메뉴 건너뛰기




Volumn 273, Issue 1, 2007, Pages 87-95

Characterization of S-adenosylhomocysteine hydrolase from Cryptosporidium parvum

Author keywords

Ara A; Cryptosporidium parvum; D eritadenine; S adenosylhomocysteine hydrolase; S DHPA

Indexed keywords

ADENOSYLHOMOCYSTEINASE; BLOOD CLOTTING FACTOR 10A; MALTOSE BINDING PROTEIN;

EID: 34347374076     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2007.00795.x     Document Type: Article
Times cited : (11)

References (40)
  • 1
    • 11144353587 scopus 로고    scopus 로고
    • Complete genome sequence of the apicomplexan, Cryptosporidium parvum
    • Abrahamsen MS, Templeton TJ, Enomoto S et al 2004) Complete genome sequence of the apicomplexan, Cryptosporidium parvum. Science 304 : 441 445.
    • (2004) Science , vol.304 , pp. 441-445
    • Abrahamsen, M.S.1    Templeton, T.J.2    Enomoto, S.3    Al, E.4
  • 3
    • 12144286157 scopus 로고    scopus 로고
    • S-adenosylhomocysteine hydrolase deficiency in a human: A genetic disorder of methionine metabolism
    • Baric I, Fumic K, Glenn B et al 2004) S-adenosylhomocysteine hydrolase deficiency in a human: a genetic disorder of methionine metabolism. Proc Natl Acad Sci USA 101 : 4234 4239.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 4234-4239
    • Baric, I.1    Fumic, K.2    Glenn, B.3    Al, E.4
  • 4
    • 0021227696 scopus 로고
    • Neplanocin A. a potent inhibitor of S-adenosylhomocysteine hydrolase and of vaccinia virus multiplication in mouse L929 cells
    • Borchardt RT, Keller BT Patel-Thombre U (1984) Neplanocin A. A potent inhibitor of S-adenosylhomocysteine hydrolase and of vaccinia virus multiplication in mouse L929 cells. J Biol Chem 259 : 4353 4358.
    • (1984) J Biol Chem , vol.259 , pp. 4353-4358
    • Borchardt, R.T.1    Keller, B.T.2    Patel-Thombre, U.3
  • 6
    • 0028292569 scopus 로고
    • Plasmodium falciparum S-adenosylhomocysteine hydrolase. cDNA identification, predicted protein sequence, and expression in Escherichia coli
    • Creedon KA, Rathod PK Wellems TE (1994) Plasmodium falciparum S-adenosylhomocysteine hydrolase. cDNA identification, predicted protein sequence, and expression in Escherichia coli. J Biol Chem 269 : 16364 16370.
    • (1994) J Biol Chem , vol.269 , pp. 16364-16370
    • Creedon, K.A.1    Rathod, P.K.2    Wellems, T.E.3
  • 8
    • 70449254180 scopus 로고
    • The enzymatic synthesis of S-adenosyl-l-homocysteine from adenosine and homocysteine
    • De La Haba G Cantoni GL (1959) The enzymatic synthesis of S-adenosyl-l-homocysteine from adenosine and homocysteine. J Biol Chem 234 : 603 608.
    • (1959) J Biol Chem , vol.234 , pp. 603-608
    • De La Haba, G.1    Cantoni, G.L.2
  • 9
    • 0019887737 scopus 로고
    • S-adenosylhomocysteine hydrolase from rat liver. Purification and some properties
    • Fujioka M Takata Y (1981) S-adenosylhomocysteine hydrolase from rat liver. Purification and some properties. J Biol Chem 256 : 1631 1635.
    • (1981) J Biol Chem , vol.256 , pp. 1631-1635
    • Fujioka, M.1    Takata, Y.2
  • 10
    • 0017658748 scopus 로고
    • Adenosylhomocysteinase from yellow lupin seeds. Purification and properties
    • Guranowski A Pawelkiewicz J (1977) Adenosylhomocysteinase from yellow lupin seeds. Purification and properties. Eur J Biochem 80 : 517 523.
    • (1977) Eur J Biochem , vol.80 , pp. 517-523
    • Guranowski, A.1    Pawelkiewicz, J.2
  • 12
    • 0022359847 scopus 로고
    • S-adenosylhomocysteine hydrolase from human placenta. Affinity purification and characterization
    • Hershfield MS, Aiyar VN, Premakumar R Small WC (1985) S-adenosylhomocysteine hydrolase from human placenta. Affinity purification and characterization. Biochem J 230 : 43 52.
    • (1985) Biochem J , vol.230 , pp. 43-52
    • Hershfield, M.S.1    Aiyar, V.N.2    Premakumar, R.3    Small, W.C.4
  • 13
    • 0021959633 scopus 로고
    • Studies on S-adenosyl-l-homocysteine hydrolase 14. Structure-activity studies on open-chain analogs of nucleosides - Inhibition of S-adenosyl-l-homocysteine hydrolase and antiviral activity 2. Acid open-chain analogs
    • Holy A, Votruba I Declercq E (1985) Studies on S-adenosyl-l-homocysteine hydrolase 14. Structure-activity studies on open-chain analogs of nucleosides - inhibition of S-adenosyl-l-homocysteine hydrolase and antiviral activity 2. Acid open-chain analogs. Collect Czech Chem Commun 50 : 262 279.
    • (1985) Collect Czech Chem Commun , vol.50 , pp. 262-279
    • Holy, A.1    Votruba, I.2    Declercq, E.3
  • 15
    • 0036141514 scopus 로고    scopus 로고
    • Epidemiology and clinical features of Cryptosporidium infection in immunocompromised patients
    • Hunter PR Nichols G (2002) Epidemiology and clinical features of Cryptosporidium infection in immunocompromised patients. Clin Microbiol Rev 15 : 145 154.
    • (2002) Clin Microbiol Rev , vol.15 , pp. 145-154
    • Hunter, P.R.1    Nichols, G.2
  • 19
    • 0031691447 scopus 로고    scopus 로고
    • Trichomonas vaginalis: Expression and characterisation of recombinant S-adenosylhomocysteinase
    • Minotto L, Ko GA, Edwards MR Bagnara AS (1998) Trichomonas vaginalis: expression and characterisation of recombinant S-adenosylhomocysteinase. Exp Parasitol 90 : 175 180.
    • (1998) Exp Parasitol , vol.90 , pp. 175-180
    • Minotto, L.1    Ko, G.A.2    Edwards, M.R.3    Bagnara, A.S.4
  • 20
    • 0035122340 scopus 로고    scopus 로고
    • Purification and properties of recombinant Plasmodium falciparum S-adenosyl-l-homocysteine hydrolase
    • Nakanishi M, Iwata A, Yatome C Kitade Y (2001) Purification and properties of recombinant Plasmodium falciparum S-adenosyl-l-homocysteine hydrolase. J Biochem (Tokyo) 129 : 101 105.
    • (2001) J Biochem (Tokyo) , vol.129 , pp. 101-105
    • Nakanishi, M.1    Iwata, A.2    Yatome, C.3    Kitade, Y.4
  • 21
    • 26844478710 scopus 로고    scopus 로고
    • Sulfur-containing amino acid metabolism in parasitic protozoa
    • Nozaki T, Ali V Tokoro M (2005) Sulfur-containing amino acid metabolism in parasitic protozoa. Adv Parasitol 60 : 1 99.
    • (2005) Adv Parasitol , vol.60 , pp. 1-99
    • Nozaki, T.1    Ali, V.2    Tokoro, M.3
  • 23
    • 0027296721 scopus 로고
    • S-adenosylhomocysteine hydrolase from the thermophilic archaeon Sulfolobus solfataricus: Purification, physico-chemical and immunological properties
    • Porcelli M, Cacciapuoti G, Fusco S, Iacomino G, Gambacorta A, De RM Zappia V (1993) S-adenosylhomocysteine hydrolase from the thermophilic archaeon Sulfolobus solfataricus: purification, physico-chemical and immunological properties. Biochim Biophys Acta 1164 : 179 188.
    • (1993) Biochim Biophys Acta , vol.1164 , pp. 179-188
    • Porcelli, M.1    Cacciapuoti, G.2    Fusco, S.3    Iacomino, G.4    Gambacorta, A.5    De, R.M.6    Zappia, V.7
  • 24
    • 0034142074 scopus 로고    scopus 로고
    • Expression, purification, and characterization of recombinant S-adenosylhomocysteine hydrolase from the thermophilic archaeon Sulfolobus solfataricus
    • Porcelli M, Fusco S, Inizio T, Zappia V Cacciapuoti G (2000) Expression, purification, and characterization of recombinant S-adenosylhomocysteine hydrolase from the thermophilic archaeon Sulfolobus solfataricus. Protein Expr Purif 18 : 27 35.
    • (2000) Protein Expr Purif , vol.18 , pp. 27-35
    • Porcelli, M.1    Fusco, S.2    Inizio, T.3    Zappia, V.4    Cacciapuoti, G.5
  • 26
    • 0021451570 scopus 로고
    • Occurrence of S-adenosylhomocysteine hydrolase in prokaryote cells. Characterization of the enzyme from Alcaligenes faecalis and role of the enzyme in the activated methyl cycle
    • Shimizu S, Shiozaki S, Ohshiro T Yamada H (1984) Occurrence of S-adenosylhomocysteine hydrolase in prokaryote cells. Characterization of the enzyme from Alcaligenes faecalis and role of the enzyme in the activated methyl cycle. Eur J Biochem 141 : 385 392.
    • (1984) Eur J Biochem , vol.141 , pp. 385-392
    • Shimizu, S.1    Shiozaki, S.2    Ohshiro, T.3    Yamada, H.4
  • 27
    • 0642302965 scopus 로고    scopus 로고
    • Characterization of S-adenosylmethionine synthetase in Cryptosporidium parvum (Apicomplexa)
    • Slapeta J, Stejskal F Keithly JS (2003) Characterization of S-adenosylmethionine synthetase in Cryptosporidium parvum (Apicomplexa). FEMS Microbiol Lett 225 : 271 277.
    • (2003) FEMS Microbiol Lett , vol.225 , pp. 271-277
    • Slapeta, J.1    Stejskal, F.2    Keithly, J.S.3
  • 28
    • 0034653305 scopus 로고    scopus 로고
    • Preliminary profile of the Cryptosporidium parvum genome: An expressed sequence tag and genome survey sequence analysis
    • Strong WB Nelson RG (2000) Preliminary profile of the Cryptosporidium parvum genome: an expressed sequence tag and genome survey sequence analysis. Mol Biochem Parasitol 107 : 1 32.
    • (2000) Mol Biochem Parasitol , vol.107 , pp. 1-32
    • Strong, W.B.1    Nelson, R.G.2
  • 29
    • 0037151004 scopus 로고    scopus 로고
    • Catalytic mechanism of S-adenosylhomocysteine hydrolase. Site-directed mutagenesis of Asp-130, Lys-185, Asp-189, and Asn-190
    • Takata Y, Yamada T, Huang Y, Komoto J, Gomi T, Ogawa H, Fujioka M Takusagawa F (2002) Catalytic mechanism of S-adenosylhomocysteine hydrolase. Site-directed mutagenesis of Asp-130, Lys-185, Asp-189, and Asn-190. J Biol Chem 277 : 22670 22676.
    • (2002) J Biol Chem , vol.277 , pp. 22670-22676
    • Takata, Y.1    Yamada, T.2    Huang, Y.3    Komoto, J.4    Gomi, T.5    Ogawa, H.6    Fujioka, M.7    Takusagawa, F.8
  • 30
    • 5144234233 scopus 로고    scopus 로고
    • Crystal structure of S-adenosyl-l-homocysteine hydrolase from the human malaria parasite Plasmodium falciparum
    • Tanaka N, Nakanishi M, Kusakabe Y, Shiraiwa K, Yabe S, Ito Y, Kitade Y Nakamura KT (2004) Crystal structure of S-adenosyl-l-homocysteine hydrolase from the human malaria parasite Plasmodium falciparum. J Mol Biol 343 : 1007 1017.
    • (2004) J Mol Biol , vol.343 , pp. 1007-1017
    • Tanaka, N.1    Nakanishi, M.2    Kusakabe, Y.3    Shiraiwa, K.4    Yabe, S.5    Ito, Y.6    Kitade, Y.7    Nakamura, K.T.8
  • 32
    • 0031947190 scopus 로고    scopus 로고
    • Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength
    • Turner MA, Yuan CS, Borchardt RT, Hershfield MS, Smith GD Howell PL (1998) Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength. Nat Struct Biol 5 : 369 376.
    • (1998) Nat Struct Biol , vol.5 , pp. 369-376
    • Turner, M.A.1    Yuan, C.S.2    Borchardt, R.T.3    Hershfield, M.S.4    Smith, G.D.5    Howell, P.L.6
  • 35
    • 7744238311 scopus 로고    scopus 로고
    • The genome of Cryptosporidium hominis
    • Xu P, Widmer G, Wang Y et al 2004) The genome of Cryptosporidium hominis. Nature 431 : 1107 1112.
    • (2004) Nature , vol.431 , pp. 1107-1112
    • Xu, P.1    Widmer, G.2    Wang, Y.3    Al, E.4
  • 36
    • 23944456820 scopus 로고    scopus 로고
    • Catalytic mechanism of S-adenosylhomocysteine hydrolase: Roles of His 54, Asp130, Glu155, Lys185, and Aspl89
    • Yamada T, Takata Y, Komoto J, Gomi T, Ogawa H, Fujioka M Takusagawa F (2005) Catalytic mechanism of S-adenosylhomocysteine hydrolase: roles of His 54, Asp130, Glu155, Lys185, and Aspl89. Int J Biochem Cell Biol 37 : 2417 2435.
    • (2005) Int J Biochem Cell Biol , vol.37 , pp. 2417-2435
    • Yamada, T.1    Takata, Y.2    Komoto, J.3    Gomi, T.4    Ogawa, H.5    Fujioka, M.6    Takusagawa, F.7
  • 37
    • 0034669468 scopus 로고    scopus 로고
    • Overexpression, purification, and characterization of S-adenosylhomocysteine hydrolase from Leishmania donovani
    • Yang X Borchardt RT (2000) Overexpression, purification, and characterization of S-adenosylhomocysteine hydrolase from Leishmania donovani. Arch Biochem Biophys 383 : 272 280.
    • (2000) Arch Biochem Biophys , vol.383 , pp. 272-280
    • Yang, X.1    Borchardt, R.T.2
  • 38
    • 0029961930 scopus 로고    scopus 로고
    • Chemical modification and site-directed mutagenesis of cysteine residues in human placental S-adenosylhomocysteine hydrolase
    • Yuan CS, ult-Riche DB Borchardt RT (1996) Chemical modification and site-directed mutagenesis of cysteine residues in human placental S-adenosylhomocysteine hydrolase. J Biol Chem 271 : 28009 28016.
    • (1996) J Biol Chem , vol.271 , pp. 28009-28016
    • Yuan, C.S.1    Ult-Riche, D.B.2    Borchardt, R.T.3
  • 39
    • 0031455414 scopus 로고    scopus 로고
    • Molecular analysis of a P-type ATPase from Cryptosporidium parvum
    • Zhu G Keithly JS (1997) Molecular analysis of a P-type ATPase from Cryptosporidium parvum. Mol Biochem Parasitol 90 : 307 316.
    • (1997) Mol Biochem Parasitol , vol.90 , pp. 307-316
    • Zhu, G.1    Keithly, J.S.2
  • 40
    • 33749512434 scopus 로고    scopus 로고
    • Catalytic mechanism of S-ribosylhomocysteinase: Ionization state of active-site residues
    • Zhu J, Knottenbelt S, Kirk ML Pei D (2006) Catalytic mechanism of S-ribosylhomocysteinase: ionization state of active-site residues. Biochemistry 45 : 12195 12203.
    • (2006) Biochemistry , vol.45 , pp. 12195-12203
    • Zhu, J.1    Knottenbelt, S.2    Kirk, M.L.3    Pei, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.