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] |
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[EC 3.1.1.8 created 1961] |
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EC |
3.1.1.80 |
Accepted name: |
acetylajmaline esterase |
Reaction: |
(1) 17-O-acetylajmaline + H2O = ajmaline + acetate (2) 17-O-acetylnorajmaline + H2O = norajmaline + acetate |
|
For diagram of ajmaline, vinorine, vomilenine and raucaffricine biosynthesis, click here |
Other name(s): |
AAE; 2β(R)-17-O-acetylajmalan:acetylesterase; acetylajmalan esterase |
Systematic name: |
17-O-acetylajmaline O-acetylhydrolase |
Comments: |
This plant enzyme is responsible for the last stages in the biosynthesis of the indole alkaloid ajmaline. The enzyme is highly specific for the substrates 17-O-acetylajmaline and 17-O-acetylnorajmaline as the structurally related acetylated alkaloids vinorine, vomilenine, 1,2-dihydrovomilenine and 1,2-dihydroraucaffricine cannot act as substrates [2]. This is a novel member of the GDSL family of serine esterases/lipases. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 110183-46-5 |
References: |
1. |
Polz, L., Schübel, H. and Stöckigt, J. Characterization of 2β(R)-17-O-acetylajmalan:acetylesterase—a
specific enzyme involved in the biosynthesis of the Rauwolfia alkaloid
ajmaline. Z. Naturforsch. [C] 42 (1987) 333–342. [PMID: 2955586] |
2. |
Ruppert, M., Woll, J., Giritch, A., Genady, E., Ma, X. and Stöckigt, J. Functional expression of an ajmaline pathway-specific esterase from
Rauvolfia in a novel plant-virus expression system. Planta 222 (2005) 888–898. [DOI] [PMID: 16133216] |
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[EC 3.1.1.80 created 2006] |
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EC |
3.1.1.81 |
Accepted name: |
quorum-quenching N-acyl-homoserine lactonase |
Reaction: |
an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine |
Other name(s): |
acyl homoserine degrading enzyme; acyl-homoserine lactone acylase; AHL lactonase; AHL-degrading enzyme; AHL-inactivating enzyme; AHLase; AhlD; AhlK; AiiA; AiiA lactonase; AiiA-like protein; AiiB; AiiC; AttM; delactonase; lactonase-like enzyme; N-acyl homoserine lactonase; N-acyl homoserine lactone hydrolase; N-acyl-homoserine lactone lactonase; N-acyl-L-homoserine lactone hydrolase; quorum-quenching lactonase; quorum-quenching N-acyl homoserine lactone hydrolase |
Systematic name: |
N-acyl-L-homoserine-lactone lactonohydrolase |
Comments: |
Acyl-homoserine lactones (AHLs) are produced by a number of bacterial species and are used by them to regulate the expression of virulence genes in a process known as quorum-sensing. Each bacterial cell has a basal level of AHL and, once the population density reaches a critical level, it triggers AHL-signalling which, in turn, initiates the expression of particular virulence genes [5]. Plants or animals capable of degrading AHLs would have a therapeutic advantage in avoiding bacterial infection as they could prevent AHL-signalling and the expression of virulence genes in quorum-sensing bacteria [5]. N-(3-Oxohexanoyl)-L-homoserine lactone, N-(3-oxododecanoyl)-L-homoserine lactone, N-butanoyl-L-homoserine lactone and N-(3-oxooctanoyl)-L-homoserine lactone can act as substrates [5]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 389867-43-0 |
References: |
1. |
Thomas, P.W., Stone, E.M., Costello, A.L., Tierney, D.L. and Fast, W. The quorum-quenching lactonase from Bacillus thuringiensis is a metalloprotein. Biochemistry 44 (2005) 7559–7569. [DOI] [PMID: 15895999] |
2. |
Dong, Y.H., Gusti, A.R., Zhang, Q., Xu, J.L. and Zhang, L.H. Identification of quorum-quenching N-acyl homoserine lactonases from Bacillus species. Appl. Environ. Microbiol. 68 (2002) 1754–1759. [DOI] [PMID: 11916693] |
3. |
Wang, L.H., Weng, L.X., Dong, Y.H. and Zhang, L.H. Specificity and enzyme kinetics of the quorum-quenching N-acyl homoserine lactone lactonase (AHL-lactonase). J. Biol. Chem. 279 (2004) 13645–13651. [DOI] [PMID: 14734559] |
4. |
Dong, Y.H., Xu, J.L., Li, X.Z. and Zhang, L.H. AiiA, an enzyme that inactivates the acylhomoserine lactone quorum-sensing signal and attenuates the virulence of Erwinia carotovora. Proc. Natl. Acad. Sci. USA 97 (2000) 3526–3531. [DOI] [PMID: 10716724] |
5. |
Dong, Y.H., Wang, L.H., Xu, J.L., Zhang, H.B., Zhang, X.F. and Zhang, L.H. Quenching quorum-sensing-dependent bacterial infection by an N-acyl homoserine lactonase. Nature 411 (2001) 813–817. [DOI] [PMID: 11459062] |
6. |
Lee, S.J., Park, S.Y., Lee, J.J., Yum, D.Y., Koo, B.T. and Lee, J.K. Genes encoding the N-acyl homoserine lactone-degrading enzyme are widespread in many subspecies of Bacillus thuringiensis. Appl. Environ. Microbiol. 68 (2002) 3919–3924. [DOI] [PMID: 12147491] |
7. |
Park, S.Y., Lee, S.J., Oh, T.K., Oh, J.W., Koo, B.T., Yum, D.Y. and Lee, J.K. AhlD, an N-acylhomoserine lactonase in Arthrobacter sp., and predicted homologues in other bacteria. Microbiology 149 (2003) 1541–1550. [DOI] [PMID: 12777494] |
8. |
Ulrich, R.L. Quorum quenching: enzymatic disruption of N-acylhomoserine lactone-mediated bacterial communication in Burkholderia thailandensis. Appl. Environ. Microbiol. 70 (2004) 6173–6180. [DOI] [PMID: 15466564] |
9. |
Kim, M.H., Choi, W.C., Kang, H.O., Lee, J.S., Kang, B.S., Kim, K.J., Derewenda, Z.S., Oh, T.K., Lee, C.H. and Lee, J.K. The molecular structure and catalytic mechanism of a quorum-quenching N-acyl-L-homoserine lactone hydrolase. Proc. Natl. Acad. Sci. USA 102 (2005) 17606–17611. [DOI] [PMID: 16314577] |
10. |
Liu, D., Lepore, B.W., Petsko, G.A., Thomas, P.W., Stone, E.M., Fast, W. and Ringe, D. Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis. Proc. Natl. Acad. Sci. USA 102 (2005) 11882–11887. [DOI] [PMID: 16087890] |
11. |
Yang, F., Wang, L.H., Wang, J., Dong, Y.H., Hu, J.Y. and Zhang, L.H. Quorum quenching enzyme activity is widely conserved in the sera of mammalian species. FEBS Lett. 579 (2005) 3713–3717. [DOI] [PMID: 15963993] |
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[EC 3.1.1.81 created 2007] |
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EC |
3.1.1.82 |
Accepted name: |
pheophorbidase |
Reaction: |
pheophorbide a + H2O = pyropheophorbide a + methanol + CO2 (overall reaction)
(1a) pheophorbide a + H2O = C-132-carboxypyropheophorbide a + methanol (1b) C-132-carboxypyropheophorbide a = pyropheophorbide a + CO2 (spontaneous) |
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For diagram of chlorophyll catabolism, click here |
Other name(s): |
phedase; PPD |
Systematic name: |
pheophorbide-a hydrolase |
Comments: |
This enzyme forms part of the chlorophyll degradation pathway, and is found in higher plants and in algae. In higher plants it participates in de-greening processes such as fruit ripening, leaf senescence, and flowering. The enzyme exists in two forms: type 1 is induced by senescence whereas type 2 is constitutively expressed [1,2]. The enzyme is highly specific for pheophorbide as substrate (with a preference for pheophorbide a over pheophorbide b) as other chlorophyll derivatives such as protochlorophyllide a, pheophytin a and c, chlorophyll a and b, and chlorophyllide a cannot act as substrates [2]. Another enzyme, called pheophorbide demethoxycarbonylase (PDC), produces pyropheophorbide a from pheophorbide a without forming an intermediate although the precise reaction is not yet known [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Suzuki, Y., Doi, M. and Shioi, Y. Two enzymatic reaction pathways in the formation of pyropheophorbide a. Photosynth. Res. 74 (2002) 225–233. [DOI] [PMID: 16228561] |
2. |
Suzuki, Y., Amano, T. and Shioi, Y. Characterization and cloning of the chlorophyll-degrading enzyme pheophorbidase from cotyledons of radish. Plant Physiol. 140 (2006) 716–725. [DOI] [PMID: 16384908] |
3. |
Hörtensteiner, S. Chlorophyll degradation during senescence. Annu. Rev. Plant Biol. 57 (2006) 55–77. [DOI] [PMID: 16669755] |
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[EC 3.1.1.82 created 2007] |
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EC |
3.1.1.83 |
Accepted name: |
monoterpene ε-lactone hydrolase |
Reaction: |
(1) isoprop(en)ylmethyloxepan-2-one + H2O = 6-hydroxyisoprop(en)ylmethylhexanoate (general reaction) (2) 4-isopropenyl-7-methyloxepan-2-one + H2O = 6-hydroxy-3-isopropenylheptanoate (3) 7-isopropyl-4-methyloxepan-2-one + H2O = 6-hydroxy-3,7-dimethyloctanoate |
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For diagram of (–)-carvone catabolism, click here and for diagram of menthol biosynthesis, click here |
Other name(s): |
MLH |
Systematic name: |
isoprop(en)ylmethyloxepan-2-one lactonohydrolase |
Comments: |
The enzyme catalyses the ring opening of ε-lactones which are formed during degradation of dihydrocarveol by the Gram-positive bacterium Rhodococcus erythropolis DCL14. The enzyme also acts on ethyl caproate, indicating that it is an esterase with a preference for lactones (internal cyclic esters). The enzyme is not stereoselective. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
van der Vlugt-Bergmans , C.J. and van der Werf , M.J. Genetic and biochemical characterization of a novel monoterpene ε-lactone hydrolase from Rhodococcus erythropolis DCL14. Appl. Environ. Microbiol. 67 (2001) 733–741. [DOI] [PMID: 11157238] |
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[EC 3.1.1.83 created 2008] |
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EC |
3.1.1.84 |
Accepted name: |
cocaine esterase |
Reaction: |
cocaine + H2O = ecgonine methyl ester + benzoate |
Glossary: |
ecgonine methyl ester = 2β-carbomethoxy-3β-tropine = methyl (1R,2R,3S,5S)-3-hydroxy-8-methyl-8-azabicyclo[3.2.1]octane-2-carboxylate |
Other name(s): |
CocE; hCE2; hCE-2; human carboxylesterase 2 |
Systematic name: |
cocaine benzoylhydrolase |
Comments: |
Rhodococcus sp. strain MB1 and Pseudomonas maltophilia strain MB11L can utilize cocaine as sole source of carbon and energy [2,3]. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Gao, D., Narasimhan, D.L., Macdonald, J., Brim, R., Ko, M.C., Landry, D.W., Woods, J.H., Sunahara, R.K. and Zhan, C.G. Thermostable variants of cocaine esterase for long-time protection against cocaine toxicity. Mol. Pharmacol. 75 (2009) 318–323. [DOI] [PMID: 18987161] |
2. |
Bresler, M.M., Rosser, S.J., Basran, A. and Bruce, N.C. Gene cloning and nucleotide sequencing and properties of a cocaine esterase from Rhodococcus sp. strain MB1. Appl. Environ. Microbiol. 66 (2000) 904–908. [DOI] [PMID: 10698749] |
3. |
Britt, A.J., Bruce, N.C. and Lowe, C.R. Identification of a cocaine esterase in a strain of Pseudomonas maltophilia. J. Bacteriol. 174 (1992) 2087–2094. [DOI] [PMID: 1551831] |
4. |
Larsen, N.A., Turner, J.M., Stevens, J., Rosser, S.J., Basran, A., Lerner, R.A., Bruce, N.C. and Wilson, I.A. Crystal structure of a bacterial cocaine esterase. Nat. Struct. Biol. 9 (2002) 17–21. [DOI] [PMID: 11742345] |
5. |
Pindel, E.V., Kedishvili, N.Y., Abraham, T.L., Brzezinski, M.R., Zhang, J., Dean, R.A. and Bosron, W.F. Purification and cloning of a broad substrate specificity human liver carboxylesterase that catalyzes the hydrolysis of cocaine and heroin. J. Biol. Chem. 272 (1997) 14769–14775. [DOI] [PMID: 9169443] |
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[EC 3.1.1.84 created 2010] |
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EC |
3.1.1.85 |
Accepted name: |
pimelyl-[acyl-carrier protein] methyl ester esterase |
Reaction: |
pimeloyl-[acyl-carrier protein] methyl ester + H2O = pimeloyl-[acyl-carrier protein] + methanol |
Other name(s): |
BioH |
Systematic name: |
pimeloyl-[acyl-carrier protein] methyl ester hydrolase |
Comments: |
Involved in biotin biosynthesis in Gram-negative bacteria. The enzyme exhibits carboxylesterase activity, particularly toward substrates with short acyl chains [1,2]. Even though the enzyme can interact with coenzyme A thioesters [3], the in vivo role of the enzyme is to hydrolyse the methyl ester of pimeloyl-[acyl carrier protein], terminating the part of the biotin biosynthesis pathway that is catalysed by the fatty acid elongation enzymes [4]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Sanishvili, R., Yakunin, A.F., Laskowski, R.A., Skarina, T., Evdokimova, E., Doherty-Kirby, A., Lajoie, G.A., Thornton, J.M., Arrowsmith, C.H., Savchenko, A., Joachimiak, A. and Edwards, A.M. Integrating structure, bioinformatics, and enzymology to discover function: BioH, a new carboxylesterase from Escherichia coli. J. Biol. Chem. 278 (2003) 26039–26045. [DOI] [PMID: 12732651] |
2. |
Lemoine, Y., Wach, A. and Jeltsch, J.M. To be free or not: the fate of pimelate in Bacillus sphaericus and in Escherichia coli. Mol. Microbiol. 19 (1996) 645–647. [DOI] [PMID: 8830257] |
3. |
Tomczyk, N.H., Nettleship, J.E., Baxter, R.L., Crichton, H.J., Webster, S.P. and Campopiano, D.J. Purification and characterisation of the BIOH protein from the biotin biosynthetic pathway. FEBS Lett. 513 (2002) 299–304. [DOI] [PMID: 11904168] |
4. |
Lin, S., Hanson, R.E. and Cronan, J.E. Biotin synthesis begins by hijacking the fatty acid synthetic pathway. Nat. Chem. Biol. 6 (2010) 682–688. [DOI] [PMID: 20693992] |
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[EC 3.1.1.85 created 2011] |
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EC |
3.1.1.86 |
Accepted name: |
rhamnogalacturonan acetylesterase |
Reaction: |
Hydrolytic cleavage of 2-O-acetyl- or 3-O-acetyl groups of α-D-galacturonic acid in rhamnogalacturonan I. |
Other name(s): |
RGAE |
Systematic name: |
rhamnogalacturonan 2/3-O-acetyl-α-D-galacturonate O-acetylhydrolase |
Comments: |
The degradation of rhamnogalacturonan by rhamnogalacturonases depends on the removal of the acetyl esters from the substrate [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Kauppinen, S., Christgau, S., Kofod, L.V., Halkier, T., Dorreich, K. and Dalboge, H. Molecular cloning and characterization of a rhamnogalacturonan acetylesterase from Aspergillus aculeatus. Synergism between rhamnogalacturonan degrading enzymes. J. Biol. Chem. 270 (1995) 27172–27178. [DOI] [PMID: 7592973] |
2. |
Molgaard, A., Kauppinen, S. and Larsen, S. Rhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases. Structure 8 (2000) 373–383. [PMID: 10801485] |
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[EC 3.1.1.86 created 2011] |
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EC |
3.1.1.87 |
Accepted name: |
fumonisin B1 esterase |
Reaction: |
fumonisin B1 + 2 H2O = aminopentol + 2 propane-1,2,3-tricarboxylate |
Glossary: |
fumonisin B1 = (2R,2′R)-2,2′-{[(5R,6R,7S,9S,11R,16R,18S,19S)-19-amino-11,16,18-trihydroxy-5,9-dimethylicosane-6,7-diyl]bis[oxy(2-oxoethane-2,1-diyl)]}dibutanedioic acid
aminopentol = (2S,3S,5R,10R,12S,14S,15R,16R)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol |
Other name(s): |
fumD (gene name) |
Systematic name: |
fumonisin B1 acylhydrolase |
Comments: |
The enzyme is involved in degradation of fumonisin B1 [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Heinl, S., Hartinger, D., Thamhesl, M., Vekiru, E., Krska, R., Schatzmayr, G., Moll, W.D. and Grabherr, R. Degradation of fumonisin B1 by the consecutive action of two bacterial enzymes. J. Biotechnol. 145 (2010) 120–129. [DOI] [PMID: 19922747] |
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[EC 3.1.1.87 created 2011] |
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EC |
3.1.1.88 |
Accepted name: |
pyrethroid hydrolase |
Reaction: |
trans-permethrin + H2O = (3-phenoxyphenyl)methanol + (1S,3R)-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate |
Other name(s): |
pyrethroid-hydrolyzing carboxylesterase; pyrethroid-hydrolysing esterase; pyrethroid-hydrolyzing esterase; pyrethroid-selective esterase; pyrethroid-cleaving enzyme; permethrinase; PytH; EstP |
Systematic name: |
pyrethroid-ester hydrolase |
Comments: |
The enzyme is involved in degradation of pyrethroid pesticides. The enzymes from Sphingobium sp., Klebsiella sp. and Aspergillus niger hydrolyse cis-permethrin at approximately equal rate to trans-permethrin [1-3]. The enzyme from mouse hydrolyses trans-permethrin at a rate about 22-fold higher than cis-permethrin [4]. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc |
References: |
1. |
Wang, B.Z., Guo, P., Hang, B.J., Li, L., He, J. and Li, S.P. Cloning of a novel pyrethroid-hydrolyzing carboxylesterase gene from Sphingobium sp. strain JZ-1 and characterization of the gene product. Appl. Environ. Microbiol. 75 (2009) 5496–5500. [DOI] [PMID: 19581484] |
2. |
Wu, P.C., Liu, Y.H., Wang, Z.Y., Zhang, X.Y., Li, H., Liang, W.Q., Luo, N., Hu, J.M., Lu, J.Q., Luan, T.G. and Cao, L.X. Molecular cloning, purification, and biochemical characterization of a novel pyrethroid-hydrolyzing esterase from Klebsiella sp. strain ZD112. J. Agric. Food Chem. 54 (2006) 836–842. [DOI] [PMID: 16448191] |
3. |
Liang, W.Q., Wang, Z.Y., Li, H., Wu, P.C., Hu, J.M., Luo, N., Cao, L.X. and Liu, Y.H. Purification and characterization of a novel pyrethroid hydrolase from Aspergillus niger ZD11. J. Agric. Food Chem. 53 (2005) 7415–7420. [DOI] [PMID: 16159167] |
4. |
Stok, J.E., Huang, H., Jones, P.D., Wheelock, C.E., Morisseau, C. and Hammock, B.D. Identification, expression, and purification of a pyrethroid-hydrolyzing carboxylesterase from mouse liver microsomes. J. Biol. Chem. 279 (2004) 29863–29869. [DOI] [PMID: 15123619] |
5. |
Maloney, S.E., Maule, A. and Smith, A.R. Purification and preliminary characterization of permethrinase from a pyrethroid-transforming strain of Bacillus cereus. Appl. Environ. Microbiol. 59 (1993) 2007–2013. [PMID: 8357241] |
6. |
Guo, P., Wang, B., Hang, B., Li, L., Ali, W., He, J. and Li, S. Pyrethroid-degrading Sphingobium sp. JZ-2 and the purification and characterization of a novel pyrethroid hydrolase. Int. Biodeter. Biodegrad. 63 (2009) 1107–1112. |
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[EC 3.1.1.88 created 2011] |
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EC |
3.1.1.89 |
Accepted name: |
protein phosphatase methylesterase-1 |
Reaction: |
[phosphatase 2A protein]-leucine methyl ester + H2O = [phosphatase 2A protein]-leucine + methanol |
Other name(s): |
PME-1; PPME1 |
Systematic name: |
[phosphatase 2A protein]-leucine ester acylhydrolase |
Comments: |
A key regulator of protein phosphatase 2A. The methyl ester is formed by EC 2.1.1.233 (leucine carboxy methyltransferase-1). Occurs mainly in the nucleus. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Ogris, E., Du, X., Nelson, K.C., Mak, E.K., Yu, X.X., Lane, W.S. and Pallas, D.C. A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A. J. Biol. Chem. 274 (1999) 14382–14391. [DOI] [PMID: 10318862] |
2. |
Xing, Y., Li, Z., Chen, Y., Stock, J.B., Jeffrey, P.D. and Shi, Y. Structural mechanism of demethylation and inactivation of protein phosphatase 2A. Cell 133 (2008) 154–163. [DOI] [PMID: 18394995] |
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[EC 3.1.1.89 created 2011] |
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