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Volumn 139, Issue 1, 2006, Pages 1-9

Aminopropyltransferases: Function, structure and genetics

Author keywords

Aminopropyltransferase; Polyamines; S adenosylmethionine; Spermidine; Spermine; Thermophiles

Indexed keywords

AMINOPROPYLTRANSFERASE INHIBITOR; ENZYME INHIBITOR; SPERMIDINE SYNTHASE; SPERMINE SYNTHASE; UNCLASSIFIED DRUG;

EID: 32944472945     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvj019     Document Type: Short Survey
Times cited : (111)

References (48)
  • 1
    • 2342631335 scopus 로고    scopus 로고
    • S-adenosylmethionine: Nothing goes to waste
    • Fontecave, M., Atta, M., and Muillez, E. (2004) S-adenosylmethionine: nothing goes to waste. Trends Biochem. Sci. 29, 243-249
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 243-249
    • Fontecave, M.1    Atta, M.2    Muillez, E.3
  • 2
    • 0022450919 scopus 로고
    • Recent advances in the biochemistry of polyamines in eukaryotes
    • Pegg, A.E. (1986) Recent advances in the biochemistry of polyamines in eukaryotes. Biochem. J. 234, 249-262
    • (1986) Biochem. J. , vol.234 , pp. 249-262
    • Pegg, A.E.1
  • 3
    • 0029024723 scopus 로고
    • Use of aminopropyltransferase inhibitors and of non-metabolizable analogues to study polyamine regulation and function
    • Pegg, A.E., Poulin, R., and Coward, J.K. (1995) Use of aminopropyltransferase inhibitors and of non-metabolizable analogues to study polyamine regulation and function. Int. J. Biochem. 27, 425-442
    • (1995) Int. J. Biochem. , vol.27 , pp. 425-442
    • Pegg, A.E.1    Poulin, R.2    Coward, J.K.3
  • 5
    • 0037364742 scopus 로고    scopus 로고
    • Structure and expression of spermidine synthase genes in apple: Two cDNAs are spatially and developmentally regulated through alternative splicing
    • Zhang, Z., Honda, C., Kita, M., Hu, C., Nakayama, M., and Moriguchi, T. (2003) Structure and expression of spermidine synthase genes in apple: two cDNAs are spatially and developmentally regulated through alternative splicing. Mol. Genet. Genomics 268, 799-807
    • (2003) Mol. Genet. Genomics , vol.268 , pp. 799-807
    • Zhang, Z.1    Honda, C.2    Kita, M.3    Hu, C.4    Nakayama, M.5    Moriguchi, T.6
  • 7
    • 0037063317 scopus 로고    scopus 로고
    • Characterization of the spermidine synthase-related gene family in Arabidopsis thaliana
    • Hanzawa, Y., Imai, A., Michael, A.J., Komeda, Y., and Takahashi, T. (2002) Characterization of the spermidine synthase-related gene family in Arabidopsis thaliana. FEBS Lett. 527, 176-180
    • (2002) FEBS Lett. , vol.527 , pp. 176-180
    • Hanzawa, Y.1    Imai, A.2    Michael, A.J.3    Komeda, Y.4    Takahashi, T.5
  • 8
    • 32944464990 scopus 로고    scopus 로고
    • Cloning and characterization of spermidine synthase and its implication in polyamine biosynthesis in Helicobacter pylori strain 26695
    • Lee, M.J., Huang, C.Y., Sun, Y.J., and Huang, H. (2005) Cloning and characterization of spermidine synthase and its implication in polyamine biosynthesis in Helicobacter pylori strain 26695. Protein Expr. Purif. 43, 140-148
    • (2005) Protein Expr. Purif. , vol.43 , pp. 140-148
    • Lee, M.J.1    Huang, C.Y.2    Sun, Y.J.3    Huang, H.4
  • 9
    • 20644442880 scopus 로고    scopus 로고
    • The spermidine synthase of the malaria parasite Plasmodium falciparum: Molecular and biochemical characterisation of the polyamine synthesis enzyme
    • Haider, N., Eschbach, M.L., Dias Sde, S., Gilberger, T.W., Walter, R.D., and Luersen, K. (2005) The spermidine synthase of the malaria parasite Plasmodium falciparum: molecular and biochemical characterisation of the polyamine synthesis enzyme. Mol. Biochem. Parasitol. 142, 224-236
    • (2005) Mol. Biochem. Parasitol. , vol.142 , pp. 224-236
    • Haider, N.1    Eschbach, M.L.2    Dias Sde, S.3    Gilberger, T.W.4    Walter, R.D.5    Luersen, K.6
  • 12
    • 0035234344 scopus 로고    scopus 로고
    • Polyamines of the thermophilic eubacteria belonging to the genera Thermosipho, Thermabacter and Caldicellulosiruptor
    • Hamana, K., Niitsu, M., Samejima, K., and Itoh, T. (2001) Polyamines of the thermophilic eubacteria belonging to the genera Thermosipho, Thermabacter and Caldicellulosiruptor. Microbios 104, 177-185
    • (2001) Microbios , vol.104 , pp. 177-185
    • Hamana, K.1    Niitsu, M.2    Samejima, K.3    Itoh, T.4
  • 13
    • 20544443981 scopus 로고    scopus 로고
    • Stabilization of nucleic acids by unusual polyamines produced by an extreme thermophile
    • Terui, Y., Ohnuma, M., Hiraga, K, Kawashima, E., and Oshima, T. (2005) Stabilization of nucleic acids by unusual polyamines produced by an extreme thermophile. Biochem. J. 388, 427-433
    • (2005) Biochem. J. , vol.388 , pp. 427-433
    • Terui, Y.1    Ohnuma, M.2    Hiraga, K.3    Kawashima, E.4    Oshima, T.5
  • 14
    • 0025977039 scopus 로고
    • Putrescine or spermidine binding site of aminopropyltransferases and competitive inhibitors
    • Shirahata, A., Morohohi, T., Fukai, M., Akatsu, F., and Samejima, K. (1991) Putrescine or spermidine binding site of aminopropyltransferases and competitive inhibitors. Biochem. Pharmacol. 41, 205-212
    • (1991) Biochem. Pharmacol. , vol.41 , pp. 205-212
    • Shirahata, A.1    Morohohi, T.2    Fukai, M.3    Akatsu, F.4    Samejima, K.5
  • 15
    • 16644368614 scopus 로고    scopus 로고
    • Mammalian spermidine synthase-identification of cysteine residues and investigation of the putrescine binding site
    • Goda, H., Watanabe, T., Takeda, N., Kobayashi, M., Wada, M., Hosoda, H., Shirahata, A., and Samejima, K. (2004) Mammalian spermidine synthase- identification of cysteine residues and investigation of the putrescine binding site. Biol. Pharm. Bull. 27, 1327-1332
    • (2004) Biol. Pharm. Bull. , vol.27 , pp. 1327-1332
    • Goda, H.1    Watanabe, T.2    Takeda, N.3    Kobayashi, M.4    Wada, M.5    Hosoda, H.6    Shirahata, A.7    Samejima, K.8
  • 16
    • 0025077338 scopus 로고
    • Aminooxy analogues of spermidine as inhibitors of spermine synthase and substrates of hepatic polyamine acetylating activity
    • Eloranta, T.O., Khomutov, A.R., Khomutov, R.M., and Hyvonen, T. (1990) Aminooxy analogues of spermidine as inhibitors of spermine synthase and substrates of hepatic polyamine acetylating activity. J. Biochem. 108, 593-598
    • (1990) J. Biochem. , vol.108 , pp. 593-598
    • Eloranta, T.O.1    Khomutov, A.R.2    Khomutov, R.M.3    Hyvonen, T.4
  • 17
    • 0023078471 scopus 로고
    • Specific multisubstrate adduct inhibitors of aminopropyltransferases and their effect on polyamine biosynthesis in cultured cells
    • Coward, J.K. and Pegg, A.E. (1987) Specific multisubstrate adduct inhibitors of aminopropyltransferases and their effect on polyamine biosynthesis in cultured cells. Adv. Enzyme Regul. 26, 107-113
    • (1987) Adv. Enzyme Regul. , vol.26 , pp. 107-113
    • Coward, J.K.1    Pegg, A.E.2
  • 18
    • 0027264131 scopus 로고
    • Effects of inhibitors of spermidine synthase and spermine synthase on polyamine synthesis in rat tissues
    • Shirahata, A., Takahashi, N., Beppu, T., Hosoda, H., and Samejima, K. (1993) Effects of inhibitors of spermidine synthase and spermine synthase on polyamine synthesis in rat tissues. Biochem. Pharmacol. 45, 1897-1903
    • (1993) Biochem. Pharmacol. , vol.45 , pp. 1897-1903
    • Shirahata, A.1    Takahashi, N.2    Beppu, T.3    Hosoda, H.4    Samejima, K.5
  • 19
    • 21144451823 scopus 로고    scopus 로고
    • Control of spermidine and spermine levels in rat tissues by trans-4-methylcyclohexylamine, a spermidine-synthase inhibitor
    • Kobayashi, M., Watanabe, T., Xu, Y.J., Tatemori, M., Goda, H., Niitsu, M., Shirahata, A., and Samejima, K. (2005) Control of spermidine and spermine levels in rat tissues by trans-4-methylcyclohexylamine, a spermidine-synthase inhibitor. Biol. Pharm. Bull. 28, 569-573
    • (2005) Biol. Pharm. Bull. , vol.28 , pp. 569-573
    • Kobayashi, M.1    Watanabe, T.2    Xu, Y.J.3    Tatemori, M.4    Goda, H.5    Niitsu, M.6    Shirahata, A.7    Samejima, K.8
  • 20
    • 0018349162 scopus 로고
    • Methylthioadenosine, a potent inhibitor of spermine synthase from bovine brain
    • Pajula, R.L. and Raina, A. (1979) Methylthioadenosine, a potent inhibitor of spermine synthase from bovine brain. FEBS Lett. 99, 343-345
    • (1979) FEBS Lett. , vol.99 , pp. 343-345
    • Pajula, R.L.1    Raina, A.2
  • 21
    • 0019017137 scopus 로고
    • Studies of inhibition of rat spermidine synthase and spermine synthase
    • Hibasami, H., Borchardt, R.T., Chen, S.Y., Coward, J.K., and Pegg, A.E. (1980) Studies of inhibition of rat spermidine synthase and spermine synthase. Biochem. J. 187, 419-428
    • (1980) Biochem. J. , vol.187 , pp. 419-428
    • Hibasami, H.1    Borchardt, R.T.2    Chen, S.Y.3    Coward, J.K.4    Pegg, A.E.5
  • 22
    • 2542531592 scopus 로고    scopus 로고
    • Targeting the polyamine pathway with transition-state analogue inhibitors of 5′-methylthioadenosine phosphorylase
    • Evans, G.B., Furneaux, R.H., Schramm, V.L., Singh, V., and Tyler, P.C. (2004) Targeting the polyamine pathway with transition-state analogue inhibitors of 5′-methylthioadenosine phosphorylase. J. Med. Chem. 47, 3275-3281
    • (2004) J. Med. Chem. , vol.47 , pp. 3275-3281
    • Evans, G.B.1    Furneaux, R.H.2    Schramm, V.L.3    Singh, V.4    Tyler, P.C.5
  • 25
    • 0023676375 scopus 로고
    • Synthesis of chirally deuteriated (S-adenosyl-S-methylsufonio) propylamines and spermidines. Elucidation of the stereochemical course of putrescine aminopropyltransferase (spermidine synthase)
    • Orr, G.J., Danz, D.W., Pontoni, G., Prabhakaran, P.C., Gould, S.J., and Coward, J.K. (1988) Synthesis of chirally deuteriated (S-adenosyl-S- methylsufonio)propylamines and spermidines. Elucidation of the stereochemical course of putrescine aminopropyltransferase (spermidine synthase). J. Am. Chem. Soc. 110, 5791-5799
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 5791-5799
    • Orr, G.J.1    Danz, D.W.2    Pontoni, G.3    Prabhakaran, P.C.4    Gould, S.J.5    Coward, J.K.6
  • 27
    • 0031039128 scopus 로고    scopus 로고
    • Spermidine biosynthesis in Saccharomyces cerevisiae: Polyamine requirement of a null mutant of the SPE3 gene (spermidine synthase)
    • Hamasaki-Katagiri, N., Tabor, C.W., and Tabor, H. (1997) Spermidine biosynthesis in Saccharomyces cerevisiae: polyamine requirement of a null mutant of the SPE3 gene (spermidine synthase). Gene 187, 35-43
    • (1997) Gene , vol.187 , pp. 35-43
    • Hamasaki-Katagiri, N.1    Tabor, C.W.2    Tabor, H.3
  • 28
    • 0032960912 scopus 로고    scopus 로고
    • Isolation of spermidine synthase gene (spsA) of Dictyostelium discoideum
    • Guo, K., Chang, W.-T., and Newell, P.C. (1999) Isolation of spermidine synthase gene (spsA) of Dictyostelium discoideum. Biochim. Biophys. Acta 1449, 211-216
    • (1999) Biochim. Biophys. Acta , vol.1449 , pp. 211-216
    • Guo, K.1    Chang, W.-T.2    Newell, P.C.3
  • 30
    • 0036436967 scopus 로고    scopus 로고
    • Requirement of spermidine for developmental transitions in Aspergillus nidulans
    • Jin, Y., Bok, J.W., Guzman-de-Pena, D., and Keller, N.P. (2002) Requirement of spermidine for developmental transitions in Aspergillus nidulans. Mol Microbiol 46, 801-812
    • (2002) Mol Microbiol , vol.46 , pp. 801-812
    • Jin, Y.1    Bok, J.W.2    Guzman-de-Pena, D.3    Keller, N.P.4
  • 31
    • 2942635960 scopus 로고    scopus 로고
    • Novel chimeric spermidine synthase-saccharopine dehydrogenase gene (SPE3-LYS9) in the human pathogen Cryptococcus neoformans
    • Kingsbury, J.M., Yang, Z., Ganous, T.M., Cox, G.M., and McCusker, J.H. (2004) Novel chimeric spermidine synthase-saccharopine dehydrogenase gene (SPE3-LYS9) in the human pathogen Cryptococcus neoformans. Eukaryot. Cell 3, 752-763
    • (2004) Eukaryot. Cell , vol.3 , pp. 752-763
    • Kingsbury, J.M.1    Yang, Z.2    Ganous, T.M.3    Cox, G.M.4    McCusker, J.H.5
  • 34
    • 18344418431 scopus 로고    scopus 로고
    • Spermine is not essential for growth of Saccharomyces cerevisiae: Identification of the SPE4 gene (spermine synthase) and characterization of a spe4 deletion mutant
    • Hamasaki-Katagiri, N., Katagiri, Y., Tabor, C.W., and Tabor, H. (1998) Spermine is not essential for growth of Saccharomyces cerevisiae: identification of the SPE4 gene (spermine synthase) and characterization of a spe4 deletion mutant. Gene 210, 195-210
    • (1998) Gene , vol.210 , pp. 195-210
    • Hamasaki-Katagiri, N.1    Katagiri, Y.2    Tabor, C.W.3    Tabor, H.4
  • 35
    • 0345133303 scopus 로고    scopus 로고
    • Spermidine but not spermine is essential for hypusine biosynthesis and growth in Saccharomyces cerevisiae: Spermine is converted to spermidine in vivo by the FMS1-amine oxidase
    • Chattopadhyay, M.K., Tabor, C.W., and Tabor, H. (2003) Spermidine but not spermine is essential for hypusine biosynthesis and growth in Saccharomyces cerevisiae: spermine is converted to spermidine in vivo by the FMS1-amine oxidase. Proc. Natl. Acad. Sci. USA 100, 13869-13874
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13869-13874
    • Chattopadhyay, M.K.1    Tabor, C.W.2    Tabor, H.3
  • 37
    • 26944478211 scopus 로고    scopus 로고
    • Arabidopsis thickvein mutation affects vein thickness and organ vascularization, and resides in a provascular cell-specific spermine synthase involved in vein definition and in polar auxin transport
    • Clay, N.K. and Nelson, T. (2005) Arabidopsis thickvein mutation affects vein thickness and organ vascularization, and resides in a provascular cell-specific spermine synthase involved in vein definition and in polar auxin transport. Plant Physiol. 138, 767-777
    • (2005) Plant Physiol. , vol.138 , pp. 767-777
    • Clay, N.K.1    Nelson, T.2
  • 38
    • 0344624870 scopus 로고    scopus 로고
    • Partial deletion of both the spermine synthase gene and the Pex gene in the x-linked hypophosphatemic, Gyro (Gy) mouse
    • Meyer, R.A., Jr., Henley, C.M., Meyer, M.H., L., M.P., McDonald, A.G., Mills, C., and Price, D.K. (1998) Partial deletion of both the spermine synthase gene and the Pex gene in the x-linked hypophosphatemic, Gyro (Gy) mouse. Genomics 48, 289-295
    • (1998) Genomics , vol.48 , pp. 289-295
    • Meyer Jr., R.A.1    Henley, C.M.2    Meyer, M.H.3    L., M.P.4    McDonald, A.G.5    Mills, C.6    Price, D.K.7
  • 39
    • 0034667601 scopus 로고    scopus 로고
    • Effect of spermine synthase deficiency on polyamine biosynthesis and content in mice and embryonic fibroblasts and the sensitivity of fibroblasts to 1,3-bis(2-chloroethyl)-N-nitrosourea
    • Mackintosh, C.A. and Pegg, A.E. (2000) Effect of spermine synthase deficiency on polyamine biosynthesis and content in mice and embryonic fibroblasts and the sensitivity of fibroblasts to 1,3-bis(2-chloroethyl)-N- nitrosourea. Biochem. J. 351, 439-447
    • (2000) Biochem. J. , vol.351 , pp. 439-447
    • Mackintosh, C.A.1    Pegg, A.E.2
  • 40
    • 0034003979 scopus 로고    scopus 로고
    • Failure of spennatogenesis in mouse lines deficient in the Na(+)-K(+)-2Cl(-) cotransporter
    • Pace, A.J., Lee, E., Athirakul, K., Coffman, T.M., O'Brien, D.A., and Koller, B.H. (2000) Failure of spennatogenesis in mouse lines deficient in the Na(+)-K(+)-2Cl(-) cotransporter. J. Clin. Invest. 105, 441-450
    • (2000) J. Clin. Invest. , vol.105 , pp. 441-450
    • Pace, A.J.1    Lee, E.2    Athirakul, K.3    Coffman, T.M.4    O'Brien, D.A.5    Koller, B.H.6
  • 42
    • 3142567130 scopus 로고    scopus 로고
    • Overexpression of spermidine synthase enhances tolerance to multiple environmental stresses and up-regulates the expression of various stress-regulated genes in transgenic Arabidopsis thaliana
    • Kasukabe, Y., He, L., Nada, K., Misawa, S., Ihara, I., and Tachibana, S. (2004) Overexpression of spermidine synthase enhances tolerance to multiple environmental stresses and up-regulates the expression of various stress-regulated genes in transgenic Arabidopsis thaliana. Plant Cell Physiol. 45, 712-722
    • (2004) Plant Cell Physiol. , vol.45 , pp. 712-722
    • Kasukabe, Y.1    He, L.2    Nada, K.3    Misawa, S.4    Ihara, I.5    Tachibana, S.6
  • 43
    • 4944244431 scopus 로고    scopus 로고
    • Effects of spermidine synthase overexpression on polyamine biosynthetic pathway in tobacco plants
    • Franceschetti, M., Fornale, S., Tassonia, A., Zuccherelli, K., Mayer, M.J., and Bagni, N. (2004) Effects of spermidine synthase overexpression on polyamine biosynthetic pathway in tobacco plants. J. Plant Physiol. 161, 989-1001
    • (2004) J. Plant Physiol. , vol.161 , pp. 989-1001
    • Franceschetti, M.1    Fornale, S.2    Tassonia, A.3    Zuccherelli, K.4    Mayer, M.J.5    Bagni, N.6
  • 45
    • 30044452238 scopus 로고    scopus 로고
    • Overproduction of cardiac S-adenosylmethionine decarboxylase in transgenic mice
    • Nisenberg, O., Pegg, A.E., Welsh, P.A., Keefer, K., and Shantz, L.M. (2006) Overproduction of cardiac S-adenosylmethionine decarboxylase in transgenic mice. Biochem. J. 393, 295-302
    • (2006) Biochem. J. , vol.393 , pp. 295-302
    • Nisenberg, O.1    Pegg, A.E.2    Welsh, P.A.3    Keefer, K.4    Shantz, L.M.5
  • 47
    • 0036184652 scopus 로고    scopus 로고
    • Androgen regulation of spermidine synthase expression in the rat prostate
    • Cyriac, J., Haleem, R., Cai, X., and Wang, Z. (2002) Androgen regulation of spermidine synthase expression in the rat prostate. Prostate 50, 252-261
    • (2002) Prostate , vol.50 , pp. 252-261
    • Cyriac, J.1    Haleem, R.2    Cai, X.3    Wang, Z.4
  • 48
    • 4944242891 scopus 로고    scopus 로고
    • Polyamines and cancer: Old molecules, new understanding
    • Gerner, E.W. and Meyskens, F.L., Jr. (2004) Polyamines and cancer: old molecules, new understanding. Nat. Rev. Cancer 4, 781-792
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 781-792
    • Gerner, E.W.1    Meyskens Jr., F.L.2


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