the molecule. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-20-3 |
References: |
1. |
Hagerman, D.D., Rosenberg, H., Ennor, A.H., Schiff, P. and Inove, S. The isolation and properties of chicken kidney serine ethanolamine phosphate phosphodiesterase. J. Biol. Chem. 240 (1965) 1108. [PMID: 14284710] |
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[EC 3.1.4.13 created 1972, modified 1976] |
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EC |
3.1.4.14 |
Accepted name: |
[acyl-carrier-protein] phosphodiesterase |
Reaction: |
holo-[acyl-carrier protein] + H2O = 4′-phosphopantetheine + apo-[acyl-carrier protein] |
Other name(s): |
ACP hydrolyase; ACP phosphodiesterase; AcpH; [acyl-carrier-protein] 4′-pantetheine-phosphohydrolase; holo-[acyl-carrier-protein] 4′-pantetheine-phosphohydrolase |
Systematic name: |
holo-[acyl-carrier protein] 4′-pantetheine-phosphohydrolase |
Comments: |
The enzyme cleaves acyl-[acyl-carrier-protein] species with acyl chains of 6-16 carbon atoms although it appears to demonstrate a preference for the unacylated acyl-carrier protein (ACP) and short-chain ACPs over the medium- and long-chain species [3]. Deletion of the gene encoding this enzyme abolishes ACP cofactor turnover in vivo [3]. Activation of apo-ACP to form the holoenzyme is carried out by EC 2.7.8.7, holo-[acyl-carrier-protein] synthase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-21-4 |
References: |
1. |
Sobhy, C. Regulation of fatty acid synthetase activity. The 4′-phosphopantetheine hydrolase of rat liver. J. Biol. Chem. 254 (1979) 8561–8566. [DOI] [PMID: 224058] |
2. |
Vagelos, P.R. and Larrabee, A.R. Acyl carrier protein. IX. Acyl carrier protein hydrolase. J. Biol. Chem. 242 (1967) 1776–1781. [DOI] [PMID: 4290442] |
3. |
Thomas, J. and Cronan, J.E. The enigmatic acyl carrier protein phosphodiesterase of Escherichia coli: genetic and enzymological characterization. J. Biol. Chem. 280 (2005) 34675–34683. [DOI] [PMID: 16107329] |
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[EC 3.1.4.14 created 1972, modified 2006] |
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EC
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3.1.4.15
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Transferred entry: | adenylyl-[glutamateammonia ligase] hydrolase. As it has been shown that the enzyme catalyses a transfer of the adenylyl group to phosphate, the enzyme has been transferred to EC 2.7.7.89, adenylyl-[glutamateammonia ligase] phosphorylase
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[EC 3.1.4.15 created 1972, deleted 2015] |
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EC |
3.1.4.16 |
Accepted name: |
2′,3′-cyclic-nucleotide 2′-phosphodiesterase |
Reaction: |
nucleoside 2′,3′-cyclic phosphate + H2O = nucleoside 3′-phosphate |
Other name(s): |
ribonucleoside 2′,3′-cyclic phosphate diesterase; 2′,3 '-cyclic AMP phosphodiesterase; 2′,3′-cyclic nucleotidase; cyclic 2′,3′-nucleotide 2′-phosphodiesterase; cyclic 2′,3′-nucleotide phosphodiesterase; 2′,3′-cyclic nucleoside monophosphate phosphodiesterase; 2′,3′-cyclic AMP 2′-phosphohydrolase; cyclic phosphodiesterase:3′-nucleotidase; 2′,3′-cyclic nucleotide phosphohydrolase; 2′:3′-cyclic phosphodiesterase; 2′:3′-cyclic nucleotide phosphodiesterase:3′-nucleotidase |
Systematic name: |
nucleoside-2′,3′-cyclic-phosphate 3′-nucleotidohydrolase |
Comments: |
Also hydrolyses 3′-nucleoside monophosphates and bis-4-nitrophenyl phosphate, but not 3′-deoxynucleotides. Similar reactions are carried out by EC 4.6.1.24 (ribonuclease T1) and EC 4.6.1.18 (pancreatic ribonuclease). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9037-18-7 |
References: |
1. |
Anraku, Y. A new cyclic phosphodiesterase having a 3′-nucleotidase activity from Escherichia coli B. I. Purification and some properties of the enzyme. J. Biol. Chem. 239 (1964) 3412–3419. [PMID: 14245396] |
2. |
Anraku, Y. A new cyclic phosphodiesterase having a 3′-nucleotidase activity from Escherichia coli B. II. Further studies on substrate specificity and mode of action of the enzyme. J. Biol. Chem. 239 (1964) 3420–3424. [PMID: 14245397] |
3. |
Center, M.S. and Behal, F.J. A cyclic phosphodiesterase with 3′-nucleotidase activity from Proteus mirabilis. J. Biol. Chem. 243 (1968) 138–143. [PMID: 4295113] |
4. |
Olafson, R.W., Drummond, G.I. and Lee, J.F. Studies on 2′,3′-cyclic nucleotide-3′-phosphohydrolase from brain. Can. J. Biochem. 47 (1969) 961–966. [PMID: 4310670] |
5. |
Unemoto, T. and Hayashi, M. Chloride ion as a modifier of 2′,3′-cyclic phosphodiesterase purified from halophilic Vibrio alginolyticus. Biochim. Biophys. Acta 171 (1969) 89–102. [DOI] [PMID: 4303200] |
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[EC 3.1.4.16 created 1972, modified 1976] |
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EC |
3.1.4.17 |
Accepted name: |
3′,5′-cyclic-nucleotide phosphodiesterase |
Reaction: |
nucleoside 3′,5′-cyclic phosphate + H2O = nucleoside 5′-phosphate |
Other name(s): |
cyclic 3′,5′-mononucleotide phosphodiesterase; PDE; cyclic 3′,5′-nucleotide phosphodiesterase; cyclic 3′,5′-phosphodiesterase; 3′,5′-nucleotide phosphodiesterase; 3′:5′-cyclic nucleotide 5′-nucleotidohydrolase; 3′,5′-cyclonucleotide phosphodiesterase; cyclic nucleotide phosphodiesterase; 3′, 5′-cyclic nucleoside monophosphate phosphodiesterase; 3′: 5′-monophosphate phosphodiesterase (cyclic CMP); cytidine 3′:5′-monophosphate phosphodiesterase (cyclic CMP); cyclic 3′,5-nucleotide monophosphate phosphodiesterase; nucleoside 3′,5′-cyclic phosphate diesterase; nucleoside-3′,5-monophosphate phosphodiesterase |
Systematic name: |
3′,5′-cyclic-nucleotide 5′-nucleotidohydrolase |
Comments: |
Acts on 3′,5′-cyclic AMP, 3′,5′-cyclic dAMP, 3′,5′-cyclic IMP, 3′,5′-cyclic GMP and 3′,5′-cyclic CMP. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9040-59-9 |
References: |
1. |
Fischer, U. and Amrhein, N. Cyclic nucleotide phosphodiesterase of Chlamydomonas reinhardtii. Biochim. Biophys. Acta 341 (1974) 412–420. [DOI] [PMID: 4365506] |
2. |
Nair, K.G. Purification and properties of 3′,5′-cyclic nucleotide phosphodiesterase from dog heart. Biochemistry 5 (1966) 150–157. [PMID: 4287216] |
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[EC 3.1.4.17 created 1972, modified 1976] |
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EC
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3.1.4.18
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Transferred entry: | phosphodiesterase II. Now EC 3.1.16.1, spleen exonuclease
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[EC 3.1.4.18 created 1972, deleted 1978] |
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EC
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3.1.4.19
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Transferred entry: | oligonucleotidase. Now EC 3.1.13.3, oligonucleotidase
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[EC 3.1.4.19 created 1972, deleted 1978] |
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EC
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3.1.4.20
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Transferred entry: | exoribonuclease. Now EC 3.1.13.1, exoribonuclease II
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[EC 3.1.4.20 created 1972, deleted 1978] |
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EC
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3.1.4.21
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Transferred entry: | single-stranded-nucleate endonuclease. Now EC 3.1.30.1, Aspergillus nuclease S1
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[EC 3.1.4.21 created 1972, deleted 1978] |
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EC
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3.1.4.22
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Transferred entry: | ribonuclease I. Now EC 3.1.27.5, pancreatic ribonuclease
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[EC 3.1.4.22 created 1972, deleted 1978] |
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EC
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3.1.4.23
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Transferred entry: | ribonuclease II. Now EC 3.1.27.1, ribonuclease T2
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[EC 3.1.4.23 created 1972, deleted 1978] |
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EC
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3.1.4.24
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Deleted entry: | endoribonuclease III |
[EC 3.1.4.24 created 1972, deleted 1978] |
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EC
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3.1.4.25
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Transferred entry: | exodeoxyribonuclease I. Now EC 3.1.11.1, exodeoxyribonuclease I
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[EC 3.1.4.25 created 1972, deleted 1978] |
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EC
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3.1.4.26
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Deleted entry: | exodeoxyribonuclease II |
[EC 3.1.4.26 created 1972, deleted 1978] |
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EC
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3.1.4.27
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Transferred entry: | exodeoxyribonuclease III. Now EC 3.1.11.2, exodeoxyribonuclease III
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[EC 3.1.4.27 created 1972, deleted 1978] |
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EC
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3.1.4.28
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Transferred entry: | exodeoxyribonuclease IV. Now EC 3.1.11.3, exodeoxyribonuclease (lambda-induced)
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[EC 3.1.4.28 created 1972, deleted 1978] |
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EC
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3.1.4.29
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Deleted entry: | oligodeoxyribonucleate exonuclease |
[EC 3.1.4.29 created 1972, deleted 1978] |
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EC
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3.1.4.30
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Transferred entry: | endodeoxyribonuclease. Now EC 3.1.21.2, deoxyribonuclease IV (phage-T4-induced)
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[EC 3.1.4.30 created 1972, deleted 1978] |
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EC
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3.1.4.31
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Transferred entry: | DNA 5′-dinucleotidohydrolase. Now EC 3.1.11.4, exodeoxyribonuclease (phage SP3-induced)
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[EC 3.1.4.31 created 1972, deleted 1978] |
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EC
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3.1.4.32
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Deleted entry: | endodeoxyribonuclease (ATP- and S-adenosylmethionine-dependent). See EC 3.1.21.3 type 1 site-specific deoxyribonuclease and EC 3.1.21.5 type III site-specific deoxyribonuclease |
[EC 3.1.4.32 created 1972, deleted 1978] |
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EC
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3.1.4.33
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Deleted entry: | endodeoxyribonuclease (ATP-hydrolysing). See EC 3.1.21.3 type 1 site-specific deoxyribonuclease and EC 3.1.21.5 type III site-specific deoxyribonuclease |
[EC 3.1.4.33 created 1972, deleted 1978] |
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EC
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3.1.4.34
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Deleted entry: | hybrid nuclease. See sub-subclasses EC 3.1.15, EC 3.1.16, EC 3.1.30 and EC 3.1.31. |
[EC 3.1.4.34 created 1972, deleted 1978] |
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EC |
3.1.4.35 |
Accepted name: |
3′,5′-cyclic-GMP phosphodiesterase |
Reaction: |
guanosine 3′,5′-cyclic phosphate + H2O = GMP |
Glossary: |
GMP = guanosine 5′-phosphate |
Other name(s): |
guanosine cyclic 3′,5′-phosphate phosphodiesterase; cyclic GMP phosphodiesterase; cyclic 3′,5′-GMP phosphodiesterase; cyclic guanosine 3′,5′-monophosphate phosphodiesterase; cyclic guanosine 3′,5′-phosphate phosphodiesterase; cGMP phosphodiesterase; cGMP-PDE |
Systematic name: |
3′,5′-cyclic-GMP 5′-nucleotidohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9068-52-4 |
References: |
1. |
Marks, F. and Raab, I. The second messenger system of mouse epidermis. IV. Cyclic AMP and cyclic GMP phosphodiesterase. Biochim. Biophys. Acta 334 (1974) 368–377. |
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[EC 3.1.4.35 created 1976] |
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EC
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3.1.4.36
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Deleted entry: | 1,2-cyclic-inositol-phosphate phosphodiesterase. Now included with EC 3.1.4.43, glycerophosphoinositol inositolphosphodiesterase |
[EC 3.1.4.36 created 1976, deleted 2002] |
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EC |
3.1.4.37 |
Accepted name: |
2′,3′-cyclic-nucleotide 3′-phosphodiesterase |
Reaction: |
nucleoside 2′,3′-cyclic phosphate + H2O = nucleoside 2′-phosphate |
Other name(s): |
cyclic-CMP phosphodiesterase; 2′,3′-cyclic AMP phosphodiesterase; cyclic 2′,3′-nucleotide 3′-phosphodiesterase; cyclic 2′,3′-nucleotide phosphodiesterase; 2′,3′-cyclic nucleoside monophosphate phosphodiesterase; 2′,3′-cyclic nucleotide 3′-phosphohydrolase; CNPase; 2′,3′-cyclic nucleotide phosphohydrolase; 2′:3′-cyclic nucleotide 3′-phosphodiesterase; 2′:3′-CNMP-3′-ase |
Systematic name: |
nucleoside-2′,3′-cyclic-phosphate 2′-nucleotidohydrolase |
Comments: |
The brain enzyme acts on 2′,3′-cyclic AMP more rapidly than on the UMP or CMP derivatives. An enzyme from liver acts on 2′,3′-cyclic CMP more rapidly than on the purine derivatives; it also hydrolyses the corresponding 3′,5′-cyclic phosphates, but more slowly. This latter enzyme has been called cyclic-CMP phosphodiesterase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 60098-35-3 |
References: |
1. |
Drummond, G.I., Iyer, N.T. and Keith, J. Hydrolysis of ribonucleoside 2′,3′-cyclic phosphates by a diesterase from brain. J. Biol. Chem. 237 (1962) 3535–3539. |
2. |
Helfman, D.M. and Kuo, J.F. A homogeneous cyclic CMP phosphodiesterase hydrolyzes both pyrimidine and purine cyclic 2′:3′- and 3′:5′-nucleotides. J. Biol. Chem. 257 (1982) 1044–1047. [PMID: 6274851] |
3. |
Helfman, D.M., Shoji, M. and Kuo, J.F. Purification to homogeneity and general properties of a novel phosphodiesterase hydrolyzing cyclic CMP and cyclic AMP. J. Biol. Chem. 256 (1981) 6327–6334. [PMID: 6263914] |
4. |
Kurihara, T., Nishizawa, Y., Takahashi, Y. and Odani, S. Chemical, immunological and catalytic properties of 2′:3′-cyclic nucleotide 3′-phosphodiesterase purified from brain white matter. Biochem. J. 195 (1981) 153–157. [PMID: 6272743] |
5. |
Nishizawa, Y., Kurihara, T. and Takahashi, Y. Spectrophotometric assay, solubilization and purification of brain 2′:3′-cyclic nucleotide 3′-phosphodiesterase. Biochem. J. 191 (1980) 71–82. [PMID: 6258586] |
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[EC 3.1.4.37 created 1976] |
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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] |
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[EC 3.1.4.38 created 1976] |
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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] |
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[EC 3.1.4.39 created 1976] |
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EC |
3.1.4.40 |
Accepted name: |
CMP-N-acylneuraminate phosphodiesterase |
Reaction: |
CMP-N-acylneuraminate + H2O = CMP + N-acylneuraminate |
Other name(s): |
CMP-sialate hydrolase; CMP-sialic acid hydrolase; CMP-N-acylneuraminic acid hydrolase; cytidine monophosphosialic hydrolase; cytidine monophosphosialate hydrolase; cytidine monophosphate-N-acetylneuraminic acid hydrolase; CMP-N-acetylneuraminate hydrolase |
Systematic name: |
CMP-N-acylneuraminate N-acylneuraminohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 55326-41-5 |
References: |
1. |
Kean, E.L. and Bighouse, K.J. Cytidine 5′-monophosphosialic acid hydrolase. Subcellular location and properties. J. Biol. Chem. 249 (1974) 7813–7823. [PMID: 4372219] |
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[EC 3.1.4.40 created 1976] |
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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] |
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[EC 3.1.4.41 created 1978] |
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EC |
3.1.4.42 |
Accepted name: |
glycerol-1,2-cyclic-phosphate 2-phosphodiesterase |
Reaction: |
glycerol 1,2-cyclic phosphate + H2O = glycerol 1-phosphate |
Other name(s): |
rac-glycerol 1:2-cyclic phosphate 2-phosphodiesterase |
Systematic name: |
rac-glycerol-1,2-cyclic-phosphate 2-glycerophosphohydrolase |
Comments: |
Acts on both stereoisomers of the substrate and also, more slowly, on 3′,5′-cyclic AMP and on 2′,3′-cyclic AMP. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 69458-89-5 |
References: |
1. |
Clarke, N. and Dawson, R.M.C. rac-Glycerol 1:2-cyclic phosphate 2-phosphodiesterase, a new soluble phosphodiesterase of mammalian tissues. Biochem. J. 173 (1978) 579–589. [PMID: 212014] |
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[EC 3.1.4.42 created 1984] |
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EC |
3.1.4.43 |
Accepted name: |
glycerophosphoinositol inositolphosphodiesterase |
Reaction: |
1-(sn-glycero-3-phospho)-1D-myo-inositol + H2O = glycerol + 1D-myo-inositol 1-phosphate |
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For diagram of 1-(glycero-3-phospho)-myo-inositol catabolism, click here |
Other name(s): |
1,2-cyclic-inositol-phosphate phosphodiesterase; D-myo-inositol 1:2-cyclic phosphate 2-phosphohydrolase; D-inositol 1,2-cyclic phosphate 2-phosphohydrolase; D-myo-inositol 1,2-cyclic phosphate 2-phosphohydrolase; 1-D-myo-inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase; inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase |
Systematic name: |
1-(sn-glycero-3-phospho)-1D-myo-inositol inositolphosphohydrolase |
Comments: |
This enzyme also hydrolyses Ins(cyclic1,2)P to Ins-1-P |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9076-91-9 (from EC 3.1.4.36), 72414-13-2 (not distinguished from EC 3.1.4.44) |
References: |
1. |
Dawson, R.M.C. and Hemington, N. A phosphodiesterase in rat kidney cortex that hydrolyses glycerylphosphorylinositol. Biochem. J. 162 (1977) 241–245. [PMID: 192216] |
2. |
Dawson, R.M.C. and Clarke, N.G. D-myoInositol 1:2-cyclic phosphate 2-phosphohydrolase. Biochem. J. 127 (1972) 113–118. [PMID: 4342209] |
3. |
Dawson, R.M.C. and Clarke, N.G. A comparison of D-inositol 1:2-cyclic phosphate 2-phosphohydrolase with other phosphodiesterases of kidney. Biochem. J. 134 (1973) 59–67. [PMID: 4353088] |
4. |
Ross, T.S. and Majerus, P.W. Inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase. Substrate specificity and regulation of activity by phospholipids, metal ion chelators, and inositol 2-phosphate. J. Biol. Chem. 266 (1991) 851–856. [PMID: 1845995] |
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[EC 3.1.4.43 created 1984, (EC 3.1.4.36 created 1976, incorporated 2002), modified 2002] |
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EC |
3.1.4.44 |
Accepted name: |
glycerophosphoinositol glycerophosphodiesterase |
Reaction: |
1-(sn-glycero-3-phospho)-1D-myo-inositol + H2O = myo-inositol + sn-glycerol 3-phosphate |
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For diagram of 1-(glycero-3-phospho)-myo-inositol catabolism, click here |
Other name(s): |
sn-glycero(3)phosphoinositol glycerophosphohydrolase; sn-glycero-3-phospho-1-inositol glycerophosphohydrolase |
Systematic name: |
1-(sn-glycero-3-phospho)-1D-myo-inositol glycerophosphohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 72414-13-2 (not distinguished from EC 3.1.4.43) |
References: |
1. |
Dawson, R.M.C., Hemington, N., Richards, D.E. and Irvine, R.F. sn-Glycero(3)phosphoinositol glycerophosphohydrolase. A new phosphodiesterase in rat tissues. Biochem. J. 182 (1979) 39–49. [PMID: 40550] |
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[EC 3.1.4.44 created 1984, modified 2002] |
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EC |
3.1.4.45 |
Accepted name: |
N-acetylglucosamine-1-phosphodiester α-N-acetylglucosaminidase |
Reaction: |
glycoprotein N-acetyl-D-glucosaminyl-phospho-D-mannose + H2O = N-acetyl-D-glucosamine + glycoprotein phospho-D-mannose |
Other name(s): |
α-N-acetylglucosaminyl phosphodiesterase; lysosomal α-N-acetylglucosaminidase; phosphodiester glycosidase; α-N-acetyl-D-glucosamine-1-phosphodiester N-acetylglucosaminidase; 2-acetamido-2-deoxy-α-D-glucose 1-phosphodiester acetamidodeoxyglucohydrolase |
Systematic name: |
glycoprotein-N-acetyl-D-glucosaminyl-phospho-D-mannose N-acetyl-D-glucosaminylphosphohydrolase |
Comments: |
Acts on a variety of compounds in which N-acetyl-D-glucosamine is α-linked to a phosphate group, including the biosynthetic intermediates of the high mannose oligosaccharide components of some lysosomal enzymes and the products of EC 2.7.8.17 UDP-N-acetylglucosamine—lysosomal-enzyme N-acetylglucosaminephosphotransferase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 75788-84-0 |
References: |
1. |
Van den Tweel, W.J.J., Smits, J.P., Ogg, R.L.H.P. and de Bont, J.A.M. The involvement of an enantioselective transaminase in the metabolism of D-3- and D-4-hydroxyphenylglycine in Pseudomonas putida. Appl. Microbiol. Biotechnol. 29 (1988) 224–230. |
2. |
van der Drift, C., van Helvoort, P.E. and Vogels, G.D. S-Ureidoglycolate dehydrogenase: purification and properties. Arch. Biochem. Biophys. 145 (1971) 465–469. [DOI] [PMID: 4399430] |
3. |
van der Drift, L., Vogels, G.D. and van der Drift, C. Allantoin racemase: a new enzyme from Pseudomonas species. Biochim. Biophys. Acta 391 (1975) 240–248. [DOI] [PMID: 237557] |
4. |
Waheed, A., Hasilik, A. and von Figura, K. Processing of the phosphorylated recognition marker in lysosomal enzymes. Characterization and partial purification of a microsomal α-N-acetylglucosaminyl phosphodiesterase. J. Biol. Chem. 256 (1981) 5717–5721. [PMID: 6263889] |
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[EC 3.1.4.45 created 1984] |
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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] |
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[EC 3.1.4.46 created 1986] |
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EC
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3.1.4.47
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Transferred entry: | variant-surface-glycoprotein phospholipase C. Now EC 4.6.1.14, glycosylphosphatidylinositol diacylglycerol-lyase
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[EC 3.1.4.47 created 1989, deleted 2002] |
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EC |
3.1.4.48 |
Accepted name: |
dolichylphosphate-glucose phosphodiesterase |
Reaction: |
dolichyl β-D-glucosyl phosphate + H2O = dolichyl phosphate + D-glucose |
Other name(s): |
dolichol phosphoglucose phosphodiesterase; Dol-P-Glc phosphodiesterase |
Systematic name: |
dolichyl-β-D-glucosyl-phosphate dolichylphosphohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 89287-42-3 |
References: |
1. |
Crean, E.V. Synthesis and degradation of dolichyl phosphoryl glucose by the cellular slime mold, Dictyostelium discoideum. Biochim. Biophys. Acta 792 (1984) 149–157. |
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[EC 3.1.4.48 created 1989] |
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EC |
3.1.4.49 |
Accepted name: |
dolichylphosphate-mannose phosphodiesterase |
Reaction: |
dolichyl β-D-mannosyl phosphate + H2O = dolichyl phosphate + D-mannose |
Other name(s): |
mannosylphosphodolichol phosphodiesterase |
Systematic name: |
dolichyl-β-D-mannosyl-phosphate dolichylphosphohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 111839-07-7 |
References: |
1. |
Tomita, Y. and Motokawa, Y. Characterization and partial purification of a novel mannosylphosphodolichol phosphodiesterase from chicken liver microsomes. Eur. J. Biochem. 170 (1987) 363–368. [PMID: 2826159] |
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[EC 3.1.4.49 created 1990] |
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EC |
3.1.4.50 |
Accepted name: |
glycosylphosphatidylinositol phospholipase D |
Reaction: |
6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = 6-(α-D-glucosaminyl)-1D-myo-inositol + 3-sn-phosphatidate |
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For diagram of glycosylphosphatidyl-myo-inositol biosynthesis, click here |
Other name(s): |
GPI-PLD; glycoprotein phospholipase D; phosphatidylinositol phospholipase D; phosphatidylinositol-specific phospholipase D |
Systematic name: |
glycoprotein-phosphatidylinositol phosphatidohydrolase |
Comments: |
This enzyme is also active when O-4 of the glucosamine is substituted by carrying the oligosaccharide that can link a protein to the structure. It therefore cleaves proteins from the lipid part of the glycosylphosphatidylinositol (GPI) anchors, but does so by hydrolysis, whereas glycosylphosphatidylinositol diacylglycerol-lyase (EC 4.6.1.14) does so by elimination. It acts on plasma membranes only after solubilization of the substrate with detergents or solvents, but it may act on intracellular membranes. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 113756-14-2 |
References: |
1. |
Low, M.G. and Prasad, A.R.S. A phospholipase D specific for the phosphatidylinositol anchor of cell-surface proteins is abundant in plasma. Proc. Natl. Acad. Sci. USA 85 (1988) 980–984. [DOI] [PMID: 3422494] |
2. |
Malik, A.-S. and Low, M.G. Conversion of human placental alkaline phosphatase from a high Mr form to a low Mr form during butanol extraction. An investigation of the role of endogenous phosphoinositide-specific phospholipases. Biochem. J. 240 (1986) 519–527. [PMID: 3028377] |
3. |
Li, J.Y., Hollfelder, K., Huang, K.S. and Low, M.G. Structural features of GPI-specific phospholipase D revealed by fragmentation and Ca2+ binding studies. J. Biol. Chem. 269 (1994) 28963–28971. [PMID: 7961859] |
4. |
Deeg, M.A, Vierman, E.L. and Cheung, M.C. GPI-specific phospholipase D associates with an apoA-I- and apoA-IV-containing complex. J. Lipid Res. 42 (2001) 442–451. [PMID: 11254757] |
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[EC 3.1.4.50 created 1990, modified 2002] |
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