메뉴 건너뛰기




Volumn 75, Issue 17, 2009, Pages 5592-5599

Identification of amino acid residues responsible for the enantioselectivity and amide formation capacity of the arylacetonitrilase from Pseudomonas fluorescens EBC191

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE RESIDUES; ALCALIGENES FAECALIS; AMIDE FORMATION; AMINO ACID RESIDUES; AROMATIC RESIDUES; CHIMERIC ENZYMES; CYSTEINE RESIDUES; ENANTIOSPECIFICITY; MANDELIC ACID; NITRILASE; POINT MUTATIONS; PSEUDOMONAS FLUORESCENS; RELATIVE ACTIVITIES; TRYPTOPHAN RESIDUES;

EID: 69449088689     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.00301-09     Document Type: Article
Times cited : (57)

References (35)
  • 1
    • 30844438925 scopus 로고    scopus 로고
    • Purification and characterization of an enantioselective arylacetonitrilase from Pseudomonas putida
    • Banerjee, A., P. Kaul, and U. C. Banerjee. 2006. Purification and characterization of an enantioselective arylacetonitrilase from Pseudomonas putida. Arch. Microbiol. 184:407-418.
    • (2006) Arch. Microbiol. , vol.184 , pp. 407-418
    • Banerjee, A.1    Kaul, P.2    Banerjee, U.C.3
  • 2
    • 0000349305 scopus 로고    scopus 로고
    • Nitriles
    • H. J. Rehm and G. Reed (ed.), Wiley-VCH, Weinheim, Germany.
    • Bunch, A. W. 1998. Nitriles, p. 277-324. In H. J. Rehm and G. Reed (ed.), Biotechnology, vol.8a. Biotransformations I. Wiley-VCH, Weinheim, Germany.
    • (1998) Biotechnology, Vol.8a. Biotransformations I , pp. 277-324
    • Bunch, A.W.1
  • 3
    • 0002805293 scopus 로고
    • Hydrolysis of the nitrile group of aminophenylacetonitrile by nitrilase: Development of a new biotechnology for stereospecific production of S-α-phenylglycine
    • Choi, S. Y., and Y. M. Goo. 1986. Hydrolysis of the nitrile group of aminophenylacetonitrile by nitrilase: development of a new biotechnology for stereospecific production of S-α-phenylglycine. Arch. Pharm. Res. 9:45-47.
    • (1986) Arch. Pharm. Res. , vol.9 , pp. 45-47
    • Choi, S.Y.1    Goo, Y.M.2
  • 4
    • 69449094568 scopus 로고    scopus 로고
    • Industrial scale process for the preparation of 2-hydroxy-4-methylbutyric acid using a nitrilase
    • January U.S. patent 6,180,359.
    • Favre-Bulle, O., J. Pierrard, C. David, P. Morel, and D. Horbez. January 2001. Industrial scale process for the preparation of 2-hydroxy-4-methylbutyric acid using a nitrilase. U.S. patent 6,180,359.
    • (2001)
    • Favre-Bulle, O.1    Pierrard, J.2    David, C.3    Morel, P.4    Horbez, D.5
  • 7
    • 0024788506 scopus 로고
    • Induction, purification, and characterization of the nitrilase of Fusarium oxysporum f. sp. melonis
    • Goldlust, A., and Z. Bohak. 1989. Induction, purification, and characterization of the nitrilase of Fusarium oxysporum f. sp. melonis. Biotechnol. Appl. Biochem. 11:581-601. (Pubitemid 20053753)
    • (1989) Biotechnology and Applied Biochemistry , vol.11 , Issue.6 , pp. 581-601
    • Goldlust, A.1    Bohak, Z.2
  • 9
    • 0024556150 scopus 로고
    • Engineering of hybrid genes without use of restriction enzymes: Gene splicing by overlap extension
    • Horton, R. M., H. D. Hunt, S. N. Ho, J. K. Pullen, and L. R. Pease. 1989. Engineering of hybrid genes without use of restriction enzymes: gene splicing by overlap extension. Gene 77:61-68.
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 10
    • 0346969549 scopus 로고    scopus 로고
    • Screening for enantioselective nitrilases: Kinetic resolution of racemic mandelonitrile to (R)-mandelic acid by new bacterial isolates
    • Kaul, P., A. Banerjee, S. Mayilraj, and U. C. Banerjee. 2004. Screening for enantioselective nitrilases: kinetic resolution of racemic mandelonitrile to (R)-mandelic acid by new bacterial isolates. Tetrahedron Asym. 15:207-211.
    • (2004) Tetrahedron Asym , vol.15 , pp. 207-211
    • Kaul, P.1    Banerjee, A.2    Mayilraj, S.3    Banerjee, U.C.4
  • 11
    • 34948906193 scopus 로고    scopus 로고
    • Cross-linked amorphous nitrilase aggregates for enantioselective nitrile hydrolysis
    • Kaul, P., A. Stolz, and U. C. Banerjee. 2007. Cross-linked amorphous nitrilase aggregates for enantioselective nitrile hydrolysis. Adv. Synth. Catal. 349:2167-2176.
    • (2007) Adv. Synth. Catal. , vol.349 , pp. 2167-2176
    • Kaul, P.1    Stolz, A.2    Banerjee, U.C.3
  • 12
    • 27744507286 scopus 로고    scopus 로고
    • Nitrilase from Pseudomonas fluorescens EBC191: Cloning and heterologous expression of the gene and biochemical characterization of the recombinant enzyme
    • Kiziak, C., D. Conradt, A. Stolz, R. Mattes, and J. Klein. 2005. Nitrilase from Pseudomonas fluorescens EBC191: cloning and heterologous expression of the gene and biochemical characterization of the recombinant enzyme. Microbiology 151:3639-3648.
    • (2005) Microbiology , vol.151 , pp. 3639-3648
    • Kiziak, C.1    Conradt, D.2    Stolz, A.3    Mattes, R.4    Klein, J.5
  • 13
    • 34548773501 scopus 로고    scopus 로고
    • Influence of different carboxy-terminal mutations on the substrate-, reaction- And enantiospecificity of the arylacetonitrilase from Pseudomonas fluorescens EBC191
    • DOI 10.1093/protein/gzm032
    • Kiziak, C., J. Klein, and A. Stolz. 2007. Influence of different carboxyterminal mutations on the substrate-, reaction-, and enantiospecifity of the aryl-acetonitrilase from Pseudomonas fluorescens EBC191. Prot. Eng. Design Sel. 20:385-396. (Pubitemid 47428965)
    • (2007) Protein Engineering, Design and Selection , vol.20 , Issue.8 , pp. 385-396
    • Kiziak, C.1    Klein, J.2    Stolz, A.3
  • 14
    • 0027525856 scopus 로고
    • Nitrilase in biosynthesis of the plant hormone indole-3-acetic acid from indole-3-acetonitrile: Cloning of the Alcaligenes gene and site-directed mutagenesis of cysteine residues
    • Kobayashi, M., H. Izui, T. Nagasawa, and H. Yamada. 1993. Nitrilase in biosynthesis of the plant hormone indole-3-acetic acid from indole-3- acetonitrile: cloning of the Alcaligenes gene and site-directed mutagenesis of cysteine residues. Proc. Natl. Acad. Sci. USA 90:247-251.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 247-251
    • Kobayashi, M.1    Izui, H.2    Nagasawa, T.3    Yamada, H.4
  • 15
    • 0026649436 scopus 로고
    • Nitrilase from Rhodococcus rhodochrous J1. Sequencing and overexpression of the gene and identification of an essential cysteine residue
    • Kobayashi, M., H. Komeda, N. Yanaka, T. Nagasawa, and H. Yamada. 1992. Nitrilase from Rhodococcus rhodochrous J1. Sequencing and overexpression of the gene and identification of an essential cysteine residue. J. Biol. Chem. 267:20746-20751.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20746-20751
    • Kobayashi, M.1    Komeda, H.2    Yanaka, N.3    Nagasawa, T.4    Yamada, H.5
  • 16
    • 0028289876 scopus 로고
    • Versatile nitrilases: Nitrile-hydrolysing enzymes
    • Kobayashi, M., and S. Shimizu. 1994. Versatile nitrilases: nitrile-hydrolysing enzymes. FEMS Microbiol. Lett. 120:217-224.
    • (1994) FEMS Microbiol. Lett. , vol.120 , pp. 217-224
    • Kobayashi, M.1    Shimizu, S.2
  • 17
    • 0025108790 scopus 로고
    • Purification and characterization of a novel nitrilase of Rhodococcus rhodochrous K22 that acts on aliphatic nitriles
    • Kobayashi, M., N. Yanaka, T. Nagasawa, and H. Yamada. 1990. Purification and characterization of a novel nitrilase of Rhodococcus rhodochrous K22 that acts on aliphatic nitriles. J. Bacteriol. 172:4807-4815.
    • (1990) J. Bacteriol. , vol.172 , pp. 4807-4815
    • Kobayashi, M.1    Yanaka, N.2    Nagasawa, T.3    Yamada, H.4
  • 18
    • 0026446033 scopus 로고
    • Enantioselective hydrolysis of O-acetylmandelonitrile to O-acetylmandelic acid by bacterial nitrilases
    • Layh, N., A. Stolz, S. Förster, F. Effenberger, and H.-J. Knackmuss. 1992. Enantioselective hydrolysis of O-acetylmandelonitrile to O-acetylmandelic acid by bacterial nitrilases. Arch. Microbiol. 158:405-411.
    • (1992) Arch. Microbiol. , vol.158 , pp. 405-411
    • Layh, N.1    Stolz, A.2    Förster, S.3    Effenberger, F.4    Knackmuss, H.-J.5
  • 20
    • 0036228279 scopus 로고    scopus 로고
    • Nitrile- And amide-converting microbial enzymes: Stereo-, regio- and chemoselectivity
    • Martinková, L., and V. Kren. 2002. Nitrile- and amide-converting microbial enzymes: stereo-, regio- and chemoselectivity. Biocatal. Biotrans. 20:79-93.
    • (2002) Biocatal. Biotrans. , vol.20 , pp. 79-93
    • Martinková, L.1    Kren, V.2
  • 21
    • 33644680778 scopus 로고    scopus 로고
    • Synthesis of enantiomerically pure (S)-mandelic acid using an oxynitrilase-nitrilase bienzymatic cascade. A nitrilase surprisingly shows nitrile hydratase activity
    • Mateo, C., A. Chmura, S. Rustler, F. van Rantwijk, A. Stolz, and R. A. Sheldon. 2006. Synthesis of enantiomerically pure (S)-mandelic acid using an oxynitrilase-nitrilase bienzymatic cascade. A nitrilase surprisingly shows nitrile hydratase activity. Tetrahedron Asym. 17:320-323.
    • (2006) Tetrahedron Asym , vol.17 , pp. 320-323
    • Mateo, C.1    Chmura, A.2    Rustler, S.3    Van Rantwijk, F.4    Stolz, A.5    Sheldon, R.A.6
  • 22
    • 0001735878 scopus 로고
    • Nitrilase-catalysed production of nicotinic acid from 3-cyanopyridine in Rhodococcus rhodochrous J1
    • Mathew, C. D., T. Nagasawa, M. Kobayashi, and H. Yamada. 1988. Nitrilase-catalysed production of nicotinic acid from 3-cyanopyridine in Rhodococcus rhodochrous J1. Appl. Environ. Microbiol. 54:1030-1032.
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 1030-1032
    • Mathew, C.D.1    Nagasawa, T.2    Kobayashi, M.3    Yamada, H.4
  • 23
    • 0025690724 scopus 로고
    • A novel nitrilase, aryl-acetonitrilase, of Alcaligenes faecalis JM3
    • Nagasawa, T., J. Mauger, and H. Yamada. 1990. A novel nitrilase, aryl-acetonitrilase, of Alcaligenes faecalis JM3. Eur. J. Biochem. 194:765-772.
    • (1990) Eur. J. Biochem. , vol.194 , pp. 765-772
    • Nagasawa, T.1    Mauger, J.2    Yamada, H.3
  • 24
    • 0036159384 scopus 로고    scopus 로고
    • Characterization and synthetic applications of recombinant AtNIT1 from Arabidopsis thaliana
    • Osswald, S., H. Wajant, and F. Effenberger. 2002. Characterization and synthetic applications of recombinant AtNIT1 from Arabidopsis thaliana. Eur. J. Biochem. 269:680-687.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 680-687
    • Osswald, S.1    Wajant, H.2    Effenberger, F.3
  • 25
    • 0035114118 scopus 로고    scopus 로고
    • The nitrilase superfamily: Classification, structure and function
    • Pace, H. C., and C. Brenner. 2001. The nitrilase superfamily: classification, structure and function. Genome Biol. 2:0001.1-0001.9.
    • (2001) Genome Biol , vol.2
    • Pace, H.C.1    Brenner, C.2
  • 26
    • 11244298760 scopus 로고    scopus 로고
    • Hydrolysis of nitriles using an immobilized nitrilase: Applications to the synthesis of methionine hydroxyl analogue derivatives
    • Rey, P., J.-C. Rossi, J. Taillades, G. Gros, and O. Nore. 2004. Hydrolysis of nitriles using an immobilized nitrilase: applications to the synthesis of methionine hydroxyl analogue derivatives. J. Agric. Food Chem. 52:8155-8162.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 8155-8162
    • Rey, P.1    Rossi, J.-C.2    Taillades, J.3    Gros, G.4    Nore, O.5
  • 27
    • 33847304920 scopus 로고    scopus 로고
    • Conversion of mandelonitrile and phenylglycinenitrile by recombinant E. coli cells synthesizing a nitrilase from Pseudomonas fluorescens EBC191
    • Rustler, S., A. Müller, V. Windeisen, A. Chmura, B. C. M. Fernandes, C. Kiziak, and A. Stolz. 2007. Conversion of mandelonitrile and phenylglycinenitrile by recombinant E. coli cells synthesizing a nitrilase from Pseudomonas fluorescens EBC191. Enzyme Microb. Technol. 40:598-606.
    • (2007) Enzyme Microb. Technol. , vol.40 , pp. 598-606
    • Rustler, S.1    Müller, A.2    Windeisen, V.3    Chmura, A.4    Fernandes, B.C.M.5    Kiziak, C.6    Stolz, A.7
  • 29
    • 0042428638 scopus 로고    scopus 로고
    • Hydrolysis and formation of C-N bonds
    • K. Drauz and H. Waldmann (ed.), Wiley-VCH, Weinheim, Germany.
    • Schulze, B. 2002. Hydrolysis and formation of C-N bonds, p. 699-715, In K. Drauz and H. Waldmann (ed.), Enzyme catalysis in organic synthesis, vol.II. Wiley-VCH, Weinheim, Germany.
    • (2002) Enzyme Catalysis in Organic Synthesis , vol.2 , pp. 699-715
    • Schulze, B.1
  • 31
    • 0025651825 scopus 로고
    • Detection of covalent enzyme-substrate complexes of nitrilase by ion-spray mass spectroscopy
    • Stevenson, D. E., R. Feng, and A. C. Storer. 1990. Detection of covalent enzyme-substrate complexes of nitrilase by ion-spray mass spectroscopy. FEBS Lett. 277:112-114.
    • (1990) FEBS Lett. , vol.277 , pp. 112-114
    • Stevenson, D.E.1    Feng, R.2    Storer, A.C.3
  • 32
    • 0020442864 scopus 로고
    • The pUC plasmids, and M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers
    • DOI 10.1016/0378-1119(82)90015-4
    • Vieira, J., and J. Messing. 1982. The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene 19:259-268. (Pubitemid 13201666)
    • (1982) Gene , vol.19 , Issue.3 , pp. 259-268
    • Vieira, J.1    Messing, J.2
  • 33
    • 0026632716 scopus 로고
    • Purification and characterization of the nitrilase from Alcaligenes faecalis ATCC 8750 responsible for enantioselective hydrolysis of mandelonitrile
    • Yamamoto, K., I. Fujimatsu, and K.-I. Komatsu. 1992. Purification and characterization of the nitrilase from Alcaligenes faecalis ATCC 8750 responsible for enantioselective hydrolysis of mandelonitrile. J. Ferment. Bioeng. 73:425-430.
    • (1992) J. Ferment. Bioeng. , vol.73 , pp. 425-430
    • Yamamoto, K.1    Fujimatsu, I.2    Komatsu, K.-I.3
  • 34
    • 0025953031 scopus 로고
    • Production of R-(-)-mandelic acid from mandelonitrile by Alcaligenes faecalis ATCC 8750
    • Yamamoto, K., K. Oishi, I. Fujimatsu, and K.-I. Komatsu. 1991. Production of R-(-)-mandelic acid from mandelonitrile by Alcaligenes faecalis ATCC 8750. Appl. Environ. Microbiol. 57:3028-3032.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 3028-3032
    • Yamamoto, K.1    Oishi, K.2    Fujimatsu, I.3    Komatsu, K.-I.4
  • 35
    • 58149142732 scopus 로고    scopus 로고
    • An amino acid at position 142 in nitrilase from Rhodococcus rhodochrous ATCC 33278 determines the substrate specificity for aliphatic and aromatic nitriles
    • Yeom, S.-J., H.-J. Kim, J.-K. Lee, D.-E. Kim, and D.-K. Oh. 2008. An amino acid at position 142 in nitrilase from Rhodococcus rhodochrous ATCC 33278 determines the substrate specificity for aliphatic and aromatic nitriles. Biochem. J. 415:401-407.
    • (2008) Biochem. J. , vol.415 , pp. 401-407
    • Yeom, S.-J.1    Kim, H.-J.2    Lee, J.-K.3    Kim, D.-E.4    Oh, D.-K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.