메뉴 건너뛰기




Volumn 177, Issue 1-2, 1996, Pages 17-22

Cloning and sequencing of the gene coding for S-adenosylhomocysteine hydrolase in the thermophilic archaeon Sulfolobus solfataricus

Author keywords

Archaea; Codon usage; NAD binding domain; Potential regulatory sites; Sequence homology; Thermostable enzymes

Indexed keywords

ADENOSYLHOMOCYSTEINASE; CYANOGEN BROMIDE; OLIGODEOXYRIBONUCLEOTIDE;

EID: 0030600445     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/0378-1119(96)00263-6     Document Type: Article
Times cited : (9)

References (30)
  • 1
    • 0028124204 scopus 로고
    • The role of cysteine 78 in fluorosulfonyl-benzoyladenosine inactivation of rat liver S-adenosylhomocysteine hydrolase
    • Aksamit, R.R., Backlund Jr., P.S., Moos Jr., M., Caryk, T., Gomi, T., Ogawa, H., Fujioka, M. and Cantoni, G.L. (1994) The role of cysteine 78 in fluorosulfonyl-benzoyladenosine inactivation of rat liver S-adenosylhomocysteine hydrolase. J. Biol. Chem. 269, 4084-4091.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4084-4091
    • Aksamit, R.R.1    Backlund P.S., Jr.2    Moos M., Jr.3    Caryk, T.4    Gomi, T.5    Ogawa, H.6    Fujioka, M.7    Cantoni, G.L.8
  • 2
    • 0028081341 scopus 로고
    • A single mutation at lysine 426 of human placental S-adenosylhomocysteine hydrolase inactivates the enzyme
    • Ault-Riché, D.B., Yuan, C.-S. and Borchardt, R.T. (1994) A single mutation at lysine 426 of human placental S-adenosylhomocysteine hydrolase inactivates the enzyme. J. Biol. Chem. 269, 31472-31478.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31472-31478
    • Ault-Riché, D.B.1    Yuan, C.-S.2    Borchardt, R.T.3
  • 3
    • 0002304781 scopus 로고
    • The centrality of S-adenosylhomocysteinase in the regulation of the biological utilization of S-adenosylmethionine
    • Borchardt, R.T., Creveling, C.R. and Ueland, P.M. (Eds). Humana Press, Clifton, NJ
    • Cantoni, G.L. (1986) The centrality of S-adenosylhomocysteinase in the regulation of the biological utilization of S-adenosylmethionine. In: Borchardt, R.T., Creveling, C.R. and Ueland, P.M. (Eds), Biological Methylation and Drug Design. Humana Press, Clifton, NJ, pp. 227-238.
    • (1986) Biological Methylation and Drug Design , pp. 227-238
    • Cantoni, G.L.1
  • 5
    • 0024409705 scopus 로고
    • Sequence of full length cDNA for human S-adenosylhomocysteine hydrolase
    • Coulter-Karis, D.E. and Hershfield, M.S. (1989) Sequence of full length cDNA for human S-adenosylhomocysteine hydrolase. Ann. Hum. Genet. 53, 169-175.
    • (1989) Ann. Hum. Genet. , vol.53 , pp. 169-175
    • Coulter-Karis, D.E.1    Hershfield, M.S.2
  • 6
    • 0028292569 scopus 로고
    • Plasmodium falciparum S-adenosylhomocysteine hydrolase. CDNA identification, predicted protein sequence, and expression in Escherichia coli
    • Creedon, K.A., Rathod, P.K. and Wellems, T.E. (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
  • 7
    • 70449254180 scopus 로고
    • The enzymatic synthesis of S-adenosyl-L-homocysteine from adenosine and homocysteine
    • de la Haba, G. and Cantoni, G.L. (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
  • 8
    • 0016426743 scopus 로고
    • Extremely thermophilic acidophilic bacteria convergent with Sulfolobus acidocaldarius
    • De Rosa, M., Gambacorta, A. and Bu'lock, J. (1975) Extremely thermophilic acidophilic bacteria convergent with Sulfolobus acidocaldarius. J. Gen. Microbiol. 86, 156-164.
    • (1975) J. Gen. Microbiol. , vol.86 , pp. 156-164
    • De Rosa, M.1    Gambacorta, A.2    Bu'lock, J.3
  • 9
    • 0027182861 scopus 로고
    • Characterization, cloning, and in vitro expression of the extremely thermostable glutamate dehydrogenase from the hyperthermophilic archaeon, ES4
    • Di Ruggiero, J., Robb, F.T., Jagus, R., Klump, H.H., Borges, K.M., Kessel, M., Mai, X. and Adam, M.W.W. (1993) Characterization, cloning, and in vitro expression of the extremely thermostable glutamate dehydrogenase from the hyperthermophilic archaeon, ES4. J. Biol. Chem. 268, 17767-17774.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17767-17774
    • Di Ruggiero, J.1    Robb, F.T.2    Jagus, R.3    Klump, H.H.4    Borges, K.M.5    Kessel, M.6    Mai, X.7    Adam, M.W.W.8
  • 10
    • 0022999804 scopus 로고
    • S-Adenosylhomocysteine hydrolase from rat liver. Amino acid sequence of the peptides containing active site cysteine residues modified by treatment with 5′-p-fluorosulfonylbenzoyladenosine
    • Gomi, T., Ogawa, H. and Fujioka, M. (1986) S-Adenosylhomocysteine hydrolase from rat liver. Amino acid sequence of the peptides containing active site cysteine residues modified by treatment with 5′-p-fluorosulfonylbenzoyladenosine. J. Biol. Chem. 261, 13422-13425.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13422-13425
    • Gomi, T.1    Ogawa, H.2    Fujioka, M.3
  • 12
    • 0024234855 scopus 로고
    • CLUSTAL: A package for performing multiple sequence alignment on a microcomputer
    • Higgins, D.G. and Sharp, P.M. (1988) CLUSTAL: a package for performing multiple sequence alignment on a microcomputer. Gene 73, 237-244.
    • (1988) Gene , vol.73 , pp. 237-244
    • Higgins, D.G.1    Sharp, P.M.2
  • 13
    • 0024300841 scopus 로고
    • Amino acid sequence of S-adenosyl-L-homocysteine hydrolase from Dictyostelium discoideum as deduced from the cDNA sequence
    • Kasir, J., Aksamit, R.R., Backlund Jr., P.S. and Cantoni, G.L. (1988) Amino acid sequence of S-adenosyl-L-homocysteine hydrolase from Dictyostelium discoideum as deduced from the cDNA sequence. Biochem. Biophys. Res. Commun. 153, 359-364.
    • (1988) Biochem. Biophys. Res. Commun. , vol.153 , pp. 359-364
    • Kasir, J.1    Aksamit, R.R.2    Backlund P.S., Jr.3    Cantoni, G.L.4
  • 14
    • 0026587102 scopus 로고
    • Induction by fungal elicitor of S-adenosyl-L-methionine synthetase and S-adenosyl-L-homocysteine hydrolase mRNAs in cultured cells and leaves of Petroselinum crispum
    • Kawalleck, P., Plesch, G., Hahlbrock, K. and Somssich, I.E. (1992) Induction by fungal elicitor of S-adenosyl-L-methionine synthetase and S-adenosyl-L-homocysteine hydrolase mRNAs in cultured cells and leaves of Petroselinum crispum. Proc. Natl. Acad. Sci. USA 89, 4713-4717.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4713-4717
    • Kawalleck, P.1    Plesch, G.2    Hahlbrock, K.3    Somssich, I.E.4
  • 15
    • 85047694290 scopus 로고
    • The gene and pseudogenes of rat S-adenosyl-L-homocysteine hydrolase
    • Merta, A., Aksamit, R.R., Kasir, J. and Cantoni, G.L. (1995) The gene and pseudogenes of rat S-adenosyl-L-homocysteine hydrolase. Eur. J. Biochem. 229, 575-582.
    • (1995) Eur. J. Biochem. , vol.229 , pp. 575-582
    • Merta, A.1    Aksamit, R.R.2    Kasir, J.3    Cantoni, G.L.4
  • 16
    • 0024222966 scopus 로고
    • Structure-stability relationship in proteins: Fundamental tasks and strategy for the development of stabilized enzyme catalists for biotechnology
    • Mozhaev, V.V., Berezin, I.V. and Martinek, K. (1988) Structure-stability relationship in proteins: fundamental tasks and strategy for the development of stabilized enzyme catalists for biotechnology. CRC Critical Reviews in Biochemistry 23, 235-281.
    • (1988) CRC Critical Reviews in Biochemistry , vol.23 , pp. 235-281
    • Mozhaev, V.V.1    Berezin, I.V.2    Martinek, K.3
  • 18
    • 0022350311 scopus 로고
    • Sequence of the 16S rRNA gene from the thermoacidophilic archaebacterium Sulfolobus solfataricus and its evolutionary implications
    • Olsen, G.J., Pace, N.R., Nuell, M., Kaine, B.P., Gupta, R. and Woese, C.R. (1985) Sequence of the 16S rRNA gene from the thermoacidophilic archaebacterium Sulfolobus solfataricus and its evolutionary implications. J. Mol. Evol. 22, 301-307.
    • (1985) J. Mol. Evol. , vol.22 , pp. 301-307
    • Olsen, G.J.1    Pace, N.R.2    Nuell, M.3    Kaine, B.P.4    Gupta, R.5    Woese, C.R.6
  • 19
    • 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 Rosa, M. and Zappia, V. (1993a) 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 Rosa, M.6    Zappia, V.7
  • 20
    • 0011894066 scopus 로고
    • Studies on stability of S-adenosylhomocysteine hydrolase from Sulfolobus solfataricus, a thermophilic archaebacterium
    • Van den Tweel, W.J.J., Harder, A. and Buitelaar, R.R. (Eds). Elsevier Science Publishers, The Netherlands
    • Porcelli, M., Cacciapuoti, G., Fusco, S., Bertoldo, C. and Zappia, V. (1993b) Studies on stability of S-adenosylhomocysteine hydrolase from Sulfolobus solfataricus, a thermophilic archaebacterium. In: Van den Tweel, W.J.J., Harder, A. and Buitelaar, R.R. (Eds), Stability and Stabilization of Enzymes. Elsevier Science Publishers, The Netherlands, pp. 437-444.
    • (1993) Stability and Stabilization of Enzymes , pp. 437-444
    • Porcelli, M.1    Cacciapuoti, G.2    Fusco, S.3    Bertoldo, C.4    Zappia, V.5
  • 21
    • 0027208964 scopus 로고
    • Molecular characterization in the dpy-14 region identifies the S-adenosylhomocysteine hydrolase gene in Caenorhabditis elegans
    • Prasad, S.S., Starr, T.V. and Rose, A.M. (1993) Molecular characterization in the dpy-14 region identifies the S-adenosylhomocysteine hydrolase gene in Caenorhabditis elegans. Genome 36, 57-65.
    • (1993) Genome , vol.36 , pp. 57-65
    • Prasad, S.S.1    Starr, T.V.2    Rose, A.M.3
  • 22
    • 0011820409 scopus 로고
    • GenBank/EMBL accession no. L11872
    • Richards, K.D. and Gardner, R.C. (1993) GenBank/EMBL accession No. L11872
    • (1993)
    • Richards, K.D.1    Gardner, R.C.2
  • 24
    • 0028397845 scopus 로고
    • cDNA for S-adenosyl-L-homocysteine hydrolase from Catharanthus roseus
    • Schroder, G., Waitz, A., Hotze, M. and Schroder, J. (1994) cDNA for S-adenosyl-L-homocysteine hydrolase from Catharanthus roseus. Plant. Physiol. 104, 1099-1100.
    • (1994) Plant. Physiol. , vol.104 , pp. 1099-1100
    • Schroder, G.1    Waitz, A.2    Hotze, M.3    Schroder, J.4
  • 25
    • 0026776409 scopus 로고
    • Mutational and nucleotide sequence analysis of S-adenosyl-L-homocysteine hydrolase from Rhodobacter capsulatus
    • Sganga, M.W., Aksamit, R.R., Cantoni, G.L. and Bauer, C.E. (1992) Mutational and nucleotide sequence analysis of S-adenosyl-L-homocysteine hydrolase from Rhodobacter capsulatus. Proc. Natl. Acad. Sci. USA 89, 6328-6332.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6328-6332
    • Sganga, M.W.1    Aksamit, R.R.2    Cantoni, G.L.3    Bauer, C.E.4
  • 26
    • 0020284631 scopus 로고
    • Pharmacological and biochemical aspects of S-adenosylhomocysteine and S-adenosylhomocysteine hydrolase
    • Ueland, P.M. (1982) Pharmacological and biochemical aspects of S-adenosylhomocysteine and S-adenosylhomocysteine hydrolase. Pharmacol. Rev. 34, 223-253.
    • (1982) Pharmacol. Rev. , vol.34 , pp. 223-253
    • Ueland, P.M.1
  • 27
    • 33845318295 scopus 로고
    • Interaction of pyrophosphate moieties with α-helices in dinucleotide binding proteins
    • Wierenga, R.K., De Maeyer, M.C.H. and Hol, W.G.J. (1985) Interaction of pyrophosphate moieties with α-helices in dinucleotide binding proteins. Biochemistry 24, 1346-1357.
    • (1985) Biochemistry , vol.24 , pp. 1346-1357
    • Wierenga, R.K.1    De Maeyer, M.C.H.2    Hol, W.G.J.3
  • 28
    • 0025300402 scopus 로고
    • Towards a natural system of organisms: Proposal for the domains Archaea, Bacteria, and Eucarya
    • Woese, C.R., Kandler, O. and Wheelis, M.L. (1990) Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya. Proc. Natl. Acad. Sci. USA 87, 4576-4579.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4576-4579
    • Woese, C.R.1    Kandler, O.2    Wheelis, M.L.3
  • 29
    • 0026179549 scopus 로고
    • A molecular model for the active site of S-adenosyl-L-homocysteine hydrolase
    • Yeh, J.C., Borchardt, R.T., Vedani, A. (1991) A molecular model for the active site of S-adenosyl-L-homocysteine hydrolase. J. Comput. Aided Mol. Des. 5, 213-234
    • (1991) J. Comput. Aided Mol. Des. , vol.5 , pp. 213-234
    • Yeh, J.C.1    Borchardt, R.T.2    Vedani, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.