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Volumn 125, Issue 4, 1999, Pages 696-704

Functional expression of nitrile hydratase in Escherichia coli: Requirement of a nitrile hydratase activator and post-translational modification of a ligand cysteine

Author keywords

Hydration; Metalloprotein; Nitrile; Overexpression; Post translational modification

Indexed keywords

CYSTEINE; ENZYME ACTIVATOR; IRON; NITRIC OXIDE; NITRILE HYDRATASE; RECOMBINANT ENZYME;

EID: 0032904843     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022339     Document Type: Article
Times cited : (94)

References (40)
  • 1
    • 0026480892 scopus 로고
    • Enzymatic synthesis of acrylamide: A success story not yet over
    • Kobayashi, M., Nagasawa, T., and 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
  • 2
    • 0023229582 scopus 로고
    • Nitrile hydratase: The first non-heme iron enzyme with a typical low-spin Fe(III)-active center
    • Sugiura, Y., Kuwahara, T., Nagasawa, H., and Yamada, H. (1987) Nitrile hydratase: The first non-heme iron enzyme with a typical low-spin Fe(III)-active center. J. Am. Chem. Soc. 109, 5848-5850
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 5848-5850
    • Sugiura, Y.1    Kuwahara, T.2    Nagasawa, H.3    Yamada, H.4
  • 3
    • 0029805756 scopus 로고    scopus 로고
    • Nitrile hydratase from Rhodococcus rhodochrous J1 contains a non-corrinoid cobalt ion with two sulfur ligands
    • Brennan, B.A., Alms, G., Nelson, M.J., Durney, L.T., and Scarrow, R.C. (1996) Nitrile hydratase from Rhodococcus rhodochrous J1 contains a non-corrinoid 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.J.3    Durney, L.T.4    Scarrow, R.C.5
  • 4
    • 0031570299 scopus 로고    scopus 로고
    • Crystal structure of nitrile hydratase reveals. a novel iron centre in a novel fold
    • Huang, W., Jia, J., Cummings, J., Nelson, M., Schneider, G., and 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
  • 6
    • 0028950097 scopus 로고
    • Photosensitive nitrile hydratase intrinsically possesses nitric oxide bound to the non-heme iron center: Evidence by fourier transform infrared spectroscopy
    • Noguchi, T., Honda, J., Nagamune, T., Sasabe, H., Inoue, Y., and Endo, I. (1995) Photosensitive nitrile hydratase intrinsically possesses nitric oxide bound to the non-heme iron center: evidence by fourier transform infrared spectroscopy. FEBS Lett. 358, 9-12
    • (1995) FEBS Lett. , vol.358 , pp. 9-12
    • Noguchi, T.1    Honda, J.2    Nagamune, T.3    Sasabe, H.4    Inoue, Y.5    Endo, I.6
  • 8
    • 0030452421 scopus 로고    scopus 로고
    • Resonance Raman evidence that photodissociation of nitric oxide from the non-heme iron center activates nitrile hydratase from Rhodococcus sp. N-771
    • Noguchi, T., Hoshino, M., Tsujimura, M., Odaka, M., Inoue, Y., and Endo, I. (1996) Resonance Raman evidence that photodissociation of nitric oxide from the non-heme iron center activates nitrile hydratase from Rhodococcus sp. N-771. Biochemistry 35, 16777-16781
    • (1996) Biochemistry , vol.35 , pp. 16777-16781
    • Noguchi, T.1    Hoshino, M.2    Tsujimura, M.3    Odaka, M.4    Inoue, Y.5    Endo, I.6
  • 9
    • 0030968204 scopus 로고    scopus 로고
    • Highly efficient control of iron-containing nitrile hydratases by stoichiometric amounts of nitric oxide and light
    • Bonnet, D., Artaud, I., Moali, C., Petre, D., and Mansuy, D. (1997) Highly efficient control of iron-containing nitrile hydratases by stoichiometric amounts of nitric oxide and light. FEBS Lett. 409, 216-220
    • (1997) FEBS Lett. , vol.409 , pp. 216-220
    • Bonnet, D.1    Artaud, I.2    Moali, C.3    Petre, D.4    Mansuy, D.5
  • 12
    • 0024363273 scopus 로고
    • Primary structure of nitrile hydratase deduced from the nucleotide sequence of a rhodococcus species and its expression in Escherichia coli
    • Ikehata, O., Nishiyama, M., Horinouchi, S., and Beppu, T. (1989) Primary structure of 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
  • 13
    • 0028519939 scopus 로고
    • Nitrile hydratase gene from rhodococcus sp. N-774 requirement for its downstream region for efficient expression
    • Hashimoto, Y., Nishiyama, M., Horinouchi, S., and Beppu, T. (1994) Nitrile hydratase gene from Rhodococcus sp. N-774 requirement for its downstream region for efficient expression. Biosci. Biotechnol. Biochem. 58, 1859-1865
    • (1994) Biosci. Biotechnol. Biochem. , vol.58 , pp. 1859-1865
    • Hashimoto, Y.1    Nishiyama, M.2    Horinouchi, S.3    Beppu, T.4
  • 14
    • 0025761763 scopus 로고
    • Cloning and characterization of genes responsible for metabolism of nitrile compounds from Pseudomonas chlororaphis B23
    • Nishiyama, M., Horinouchi, S., Kobayashi, M., Nagasawa, T., Yamada, H., and Beppu, T. (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    Yamada, H.5    Beppu, T.6
  • 15
    • 0029913827 scopus 로고    scopus 로고
    • Characterization of the gene cluster of high-molecular-mass nitrile hydratase (H-NHase) induced by its reaction product in Rhodococcus rhodochrous J1
    • Komeda, H., Kobayashi, M., and Shimizu, S. (1996) Characterization of the gene cluster of high-molecular-mass nitrile 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
  • 17
    • 0031450886 scopus 로고    scopus 로고
    • Over-production of stereoselective nitrile hydratase from Pseudomonas putida 5B in Escherichia coli: Activity requires a novel downstream protein
    • Wu, S., Fallon, R.D., and Payne, M.S. (1997) Over-production of stereoselective nitrile hydratase from Pseudomonas putida 5B in Escherichia coli: activity requires a novel downstream protein. Appl. Microbiol. Biotechnol. 48, 704-708
    • (1997) Appl. Microbiol. Biotechnol. , vol.48 , pp. 704-708
    • Wu, S.1    Fallon, R.D.2    Payne, M.S.3
  • 18
    • 0028307332 scopus 로고
    • Molecular cloning and nucleotide sequence of the gene coding photosensitive nitrile hydratase
    • Yohda, M., Honda, J., Nagamune, T., Endo, I., Yoshida, T., and Miura, K. (1994) Molecular cloning and nucleotide sequence of the gene coding photosensitive nitrile hydratase. Ann. N.Y. Acad. Sci. 721, 158-159
    • (1994) Ann. N.Y. Acad. Sci. , vol.721 , pp. 158-159
    • Yohda, M.1    Honda, J.2    Nagamune, T.3    Endo, I.4    Yoshida, T.5    Miura, K.6
  • 20
    • 0029738645 scopus 로고    scopus 로고
    • Resonance raman spectroscopy of nitrile hydratase, a novel iron-sulfur enzyme
    • Brennan, B.A., Cummings, J.G., Chase, D.B., Turner, I.M. Jr., and Nelson, M.J. (1996) Resonance raman spectroscopy of nitrile hydratase, a novel iron-sulfur enzyme. Biochemistry 35, 10068-10077
    • (1996) Biochemistry , vol.35 , pp. 10068-10077
    • Brennan, B.A.1    Cummings, J.G.2    Chase, D.B.3    Turner I.M., Jr.4    Nelson, M.J.5
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 1842327489 scopus 로고    scopus 로고
    • Genes encoding the NAD-reducing hydrogenase of Rhodococcus opacus MR11
    • Grzeszik, C., Lubbers, M., Reh, M., and Schlegel, H.G. (1997) Genes encoding the NAD-reducing hydrogenase of Rhodococcus opacus MR11. Microbiology 143, 1271-1286
    • (1997) Microbiology , vol.143 , pp. 1271-1286
    • Grzeszik, C.1    Lubbers, M.2    Reh, M.3    Schlegel, H.G.4
  • 24
    • 0029984895 scopus 로고    scopus 로고
    • A novel gene cluster including the Rhodococcus rhodochrous J1 nhlBA genes encoding a low molecular mass nitrile hydratase (L-NHase) induced by its reaction product
    • Komeda, H., Kobayashi, M., and Shimizu, S. (1996) A novel gene cluster including the Rhodococcus rhodochrous J1 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
  • 25
    • 0026328061 scopus 로고
    • Cloning and DNA sequence of amiC, a new gene regulating expression of the Pseudomonas aeruginosa aliphatic amidase, and purification of the amic product
    • Wilson, S. and Drew, R. (1991) Cloning and DNA sequence of amiC, a new gene regulating expression of the Pseudomonas aeruginosa aliphatic amidase, and purification of the amiC product. J. Bacteriol. 173, 4914-4921
    • (1991) J. Bacteriol. , vol.173 , pp. 4914-4921
    • Wilson, S.1    Drew, R.2
  • 27
    • 0029962401 scopus 로고    scopus 로고
    • Photoreactive nitrile hydratase: The photoreaction site is located on the a subunit
    • Tsujimura, M., Odaka, M., Nagashima, S., Yohda, M., and Endo, I. (1996) Photoreactive nitrile hydratase: the photoreaction site is located on the a subunit. J. Biochem. 119, 407-413
    • (1996) J. Biochem. , vol.119 , pp. 407-413
    • Tsujimura, M.1    Odaka, M.2    Nagashima, S.3    Yohda, M.4    Endo, I.5
  • 29
    • 0028822799 scopus 로고
    • An iron-regulated gene, magA, encoding an iron transport protein of Magnetospirillum sp. strain AMB-1
    • Nakamura, C., Burgess, J.G., Sode, K., and Matsunaga, T. (1995) An iron-regulated gene, magA, encoding an iron transport protein of Magnetospirillum sp. strain AMB-1. J. Biol. Chem. 270, 28392-28396
    • (1995) J. Biol. Chem. , vol.270 , pp. 28392-28396
    • Nakamura, C.1    Burgess, J.G.2    Sode, K.3    Matsunaga, T.4
  • 31
    • 0030805135 scopus 로고    scopus 로고
    • The oxidation of selenocysteine is involved in the inactivation of glutathione peroxidase by nitric oxide donor
    • Asahi, M., Fujii, J., Takao, T., Kuzuya, T., Hori, M., Shimonishi, Y., and Taniguchi, N. (1997) The oxidation of selenocysteine is involved in the inactivation of glutathione peroxidase by nitric oxide donor. J. Biol. Chem. 272, 19152-19157
    • (1997) J. Biol. Chem. , vol.272 , pp. 19152-19157
    • Asahi, M.1    Fujii, J.2    Takao, T.3    Kuzuya, T.4    Hori, M.5    Shimonishi, Y.6    Taniguchi, N.7
  • 33
    • 0029039754 scopus 로고
    • Peroxynitrite-mediated oxidative protein modifications
    • Ischiropoulos, H. and Al-Mehdi, A.B. (1995) Peroxynitrite-mediated oxidative protein modifications. FEBS Lett. 364, 279-282
    • (1995) FEBS Lett. , vol.364 , pp. 279-282
    • Ischiropoulos, H.1    Al-Mehdi, A.B.2
  • 34
    • 0029160661 scopus 로고
    • Reaction of nitric oxide with the free sulfhydryl group of human serum albumin yields a sulfenic acid and nitrous oxide
    • DeMaster, E.G., Quast, B.J., Redfern, B., and Nagasawa, H.T. (1995) Reaction of nitric oxide with the free sulfhydryl group of human serum albumin yields a sulfenic acid and nitrous oxide. Biochemistry 34, 11494-11499
    • (1995) Biochemistry , vol.34 , pp. 11494-11499
    • DeMaster, E.G.1    Quast, B.J.2    Redfern, B.3    Nagasawa, H.T.4
  • 36
    • 0028033732 scopus 로고
    • Human cysteine dioxygenase type I: Primary structure derived from base sequencing of cDNA
    • McCann, K.P., Akbari, M.T., Williams, A.C., and Ramsden, D.B. (1994) Human cysteine dioxygenase type I: primary structure derived from base sequencing of cDNA. Biochim. Biophys. Acta 1209, 107-110
    • (1994) Biochim. Biophys. Acta , vol.1209 , pp. 107-110
    • McCann, K.P.1    Akbari, M.T.2    Williams, A.C.3    Ramsden, D.B.4
  • 37
    • 0027965409 scopus 로고
    • Generation of the topa quinone cofactor in bacterial monoamine oxidase by cupric ion-dependent autooxidation of a specific tyrosyl residue
    • Matsuzaki, R., Fukui, T., Sato, H., Ozaki, Y., and Tanizawa, K. (1994) Generation of the topa quinone cofactor in bacterial monoamine oxidase by cupric ion-dependent autooxidation of a specific tyrosyl residue. FEBS Lett. 351, 360-364
    • (1994) FEBS Lett. , vol.351 , pp. 360-364
    • Matsuzaki, R.1    Fukui, T.2    Sato, H.3    Ozaki, Y.4    Tanizawa, K.5
  • 38
    • 0028914513 scopus 로고
    • Spectroscopic studies on the mechanism of the topa quinone generation in bacterial monoamine oxidase
    • Matsuzaki, R., Suzuki, S., Yamaguchi, K., Fukui, T., and Tanizawa, K. (1995) Spectroscopic studies on the mechanism of the topa quinone generation in bacterial monoamine oxidase. Biochemistry 34, 4524-4530
    • (1995) Biochemistry , vol.34 , pp. 4524-4530
    • Matsuzaki, R.1    Suzuki, S.2    Yamaguchi, K.3    Fukui, T.4    Tanizawa, K.5
  • 40
    • 0028245290 scopus 로고
    • Copper amine oxidase: Heterologous expression, purification, and characterization of an active enzyme in Saccharomyces cerevisiae
    • Cai, D. and Klinman, J.P. (1994) Copper amine oxidase: heterologous expression, purification, and characterization of an active enzyme in Saccharomyces cerevisiae. Biochemistry 33, 7647-7653
    • (1994) Biochemistry , vol.33 , pp. 7647-7653
    • Cai, D.1    Klinman, J.P.2


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