The Enzyme Database

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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. (Eds), The Enzymes, 2nd edn, vol. 5, Academic Press, New York, 1961, pp. 79–94.
[EC 3.1.4.1 created 1961]
 
 
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, 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 3.1.4.5      
Transferred entry: deoxyribonuclease. Now EC 3.1.21.1, deoxyribonuclease I
[EC 3.1.4.5 created 1961, deleted 1978]
 
 
EC 3.1.4.6      
Transferred entry: deoxyribonuclease II. Now EC 3.1.22.1, deoxyribonuclease II
[EC 3.1.4.6 created 1961, deleted 1978]
 
 
EC 3.1.4.7      
Transferred entry: micrococcal nuclease. Now EC 3.1.31.1, micrococcal nuclease
[EC 3.1.4.7 created 1961, deleted 1978]
 
 
EC 3.1.4.8      
Transferred entry: Aspergillus oryzae ribonuclease. Now EC 3.1.27.3, ribonuclease T1
[EC 3.1.4.8 created 1961, transferred 1965 to EC 2.7.7.26, reinstated 1972, deleted 1978]
 
 
EC 3.1.4.9      
Transferred entry: nucleate endonuclease. Now EC 3.1.30.2, Serratia marcescens nuclease
[EC 3.1.4.9 created 1965, deleted 1978]
 
 
EC 3.1.4.10      
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
[EC 3.1.4.10 created 1972, modified 1976, deleted 2002]
 
 
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
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]
[EC 3.1.4.11 created 1972, modified 2002]
 
 
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 3.1.4.13     
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]
[EC 3.1.4.13 created 1972, modified 1976]
 
 
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 prosthetic-group 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, 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. [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. [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]
[EC 3.1.4.14 created 1972, modified 2006]
 
 
EC 3.1.4.15      
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
[EC 3.1.4.15 created 1972, deleted 2015]
 
 
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 3.1.27.3 (ribonuclease T1) and EC 3.1.27.5 (pancreatic ribonuclease).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, 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]
[EC 3.1.4.16 created 1972, modified 1976]
 
 
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]
[EC 3.1.4.17 created 1972, modified 1976]
 
 
EC 3.1.4.18      
Transferred entry: phosphodiesterase II. Now EC 3.1.16.1, spleen exonuclease
[EC 3.1.4.18 created 1972, deleted 1978]
 
 
EC 3.1.4.19      
Transferred entry: oligonucleotidase. Now EC 3.1.13.3, oligonucleotidase
[EC 3.1.4.19 created 1972, deleted 1978]
 
 
EC 3.1.4.20      
Transferred entry: exoribonuclease. Now EC 3.1.13.1, exoribonuclease II
[EC 3.1.4.20 created 1972, deleted 1978]
 
 
EC 3.1.4.21      
Transferred entry: single-stranded-nucleate endonuclease. Now EC 3.1.30.1, Aspergillus nuclease S1
[EC 3.1.4.21 created 1972, deleted 1978]
 
 
EC 3.1.4.22      
Transferred entry: ribonuclease I. Now EC 3.1.27.5, pancreatic ribonuclease
[EC 3.1.4.22 created 1972, deleted 1978]
 
 
EC 3.1.4.23      
Transferred entry: ribonuclease II. Now EC 3.1.27.1, ribonuclease T2
[EC 3.1.4.23 created 1972, deleted 1978]
 
 
EC 3.1.4.24      
Deleted entry:  endoribonuclease III
[EC 3.1.4.24 created 1972, deleted 1978]
 
 
EC 3.1.4.25      
Transferred entry: exodeoxyribonuclease I. Now EC 3.1.11.1, exodeoxyribonuclease I
[EC 3.1.4.25 created 1972, deleted 1978]
 
 
EC 3.1.4.26      
Deleted entry:  exodeoxyribonuclease II
[EC 3.1.4.26 created 1972, deleted 1978]
 
 
EC 3.1.4.27      
Transferred entry: exodeoxyribonuclease III. Now EC 3.1.11.2, exodeoxyribonuclease III
[EC 3.1.4.27 created 1972, deleted 1978]
 
 
EC 3.1.4.28      
Transferred entry: exodeoxyribonuclease IV. Now EC 3.1.11.3, exodeoxyribonuclease (lambda-induced)
[EC 3.1.4.28 created 1972, deleted 1978]
 
 
EC 3.1.4.29      
Deleted entry:  oligodeoxyribonucleate exonuclease
[EC 3.1.4.29 created 1972, deleted 1978]
 
 
EC 3.1.4.30      
Transferred entry: endodeoxyribonuclease. Now EC 3.1.21.2, deoxyribonuclease IV (phage-T4-induced)
[EC 3.1.4.30 created 1972, deleted 1978]
 
 
EC 3.1.4.31      
Transferred entry: DNA 5′-dinucleotidohydrolase. Now EC 3.1.11.4, exodeoxyribonuclease (phage SP3-induced)
[EC 3.1.4.31 created 1972, deleted 1978]
 
 
EC 3.1.4.32      
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]
 
 
EC 3.1.4.33      
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]
 
 
EC 3.1.4.34      
Deleted entry:  hybrid nuclease. See 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]
 
 
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.
[EC 3.1.4.35 created 1976]
 
 
EC 3.1.4.36      
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]
 
 
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]
[EC 3.1.4.37 created 1976]
 
 
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, 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, 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 3.1.4.40     
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]
[EC 3.1.4.40 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 3.1.4.42     
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]
[EC 3.1.4.42 created 1984]
 
 
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
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]
[EC 3.1.4.43 created 1984, (EC 3.1.4.36 created 1976, incorporated 2002), modified 2002]
 
 
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
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]
[EC 3.1.4.44 created 1984, modified 2002]
 
 
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]
[EC 3.1.4.45 created 1984]
 
 
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 3.1.4.47      
Transferred entry: variant-surface-glycoprotein phospholipase C. Now EC 4.6.1.14, glycosylphosphatidylinositol diacylglycerol-lyase
[EC 3.1.4.47 created 1989, deleted 2002]
 
 
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.
[EC 3.1.4.48 created 1989]
 
 
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]
[EC 3.1.4.49 created 1990]
 
 
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
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]
[EC 3.1.4.50 created 1990, modified 2002]
 
 


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