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Volumn 43, Issue 12, 2008, Pages 1391-1397

Nitrile hydratase from Mesorhizobium sp. F28 and its potential for nitrile biotransformation

Author keywords

Acrylamide; Acrylonitrile; Biotransformation; Mesorhizobium sp.; Nitrile; Nitrile hydratase

Indexed keywords

AMIDES; COBALT; CYANIDES; METAL REFINING; TRANSITION METALS; WASTEWATER; WASTEWATER RECLAMATION; WATER TREATMENT;

EID: 54949120157     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2008.08.009     Document Type: Article
Times cited : (25)

References (43)
  • 2
    • 0001589229 scopus 로고    scopus 로고
    • Microbial metabolism of nitriles and its biotechnological potential
    • Ramakrishna C., Dave H., and Ravindranathan M. Microbial metabolism of nitriles and its biotechnological potential. J Sci Ind Res 58 (1999) 925-947
    • (1999) J Sci Ind Res , vol.58 , pp. 925-947
    • Ramakrishna, C.1    Dave, H.2    Ravindranathan, M.3
  • 3
    • 0000020934 scopus 로고
    • A new enzyme "nitrile hydratase" which degrades acetonitrile in combination with amidase
    • Asano Y., Tani Y., and Yamada H. A new enzyme "nitrile hydratase" which degrades acetonitrile in combination with amidase. Agric Biol Chem 44 (1980) 2251-2252
    • (1980) Agric Biol Chem , vol.44 , pp. 2251-2252
    • Asano, Y.1    Tani, Y.2    Yamada, H.3
  • 4
    • 0024970709 scopus 로고
    • Nitrilase of Rhodococcus rhodochrous J1. Purification and characterization
    • Kobayashi M., Nagasawa T., and Yamada H. Nitrilase of Rhodococcus rhodochrous J1. Purification and characterization. Eur J Biochem 182 (1989) 349-356
    • (1989) Eur J Biochem , vol.182 , pp. 349-356
    • Kobayashi, M.1    Nagasawa, T.2    Yamada, H.3
  • 6
    • 0033152216 scopus 로고    scopus 로고
    • An enzyme controlled by light: the molecular mechanism of photoreactivity in nitrile hydratase
    • Endo I., Odaka M., and Yohda M. An enzyme controlled by light: the molecular mechanism of photoreactivity in nitrile hydratase. Trends Biotechnol 17 (1999) 244-249
    • (1999) Trends Biotechnol , vol.17 , pp. 244-249
    • Endo, I.1    Odaka, M.2    Yohda, M.3
  • 7
    • 0039466853 scopus 로고    scopus 로고
    • Nitrile hydratase involved in aldoxime metabolism from Rhodococcus sp. strain YH3-3: purification and characterization
    • Kato Y., Tsuda T., and Asano Y. Nitrile hydratase involved in aldoxime metabolism from Rhodococcus sp. strain YH3-3: purification and characterization. Eur J Biochem 263 (1999) 662-670
    • (1999) Eur J Biochem , vol.263 , pp. 662-670
    • Kato, Y.1    Tsuda, T.2    Asano, Y.3
  • 8
    • 11844278551 scopus 로고    scopus 로고
    • Treatment of wastewater containing toxic amides by immobilized Rhodococcus rhodochrous NHB-2 using a highly compact five-stage plug flow reactor
    • Chand D., Kumar H., Sankhian U.D., Kumar D., Vitzthum F., and Bhalla T.C. Treatment of wastewater containing toxic amides by immobilized Rhodococcus rhodochrous NHB-2 using a highly compact five-stage plug flow reactor. World J Microbiol Biotechnol 20 (2004) 679-686
    • (2004) World J Microbiol Biotechnol , vol.20 , pp. 679-686
    • Chand, D.1    Kumar, H.2    Sankhian, U.D.3    Kumar, D.4    Vitzthum, F.5    Bhalla, T.C.6
  • 9
    • 33747726384 scopus 로고    scopus 로고
    • Convenient treatment of acetonitrile-containing wastes using the tandem combination of nitrile hydratase and amidase-producing microorganisms
    • Kohyama E., Yoshimura A., Aoshima D., Yoshida T., Kawamoto H., and Nagasawa T. Convenient treatment of acetonitrile-containing wastes using the tandem combination of nitrile hydratase and amidase-producing microorganisms. Appl Microbiol Biotechnol 72 (2006) 600-606
    • (2006) Appl Microbiol Biotechnol , vol.72 , pp. 600-606
    • Kohyama, E.1    Yoshimura, A.2    Aoshima, D.3    Yoshida, T.4    Kawamoto, H.5    Nagasawa, T.6
  • 10
    • 2442522450 scopus 로고    scopus 로고
    • A study in UF-membrane reactor on activity and stability of nitrile hydratase from Microbacterium imperiale CBS 498-74 resting cells for propionamide production
    • Cantarella M., Cantarella L., Gallifuoco A., Frezzini R., Spera A., and Alfani F. A study in UF-membrane reactor on activity and stability of nitrile hydratase from Microbacterium imperiale CBS 498-74 resting cells for propionamide production. J Mol Catal B: Enzym 29 (2004) 105-113
    • (2004) J Mol Catal B: Enzym , vol.29 , pp. 105-113
    • Cantarella, M.1    Cantarella, L.2    Gallifuoco, A.3    Frezzini, R.4    Spera, A.5    Alfani, F.6
  • 11
    • 33746908959 scopus 로고    scopus 로고
    • Enantioselective biotransformations of nitriles in organic synthesis
    • Wang M.X. Enantioselective biotransformations of nitriles in organic synthesis. Top Catal 35 (2005) 117-130
    • (2005) Top Catal , vol.35 , pp. 117-130
    • Wang, M.X.1
  • 12
    • 17044374655 scopus 로고    scopus 로고
    • Nitrile biotransformations for highly enantioselective synthesis of oxiranecarboxamides with tertiary and quaternary stereocenters; efficient chemoenzymatic approaches to enantiopure α-methylated serine and isoserine derivatives
    • Wang M.X., Deng G., Wang D.X., and Zheng Q.Y. Nitrile biotransformations for highly enantioselective synthesis of oxiranecarboxamides with tertiary and quaternary stereocenters; efficient chemoenzymatic approaches to enantiopure α-methylated serine and isoserine derivatives. J Org Chem 70 (2005) 2439-2444
    • (2005) J Org Chem , vol.70 , pp. 2439-2444
    • Wang, M.X.1    Deng, G.2    Wang, D.X.3    Zheng, Q.Y.4
  • 13
    • 33947279549 scopus 로고    scopus 로고
    • Nitrile biotransformations for the efficient synthesis of highly enantiopure 1-arylaziridine-2-carboxylic acid derivatives and their stereoselective ring-opening reactions
    • Wang J.Y., Wang D.X., Zheng Q.Y., Huang Z.T., and Wang M.X. Nitrile biotransformations for the efficient synthesis of highly enantiopure 1-arylaziridine-2-carboxylic acid derivatives and their stereoselective ring-opening reactions. J Org Chem 72 (2007) 2040-2045
    • (2007) J Org Chem , vol.72 , pp. 2040-2045
    • Wang, J.Y.1    Wang, D.X.2    Zheng, Q.Y.3    Huang, Z.T.4    Wang, M.X.5
  • 14
    • 34547619996 scopus 로고    scopus 로고
    • Remarkable electronic and steric effects in the nitrile biotransformations for the preparation of enantiopure functionalized carboxylic acids and amides: implication for an unsaturated carbon-carbon bond binding domain of the amidase
    • Gao M., Wang D.X., Zheng Q.X., Huang Z.T., and Wang M.X. Remarkable electronic and steric effects in the nitrile biotransformations for the preparation of enantiopure functionalized carboxylic acids and amides: implication for an unsaturated carbon-carbon bond binding domain of the amidase. J Org Chem 72 (2007) 6060-6066
    • (2007) J Org Chem , vol.72 , pp. 6060-6066
    • Gao, M.1    Wang, D.X.2    Zheng, Q.X.3    Huang, Z.T.4    Wang, M.X.5
  • 15
    • 0021971186 scopus 로고
    • A new medium for the enumeration and subculture of bacteria from potable water
    • Reasoner D.J., and Geldreich E.E. A new medium for the enumeration and subculture of bacteria from potable water. Appl Environ Microbiol 49 1 (1985) 1-7
    • (1985) Appl Environ Microbiol , vol.49 , Issue.1 , pp. 1-7
    • Reasoner, D.J.1    Geldreich, E.E.2
  • 16
    • 0023676808 scopus 로고
    • Conversion of cyanide to formate and ammonia by a pseudomonad obtained from industrial wastewater
    • White J.M., Jones D.D., Huang D., and Gauthier J.J. Conversion of cyanide to formate and ammonia by a pseudomonad obtained from industrial wastewater. J Ind Microbiol 3 (1988) 263-272
    • (1988) J Ind Microbiol , vol.3 , pp. 263-272
    • White, J.M.1    Jones, D.D.2    Huang, D.3    Gauthier, J.J.4
  • 18
    • 0031970018 scopus 로고    scopus 로고
    • Molecular investigation of a microbial mat associated with the great artesian basin
    • Byers H.K., Stackebrandt E., Hayward C., and Blackall L.L. Molecular investigation of a microbial mat associated with the great artesian basin. FEMS Microbiol Ecol 25 (1998) 391-403
    • (1998) FEMS Microbiol Ecol , vol.25 , pp. 391-403
    • Byers, H.K.1    Stackebrandt, E.2    Hayward, C.3    Blackall, L.L.4
  • 19
    • 0000918060 scopus 로고
    • Indophenol-blue method
    • Page A.L., Miller R.H., and Keeney D.R. (Eds), Chemical and Microbiological Properties
    • Keeney D.R., and Nelson D.W. Indophenol-blue method. In: Page A.L., Miller R.H., and Keeney D.R. (Eds). Methods of soil analysis. Part 2. second edition (1982), Chemical and Microbiological Properties 674-676
    • (1982) Methods of soil analysis. Part 2. second edition , pp. 674-676
    • Keeney, D.R.1    Nelson, D.W.2
  • 20
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein-dye-binding
    • Bradford M.M. A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein-dye-binding. Anal Biochem 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 21
    • 0027378489 scopus 로고
    • The superiority of the third-generation catalyst Rhodococcus rhodochrous J1 nitrile hydratase for industrial production of acrylamide
    • Nagasawa T., Shimizu H., and Yamada H. The superiority of the third-generation catalyst Rhodococcus rhodochrous J1 nitrile hydratase for industrial production of acrylamide. Appl Microbiol Biotechnol 40 (1993) 189-195
    • (1993) Appl Microbiol Biotechnol , vol.40 , pp. 189-195
    • Nagasawa, T.1    Shimizu, H.2    Yamada, H.3
  • 22
    • 21644435403 scopus 로고    scopus 로고
    • Rhodococcus pyridinovorans MW3, a bacterium producing a nitrile hydratase
    • Precigou S., Wieser M., Pommares P., Goulas P., and Duran R. Rhodococcus pyridinovorans MW3, a bacterium producing a nitrile hydratase. Biotechnol Lett 26 (2004) 1379-1384
    • (2004) Biotechnol Lett , vol.26 , pp. 1379-1384
    • Precigou, S.1    Wieser, M.2    Pommares, P.3    Goulas, P.4    Duran, R.5
  • 23
    • 0037010701 scopus 로고    scopus 로고
    • Influence of initial glucose concentration on nitrile hydratase production in Brevibacterium imperialis CBS 498-74
    • Cantarella M., Spera A., Leonetti P., and Alfani F. Influence of initial glucose concentration on nitrile hydratase production in Brevibacterium imperialis CBS 498-74. J Mol Catal B: Enzym 19/20 (2002) 405-414
    • (2002) J Mol Catal B: Enzym , vol.19-20 , pp. 405-414
    • Cantarella, M.1    Spera, A.2    Leonetti, P.3    Alfani, F.4
  • 24
    • 33646076734 scopus 로고    scopus 로고
    • Rhodococcus rhodochrous PA-34: a potential biocatalyst for acrylamide synthesis
    • Raj J., Prasad S., and Bhalla T.C. Rhodococcus rhodochrous PA-34: a potential biocatalyst for acrylamide synthesis. Process Biochem 41 (2006) 1359-1363
    • (2006) Process Biochem , vol.41 , pp. 1359-1363
    • Raj, J.1    Prasad, S.2    Bhalla, T.C.3
  • 25
    • 0024288701 scopus 로고
    • Occurrence of a cobalt-induced and cobalt-containing nitrile hydratase in Rhodococcus rhodochrous J1
    • Nagasawa T., Takeuchi K., and Yamada H. Occurrence of a cobalt-induced and cobalt-containing nitrile hydratase in Rhodococcus rhodochrous J1. Biochem Biophys Res Commun 155 (1991) 1008-1016
    • (1991) Biochem Biophys Res Commun , vol.155 , pp. 1008-1016
    • Nagasawa, T.1    Takeuchi, K.2    Yamada, H.3
  • 26
    • 0025644814 scopus 로고
    • Production of acrylic acid and methacrylic acid using Rhodococcus rhodochrous J1 nitrilase
    • Nagasawa T., Nakamura T., and Yamada H. Production of acrylic acid and methacrylic acid using Rhodococcus rhodochrous J1 nitrilase. Appl Microbiol Biotechnol 34 (1990) 322-324
    • (1990) Appl Microbiol Biotechnol , vol.34 , pp. 322-324
    • Nagasawa, T.1    Nakamura, T.2    Yamada, H.3
  • 28
    • 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
    • Kobayashi M., Suzuki T., Fujita T., Masuda M., and Shimizu S. Occurrence of enzymes involved in biosynthesis of indole-3-acetic acid from indole-3-acetonitrile in plant associated bacteria, Agrobacterium and Rhizobium. PNAS 92 (1995) 714-718
    • (1995) PNAS , vol.92 , pp. 714-718
    • Kobayashi, M.1    Suzuki, T.2    Fujita, T.3    Masuda, M.4    Shimizu, S.5
  • 31
    • 54949134120 scopus 로고    scopus 로고
    • Lourenco PML, Almeida T, Mendonca D, Simoes F, Novo C. Nitrile hydratase from Agrobacterium tumefaciens-sequence and structure. EMBL/GenBank/DDBJ databases accession number AJ548497.
    • Lourenco PML, Almeida T, Mendonca D, Simoes F, Novo C. Nitrile hydratase from Agrobacterium tumefaciens-sequence and structure. EMBL/GenBank/DDBJ databases accession number AJ548497.
  • 32
    • 0345276480 scopus 로고    scopus 로고
    • Crystal structure of nitrile hydratase from a thermophilic Bacillus smithii
    • Hourai S., Miki M., Takashima Y., Mitsuda S., and Yanagi K. Crystal structure of nitrile hydratase from a thermophilic Bacillus smithii. Biochem Biophys Res Commun 312 2 (2003) 340-345
    • (2003) Biochem Biophys Res Commun , vol.312 , Issue.2 , pp. 340-345
    • Hourai, S.1    Miki, M.2    Takashima, Y.3    Mitsuda, S.4    Yanagi, K.5
  • 33
    • 0030944711 scopus 로고    scopus 로고
    • Cloning and sequencing of a nitrile hydratase gene from Pseudonocardia thermophila JCM3095
    • Yamaki T., Oikawa T., Ito K., and Nakamura T. Cloning and sequencing of a nitrile hydratase gene from Pseudonocardia thermophila JCM3095. J Ferment Bioeng 83 (1997) 474-477
    • (1997) J Ferment Bioeng , vol.83 , pp. 474-477
    • Yamaki, T.1    Oikawa, T.2    Ito, K.3    Nakamura, T.4
  • 34
    • 0027651143 scopus 로고
    • Characterization of nitrile hydratase genes cloned by DNA screening from Rhodococcus erythropolis
    • Duran R., Nishiyama M., Horinouchi S., and Beppu T. Characterization of nitrile hydratase genes cloned by DNA screening from Rhodococcus erythropolis. Biosci Biotechnol Biochem 57 8 (1993) 1323-1328
    • (1993) Biosci Biotechnol Biochem , vol.57 , Issue.8 , pp. 1323-1328
    • Duran, R.1    Nishiyama, M.2    Horinouchi, S.3    Beppu, T.4
  • 35
    • 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. Cloning and characterization of genes responsible for metabolism of nitrile compounds from Pseudomonas chlororaphis B23. J Bacteriol 173 8 (1991) 2465-2472
    • (1991) J Bacteriol , vol.173 , Issue.8 , pp. 2465-2472
    • Nishiyama, M.1    Horinouchi, S.2    Kobayashi, M.3    Nagasawa, T.4    Yamada, H.5    Beppu, T.6
  • 36
    • 0027057954 scopus 로고
    • Photosensitive nitrile hydratase from Rhodococcus sp. N-771. Structure and function of the enzyme
    • Honda J., Nagamune T., Teratani Y., Hirata A., Sasabe H., and Endo I. Photosensitive nitrile hydratase from Rhodococcus sp. N-771. Structure and function of the enzyme. Ann NY Acad Sci 672 (1992) 29-36
    • (1992) Ann NY Acad Sci , vol.672 , pp. 29-36
    • Honda, J.1    Nagamune, T.2    Teratani, Y.3    Hirata, A.4    Sasabe, H.5    Endo, I.6
  • 37
    • 52049088940 scopus 로고    scopus 로고
    • Biochemical characterization of Rhodococcus erythropolis N′4 nitrile hydratase acting on 4-chloro-3-hydroxybutyronitrile
    • Choi Y.H., Uhm K.N., and Kim H.K. Biochemical characterization of Rhodococcus erythropolis N′4 nitrile hydratase acting on 4-chloro-3-hydroxybutyronitrile. J Mol Catal B: Enzym 55 (2008) 157-163
    • (2008) J Mol Catal B: Enzym , vol.55 , pp. 157-163
    • Choi, Y.H.1    Uhm, K.N.2    Kim, H.K.3
  • 38
    • 0025962966 scopus 로고
    • Characterisation of a new cobalt-containing nitrile hydratase purified from urea-induced cells of Rhodococcus rhodochrous J1
    • Nagasawa T., Takeuchi K., and Yamada H. Characterisation of a new cobalt-containing nitrile hydratase purified from urea-induced cells of Rhodococcus rhodochrous J1. Eur J Biochem 196 (1991) 581-589
    • (1991) Eur J Biochem , vol.196 , pp. 581-589
    • Nagasawa, T.1    Takeuchi, K.2    Yamada, H.3
  • 39
    • 0032934512 scopus 로고    scopus 로고
    • Molecular characterization of a novel thermophilic nitrile hydratase
    • Cramp R.A., and Cowan D.A. Molecular characterization of a novel thermophilic nitrile hydratase. Biochim Biophys Acta 1431 (1999) 249-260
    • (1999) Biochim Biophys Acta , vol.1431 , pp. 249-260
    • Cramp, R.A.1    Cowan, D.A.2
  • 40
    • 0025729807 scopus 로고
    • Isolation and properties of a nitrile hydratase from the soil fungus Myrothecium verrucaria that is highly specific for the fertilizer cyanamide and cloning of its gene
    • Maier-Greiner U.H., Obermaier-Skrobranek B.M.M., Estermaier L.M., Kammerloher W., Freund C., Wulfing C., et al. Isolation and properties of a nitrile hydratase from the soil fungus Myrothecium verrucaria that is highly specific for the fertilizer cyanamide and cloning of its gene. PNAS 88 (1991) 4260-4264
    • (1991) PNAS , vol.88 , pp. 4260-4264
    • Maier-Greiner, U.H.1    Obermaier-Skrobranek, B.M.M.2    Estermaier, L.M.3    Kammerloher, W.4    Freund, C.5    Wulfing, C.6
  • 43
    • 0031734072 scopus 로고    scopus 로고
    • Low-molecular-mass nitrile hydratase from Rhodococcus rhodochrous J1: purification, substrate specificity and comparison with the analogous high-molecular-mass enzyme
    • Wieser M., Takeuchi K., Wada Y., Yamada H., and Nagasawa T. Low-molecular-mass nitrile hydratase from Rhodococcus rhodochrous J1: purification, substrate specificity and comparison with the analogous high-molecular-mass enzyme. FEMS Microbiol Lett 169 (1998) 17-22
    • (1998) FEMS Microbiol Lett , vol.169 , pp. 17-22
    • Wieser, M.1    Takeuchi, K.2    Wada, Y.3    Yamada, H.4    Nagasawa, T.5


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