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Volumn 261, Issue 1, 1999, Pages 1-9

Cobalt proteins

Author keywords

Cobalt; Glucose isomerase; Inorganic chemistry; Metal; Methionine aminopeptidase; Nitrile hydratase; Noncorrin; Prolidase; Transporter

Indexed keywords

AMINOPEPTIDASE; CARRIER PROTEIN; COBALT; CORRINOID; CYANOCOBALAMIN; GLUCOSE ISOMERASE; METALLOPROTEIN; METALLOPROTEINASE; METHYLMALONYL COENZYME A CARBOXYLTRANSFERASE; NICKEL; NITRILE HYDRATASE; PROLINE DIPEPTIDASE;

EID: 0033118237     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00186.x     Document Type: Review
Times cited : (396)

References (60)
  • 3
    • 0027425204 scopus 로고
    • Cobalt as probe and label of proteins
    • 3. Maret, W. & Valle, B.L. (1993) Cobalt as probe and label of proteins. Meth. Enzymol. 226, 52-71.
    • (1993) Meth. Enzymol. , vol.226 , pp. 52-71
    • Maret, W.1    Valle, B.L.2
  • 4
    • 0002856939 scopus 로고
    • Reactions of carbon monoxide and hydrogen with olefinic substrates: The hydroformylation (OXO) reaction
    • (Wender, I. & Pino, P., eds), John Wiley & Sons, New York
    • 4. Pino, P., Piacenti, F. & Bianchi, M. (1977) Reactions of carbon monoxide and hydrogen with olefinic substrates: the hydroformylation (OXO) reaction. In Organic Synthesis via Metal Carbonyls, Vol. 2, (Wender, I. & Pino, P., eds), pp. 43-135. John Wiley & Sons, New York.
    • (1977) Organic Synthesis Via Metal Carbonyls , vol.2 , pp. 43-135
    • Pino, P.1    Piacenti, F.2    Bianchi, M.3
  • 6
    • 0027273988 scopus 로고
    • Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: A new type of proteolytic enzyme
    • 6. Roderick, S.L. & Matthews, B.W. (1993) Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme. Biochemistry 32, 3907-3912.
    • (1993) Biochemistry , vol.32 , pp. 3907-3912
    • Roderick, S.L.1    Matthews, B.W.2
  • 7
    • 0028198617 scopus 로고
    • Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold
    • 7. Bazan, J.F., Weaver, L.H., Roderick, S.L., Huber, R. & Matthews, B.W. (1994) Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold. Proc. Natl Acad. Sci. USA 91, 2473-2477.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 2473-2477
    • Bazan, J.F.1    Weaver, L.H.2    Roderick, S.L.3    Huber, R.4    Matthews, B.W.5
  • 9
    • 0032514659 scopus 로고    scopus 로고
    • The anti-angiogenic agent fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidase
    • 9. Lowther, W.T., McMillen, D.A., Orville, A.M. & Matthews, B.W. (1998) The anti-angiogenic agent fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidase. Proc. Natl Acad. Sci. USA 95, 12153-12157.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 12153-12157
    • Lowther, W.T.1    McMillen, D.A.2    Orville, A.M.3    Matthews, B.W.4
  • 12
    • 0031927708 scopus 로고    scopus 로고
    • High-resolution crystals of methionine aminopeptidase from Pyrococcus furiosus obtained by water-mediated transformation
    • 12. Tahirov, T.H., Oki, H., Tsukihara, T., Ogasahara, K., Yutani, K., Libeu, C.P., Izu, Y., Tsunasawa, S. & Kato, I. (1998) High-resolution crystals of methionine aminopeptidase from Pyrococcus furiosus obtained by water-mediated transformation. J. Struct. Biol. 121, 68-72.
    • (1998) J. Struct. Biol. , vol.121 , pp. 68-72
    • Tahirov, T.H.1    Oki, H.2    Tsukihara, T.3    Ogasahara, K.4    Yutani, K.5    Libeu, C.P.6    Izu, Y.7    Tsunasawa, S.8    Kato, I.9
  • 14
    • 0031705698 scopus 로고    scopus 로고
    • Characterization of native and recomhinant forms of an unusual cobalt-dependent proline dipeptidase (prolidase) from the hyperthermophilic archaeon Pyrococcus furiosus
    • 14. Ghosh, M., Grunden, A.M., Dunn, D.M., Weiss, R. & Adams, M.W. (1998) Characterization of native and recomhinant forms of an unusual cobalt-dependent proline dipeptidase (prolidase) from the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 180, 4781-4789.
    • (1998) J. Bacteriol. , vol.180 , pp. 4781-4789
    • Ghosh, M.1    Grunden, A.M.2    Dunn, D.M.3    Weiss, R.4    Adams, M.W.5
  • 15
    • 0026480892 scopus 로고
    • Enzymatic synthesis of acrylamide: A success story not yet over
    • 15. Kobayashi, M., Nagasawa, T. & Yamada, H. (1992) Enzymatic synthesis of acrylamide: a success story not yet over. Trends Biotechnol. 10, 402-408.
    • (1992) Trends Biotechnol. , vol.10 , pp. 402-408
    • Kobayashi, M.1    Nagasawa, T.2    Yamada, H.3
  • 16
    • 0030250538 scopus 로고    scopus 로고
    • Nitrile hydratase and its application to industrial production of acrylamide
    • 16. Yamada, H. & Kobayashi, M. (1996) Nitrile hydratase and its application to industrial production of acrylamide. Biosci. Biotechnol. Biochem. 60, 1391-1400.
    • (1996) Biosci. Biotechnol. Biochem. , vol.60 , pp. 1391-1400
    • Yamada, H.1    Kobayashi, M.2
  • 17
    • 0031879561 scopus 로고    scopus 로고
    • Metalloenzyme nitrile hydratase: Structure, regulation, and application to biotechnology
    • 17. Kobayashi, M. & Shimizu, S. (1998) Metalloenzyme nitrile hydratase: structure, regulation, and application to biotechnology. Nature Biotechnol. 16, 733-736.
    • (1998) Nature Biotechnol. , vol.16 , pp. 733-736
    • Kobayashi, M.1    Shimizu, S.2
  • 18
    • 0025934442 scopus 로고
    • Cloning, nucleotide sequence and expression in Escherichia coli of two cobalt-containing nitrile hydratase genes from Rhodococcus rhodochrous J1
    • 18. Kobayashi, M., Nishiyama, M., Nagasawa, T., Horinouchi, S., Beppu, T. & Yamada, H. (1991) Cloning, nucleotide sequence and expression in Escherichia coli of two cobalt-containing nitrile hydratase genes from Rhodococcus rhodochrous J1. Biochim. Biophys. Acta 1129, 23-33.
    • (1991) Biochim. Biophys. Acta , vol.1129 , pp. 23-33
    • Kobayashi, M.1    Nishiyama, M.2    Nagasawa, T.3    Horinouchi, S.4    Beppu, T.5    Yamada, H.6
  • 20
    • 0031570299 scopus 로고    scopus 로고
    • Crystal structure of nitrile hydratase reveals a novel iron centre in a novel fold
    • 20. Huang, W., Jia, J., Cummings, J., Nelson, M., Schneider, G. & Lindqvist, Y. (1997) Crystal structure of nitrile hydratase reveals a novel iron centre in a novel fold. Structure 5, 691-699.
    • (1997) Structure , vol.5 , pp. 691-699
    • Huang, W.1    Jia, J.2    Cummings, J.3    Nelson, M.4    Schneider, G.5    Lindqvist, Y.6
  • 21
    • 0029805756 scopus 로고    scopus 로고
    • Nitrile hydratase from Rhodococcus rhodochrous J1 contains a non-corrin cobalt ion with two sulfur ligands
    • 21. Brennan, B.A., Alms, G., Nelson, M., Durney, L.T. & Scarrow, R.C. (1996) Nitrile hydratase from Rhodococcus rhodochrous J1 contains a non-corrin cobalt ion with two sulfur ligands. J. Am. Chem. Soc. 118, 9194-9195.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 9194-9195
    • Brennan, B.A.1    Alms, G.2    Nelson, M.3    Durney, L.T.4    Scarrow, R.C.5
  • 23
    • 0031924251 scopus 로고    scopus 로고
    • Cloning of genes coding for the three subunits of thiocyanate hydrolase of Thiobacillus thioparus THI115 and their evolutionary relationships to nitrile hydratase
    • 23. Katayama, Y, Matsushita, Y., Kaneko, M., Kondo, M., Mizuno, T. & Nyunoya, H. (1998) Cloning of genes coding for the three subunits of thiocyanate hydrolase of Thiobacillus thioparus THI115 and their evolutionary relationships to nitrile hydratase. J. Bacteriol. 180, 2583-2589.
    • (1998) J. Bacteriol. , vol.180 , pp. 2583-2589
    • Katayama, Y.1    Matsushita, Y.2    Kaneko, M.3    Kondo, M.4    Mizuno, T.5    Nyunoya, H.6
  • 24
    • 0029913827 scopus 로고    scopus 로고
    • Characterization of the gene cluster of high-molecular-mass nilrile hydratase (H-NHase) induced by its reaction product in Rhodococcus rhodochrous J1
    • 24. Komeda, H., Kobayashi, M. & Shimizu, S. (1996) Characterization of the gene cluster of high-molecular-mass nilrile hydratase (H-NHase) induced by its reaction product in Rhodococcus rhodochrous J1. Proc. Natl Acad. Sci. USA 93, 4267-4272.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 4267-4272
    • Komeda, H.1    Kobayashi, M.2    Shimizu, S.3
  • 25
    • 0029984895 scopus 로고    scopus 로고
    • A novel gene cluster including the Rhodococcus rhodochrous JI nhlBA genes encoding a low molecular mass nitrile hydratase (L-NHase) induced by its reaction product
    • 25. Komeda, H., Kobayashi, M. & Shimizu, S. (1996) A novel gene cluster including the Rhodococcus rhodochrous JI nhlBA genes encoding a low molecular mass nitrile hydratase (L-NHase) induced by its reaction product. J. Biol. Chem. 271, 15796-15802.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15796-15802
    • Komeda, H.1    Kobayashi, M.2    Shimizu, S.3
  • 26
    • 0030296682 scopus 로고    scopus 로고
    • Cobalt-dependent transcription of the nitrile hydratase gene in Rhodococcus rhodochrous M8
    • 26. Pogorelova, T.E., Ryabchenko, L.E., Sunzov, N.I. & Yanenko, A.S. (1996) Cobalt-dependent transcription of the nitrile hydratase gene in Rhodococcus rhodochrous M8. FEMS Microbiol. Lett. 144, 191-195.
    • (1996) FEMS Microbiol. Lett. , vol.144 , pp. 191-195
    • Pogorelova, T.E.1    Ryabchenko, L.E.2    Sunzov, N.I.3    Yanenko, A.S.4
  • 27
    • 0027183546 scopus 로고
    • Transition metals in control of gene expression
    • 27. O'Halloran, T.V. (1993) Transition metals in control of gene expression. Science 261, 715-725.
    • (1993) Science , vol.261 , pp. 715-725
    • O'Halloran, T.V.1
  • 28
    • 0029998291 scopus 로고    scopus 로고
    • Molecular and industrial aspects of glucose isomerase
    • 28. Bhosale, S.H., Rao, M.B. &Deshpande, V.V. (1996) Molecular and industrial aspects of glucose isomerase. Microbiol. Rev. 60, 280-300.
    • (1996) Microbiol. Rev. , vol.60 , pp. 280-300
    • Bhosale, S.H.1    Rao, M.B.2    Deshpande, V.V.3
  • 29
    • 84948020932 scopus 로고
    • Studies on sugar isomerisation enzyme: Production and utilization of glucose isomerase from Streptomyces spp
    • 29. Takasaki, Y. & Tanabe, O. (1966) Studies on sugar isomerisation enzyme: Production and utilization of glucose isomerase from Streptomyces spp. Agric. Biol. Chem. 30, 1247-1253.
    • (1966) Agric. Biol. Chem. , vol.30 , pp. 1247-1253
    • Takasaki, Y.1    Tanabe, O.2
  • 31
    • 0027394809 scopus 로고
    • Characterization of the inducible nickel and cobalt resistance determinant cnr from pMOL28 of Alcaligenes eutrophus CH34
    • 31. Liesegang, H., Lemke, K., Siddiqui, R.A. & Schlegel, H.G. (1993) Characterization of the inducible nickel and cobalt resistance determinant cnr from pMOL28 of Alcaligenes eutrophus CH34. J. Bacteriol. 175, 767-778.
    • (1993) J. Bacteriol. , vol.175 , pp. 767-778
    • Liesegang, H.1    Lemke, K.2    Siddiqui, R.A.3    Schlegel, H.G.4
  • 32
    • 0026707878 scopus 로고
    • COT1, a gene involved in cobalt accumulation in Saccharomyces cerevisiae
    • 32. Conklin, D.S., McMaster, J.A., Culbertson, M.R. & Kung, C. (1992) COT1, a gene involved in cobalt accumulation in Saccharomyces cerevisiae. Mol. Cell. Biol. 12, 3678-3688.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3678-3688
    • Conklin, D.S.1    McMaster, J.A.2    Culbertson, M.R.3    Kung, C.4
  • 33
    • 0028095510 scopus 로고
    • Interactions between gene products involved in divalent cation transport in Saccharomyces cerevisiae
    • 33. Conklin, D.S., Culbertson, M.R. & Kung, C. (1994) Interactions between gene products involved in divalent cation transport in Saccharomyces cerevisiae. Mol. Gen. Genet. 244, 303-311.
    • (1994) Mol. Gen. Genet. , vol.244 , pp. 303-311
    • Conklin, D.S.1    Culbertson, M.R.2    Kung, C.3
  • 34
    • 0030611269 scopus 로고    scopus 로고
    • 2+ binding motif is the basis of high affinity transport of the Alcaligenes eutrophus nickel permease
    • 2+ binding motif is the basis of high affinity transport of the Alcaligenes eutrophus nickel permease. J. Biol Chem. 272, 17139-17144.
    • (1997) J. Biol Chem. , vol.272 , pp. 17139-17144
    • Eitinger, T.1    Wolfram, L.2    Degen, O.3    Anthon, C.4
  • 35
    • 0031982679 scopus 로고    scopus 로고
    • Conserved residues and motifs in the NixA protein of Helicobacter pylori are critical for the high affinity transport of nickel ions
    • 35. Fulkerson, J.F. Jr, Garner, R.M. & Mobley, H.L. (1998) Conserved residues and motifs in the NixA protein of Helicobacter pylori are critical for the high affinity transport of nickel ions. J. Biol. Chem. 273, 235-241.
    • (1998) J. Biol. Chem. , vol.273 , pp. 235-241
    • Fulkerson J.F., Jr.1    Garner, R.M.2    Mobley, H.L.3
  • 36
    • 0024357496 scopus 로고
    • Metal ion uptake by a plasmid-free metal-sensitive Alcaligenes eutrophus strain
    • 36. Nies, D.H. & Silver, S. (1989) Metal ion uptake by a plasmid-free metal-sensitive Alcaligenes eutrophus strain. J. Bacteriol. 171, 4073-4075.
    • (1989) J. Bacteriol. , vol.171 , pp. 4073-4075
    • Nies, D.H.1    Silver, S.2
  • 37
    • 0027193293 scopus 로고
    • Sequence and topology of the CorA magnesium transport systems of Salmonella typhimurium and Escherichia coli: Identification of a new class of transport protein
    • 37. Smith, R.L., Banks, J.L., Snavely, M.D. & Maguire, M.E. (1993) Sequence and topology of the CorA magnesium transport systems of Salmonella typhimurium and Escherichia coli: identification of a new class of transport protein. J. Biol. Chem. 268, 14071-14080.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14071-14080
    • Smith, R.L.1    Banks, J.L.2    Snavely, M.D.3    Maguire, M.E.4
  • 38
    • 0028245449 scopus 로고
    • Bacterial genes involved in incorporation of nickel into a hydrogenase enzyme
    • 38. Fu, C., Javedan, S., Moshiri, F. & Maier, R.J. (1994) Bacterial genes involved in incorporation of nickel into a hydrogenase enzyme. Proc. Natl Acad. Sci. USA 91, 5099-5103.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 5099-5103
    • Fu, C.1    Javedan, S.2    Moshiri, F.3    Maier, R.J.4
  • 39
    • 0020477474 scopus 로고
    • Stabilization of the quaternary structure of transcarboxylase by cobalt (II) ions
    • 39. Harmon, F.R., Goss, N.H. & Wood, H.G. (1982) Stabilization of the quaternary structure of transcarboxylase by cobalt (II) ions. Biochemistry 21, 2847-2852.
    • (1982) Biochemistry , vol.21 , pp. 2847-2852
    • Harmon, F.R.1    Goss, N.H.2    Wood, H.G.3
  • 40
    • 0016390537 scopus 로고
    • Electron and nuclear magnetic resonance studies of the interaction of pyruvate with transcarboxylase
    • 40. Fung, C.-H., Mildvan, A.S. & Leigh, J.S. Jr (1974) Electron and nuclear magnetic resonance studies of the interaction of pyruvate with transcarboxylase. Biochemistry 13, 1160-1169.
    • (1974) Biochemistry , vol.13 , pp. 1160-1169
    • Fung, C.-H.1    Mildvan, A.S.2    Leigh J.S., Jr.3
  • 41
    • 0031732083 scopus 로고    scopus 로고
    • Structural characterization of the entire 1.3S subunit of transcarboxylase from Propionibacterium shermanii
    • 41. Reddy, D.V., Rothemund, S., Shenoy, B.C., Carey, P.R. & Sonnichsen, F.D. (1998) Structural characterization of the entire 1.3S subunit of transcarboxylase from Propionibacterium shermanii. Protein Sci. 7, 2156-2163.
    • (1998) Protein Sci. , vol.7 , pp. 2156-2163
    • Reddy, D.V.1    Rothemund, S.2    Shenoy, B.C.3    Carey, P.R.4    Sonnichsen, F.D.5
  • 42
    • 0028085434 scopus 로고
    • Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase
    • 42. Waldrop, G.L., Rayment, I. & Holden, H.M. (1994) Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase. Biochemistry 33, 10249-10256.
    • (1994) Biochemistry , vol.33 , pp. 10249-10256
    • Waldrop, G.L.1    Rayment, I.2    Holden, H.M.3
  • 43
    • 0026764128 scopus 로고
    • A cobalt-porphyrin enzyme converts a fatty aldehyde to a hydrocarbon and CO
    • 43. Dennis, M. & Kolattukudy, P.E. (1992) A cobalt-porphyrin enzyme converts a fatty aldehyde to a hydrocarbon and CO. Proc. Natl Acad. Sci. USA 89, 5306-5310.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 5306-5310
    • Dennis, M.1    Kolattukudy, P.E.2
  • 44
    • 0029148725 scopus 로고
    • Characterization of a radical intermediate in the lysine 2,3-aminomutase reaction
    • 44. Reed, G.H. & Ballinger, M.D. (1995) Characterization of a radical intermediate in the lysine 2,3-aminomutase reaction. Meth. Enzymol. 258, 362-379.
    • (1995) Meth. Enzymol. , vol.258 , pp. 362-379
    • Reed, G.H.1    Ballinger, M.D.2
  • 46
    • 0026483949 scopus 로고
    • Characterization of iron-sulfur clusters in lysine 2,3-aminomutase by electron paramagnetic resonance spectroscopy
    • 46. Petrovich, R.M., Ruzicka, F.J., Reed, G.H. & Frey, P.A. (1992) Characterization of iron-sulfur clusters in lysine 2,3-aminomutase by electron paramagnetic resonance spectroscopy. Biochemistry 31, 10774-10781.
    • (1992) Biochemistry , vol.31 , pp. 10774-10781
    • Petrovich, R.M.1    Ruzicka, F.J.2    Reed, G.H.3    Frey, P.A.4
  • 47
    • 0027998521 scopus 로고
    • Purification and characterization of a novel metal-containing nonheme bromoperoxidase from Pseudomonas putida
    • 47. Itoh, N., Morinaga, N. & Kouzai, T. (1994) Purification and characterization of a novel metal-containing nonheme bromoperoxidase from Pseudomonas putida. Biochim. Biophys. Acta 1207, 208-216.
    • (1994) Biochim. Biophys. Acta , vol.1207 , pp. 208-216
    • Itoh, N.1    Morinaga, N.2    Kouzai, T.3
  • 48
    • 37049098889 scopus 로고
    • III-isobacteriochlorins: Relationship to the cobalt-containing proteins from Desulphovibrio gigas and Desulphovibrio desulphuricans
    • III-isobacteriochlorins: relationship to the cobalt-containing proteins from Desulphovibrio gigas and Desulphovibrio desulphuricans. J. Chem. Soc. Chem. Commun. 1393-1394.
    • (1982) J. Chem. Soc. Chem. Commun. , pp. 1393-1394
    • Battersby, A.R.1    Sheng, Z.-C.2
  • 50
    • 0019768086 scopus 로고
    • A cobalt porphyrin containing protein reducible by hydrogenase isolated from Desulfovibrio desulfuricans (Norway)
    • 50. Hatchikian, E.C. (1981) A cobalt porphyrin containing protein reducible by hydrogenase isolated from Desulfovibrio desulfuricans (Norway). Biochem. Biophys. Res. Commun. 103, 521-530.
    • (1981) Biochem. Biophys. Res. Commun. , vol.103 , pp. 521-530
    • Hatchikian, E.C.1
  • 51
    • 77049313195 scopus 로고
    • Acetylornithinase of Escherichia coli: Partial purification and some properties
    • 51. Vogel, H.J. & Bonner, D.M. (1956) Acetylornithinase of Escherichia coli: partial purification and some properties. J. Biol. Chem. 218, 97-106.
    • (1956) J. Biol. Chem. , vol.218 , pp. 97-106
    • Vogel, H.J.1    Bonner, D.M.2
  • 52
    • 0028352336 scopus 로고
    • Methanobacterium thermoautotrophicum (strain DH) contains a membrane-bound cyclic 2,3-diphosphoglycerate hydrolase
    • 52. van Alebeek, G.-J.W.M., Kreuwels, M.J.J., Keltjens, J.T. & Vogels, G.D. (1994) Methanobacterium thermoautotrophicum (strain DH) contains a membrane-bound cyclic 2,3-diphosphoglycerate hydrolase. Arch. Microbiol. 161, 514-520.
    • (1994) Arch. Microbiol. , vol.161 , pp. 514-520
    • Van Alebeek, G.-J.W.M.1    Kreuwels, M.J.J.2    Keltjens, J.T.3    Vogels, G.D.4
  • 53
    • 0028178718 scopus 로고
    • Soluble forms of alpha-D-mannosidases from rat liver: Separation and characterization of two enzymic forms with different substrate specificities
    • 53. Grard, T., Saint-Pol, A., Haeuw, J.F., Alonso, C., Wieruszeski, J.M., Strecker, G. & Michalski, J.C. (1994) Soluble forms of alpha-D-mannosidases from rat liver: separation and characterization of two enzymic forms with different substrate specificities. Eur. J. Biochem. 223, 99-106.
    • (1994) Eur. J. Biochem. , vol.223 , pp. 99-106
    • Grard, T.1    Saint-Pol, A.2    Haeuw, J.F.3    Alonso, C.4    Wieruszeski, J.M.5    Strecker, G.6    Michalski, J.C.7
  • 56
    • 0028872551 scopus 로고
    • Occurrence of enzymes involved in biosynthesis of indole-3-acetic acid from indole-3-acetonitrile in plant-associated bacteria, Agrobacterium and Rhizobium
    • 56. Kobayashi, M., Suzuki, T., Fujita, T., Masuda, M. & Shimizu, S. (1995) Occurrence of enzymes involved in biosynthesis of indole-3-acetic acid from indole-3-acetonitrile in plant-associated bacteria, Agrobacterium and Rhizobium. Proc. Natl Acad. Sci. USA 92, 714-718.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 714-718
    • Kobayashi, M.1    Suzuki, T.2    Fujita, T.3    Masuda, M.4    Shimizu, S.5
  • 57
    • 0024363273 scopus 로고
    • Primary structure of a nitrile hydratase deduced from the nucleotide sequence of a Rhodococcus species and its expression in Escherichia coli
    • 57. Ikehata, O., Nishiyama, M., Horinouchi, S. & Beppu, T. (1989) Primary structure of a nitrile hydratase deduced from the nucleotide sequence of a Rhodococcus species and its expression in Escherichia coli. Eur. J. Biochem. 181, 563-570.
    • (1989) Eur. J. Biochem. , vol.181 , pp. 563-570
    • Ikehata, O.1    Nishiyama, M.2    Horinouchi, S.3    Beppu, T.4
  • 58
    • 0027651143 scopus 로고
    • Characterization of nitrile hydratase genes cloned by DNA screening from Rhodococcus erythropolis
    • 58. Duran, R., Nishiyama, M., Horinouchi, S. & Beppu. T. (1993) Characterization of nitrile hydratase genes cloned by DNA screening from Rhodococcus erythropolis. Biosci Biotechnol. Biochem. 57, 1323-1328.
    • (1993) Biosci Biotechnol. Biochem. , vol.57 , pp. 1323-1328
    • Duran, R.1    Nishiyama, M.2    Horinouchi, S.3    Beppu, T.4
  • 59
    • 0025761763 scopus 로고
    • Cloning and characterization of genes responsible for metabolism of nitrile compounds from Pseudomonas chlororaphis B23
    • 59. Nishiyama, M., Horinouchi, S., Kobayashi, M., Nagasawa, T., Beppu, T. & Yamada, H. (1991) Cloning and characterization of genes responsible for metabolism of nitrile compounds from Pseudomonas chlororaphis B23. J. Bacteriol. 173, 2465-2472.
    • (1991) J. Bacteriol. , vol.173 , pp. 2465-2472
    • Nishiyama, M.1    Horinouchi, S.2    Kobayashi, M.3    Nagasawa, T.4    Beppu, T.5    Yamada, H.6
  • 60
    • 0025747960 scopus 로고
    • Purification, cloning, and primary structure of a new enantiomer-selective amidase from a Rhodococcus strain: Structural evidence for a conserved genetic coupling with nitrile hydratase
    • 60. Mayaux, J.F., Cerbelaud, E., Soubrier, F., Yeh, P., Blanche, F. & Petre, D. (1991) Purification, cloning, and primary structure of a new enantiomer-selective amidase from a Rhodococcus strain: structural evidence for a conserved genetic coupling with nitrile hydratase. J. Bacteriol. 173, 6694-6704.
    • (1991) J. Bacteriol. , vol.173 , pp. 6694-6704
    • Mayaux, J.F.1    Cerbelaud, E.2    Soubrier, F.3    Yeh, P.4    Blanche, F.5    Petre, D.6


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