메뉴 건너뛰기




Volumn 60, Issue 1-2, 2002, Pages 33-44

Retraction Note To: The nitrile-degrading enzymes: current status and future prospects (Appl Microbiol Biotechnol, 60, 33-44, 2002, 10.1007/s00253-002-1062-0);The nitrile-degrading enzymes: Current status and future prospects

Author keywords

[No Author keywords available]

Indexed keywords

AMIDASE; NITRILASE; NITRILE; NITRILE HYDRATASE;

EID: 0037209758     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-016-7708-0     Document Type: Erratum
Times cited : (377)

References (112)
  • 1
    • 0035931535 scopus 로고    scopus 로고
    • Operational stability of Brevibacterium imperialis CBS 489-74 nitrile hydratase
    • Alfani F, Cantarella M, Spera A, Viparelli P (2001) Operational stability of Brevibacterium imperialis CBS 489-74 nitrile hydratase. J Mol Catal B 11:687-697
    • (2001) J Mol Catal B , vol.11 , pp. 687-697
    • Alfani, F.1    Cantarella, M.2    Spera, A.3    Viparelli, P.4
  • 2
    • 0033227463 scopus 로고    scopus 로고
    • Characterization of an inducible nitrilase from a thermophilic Bacillus
    • Almatawah QA, Cramp R, Cowan D (1999) Characterization of an inducible nitrilase from a thermophilic Bacillus. Extremophiles 3:283-291
    • (1999) Extremophiles , vol.3 , pp. 283-291
    • Almatawah, Q.A.1    Cramp, R.2    Cowan, D.3
  • 3
    • 0001328722 scopus 로고
    • Aliphatic nitrile hydratase from Arthrobacter sp. J1: Purification and characterization
    • Asano Y, Tashibana M, Tani Y, Yamada H (1982a) Aliphatic nitrile hydratase from Arthrobacter sp. J1: purification and characterization. Agric Biol Chem 46:1165-1174
    • (1982) Agric Biol Chem , vol.46 , pp. 1165-1174
    • Asano, Y.1    Tashibana, M.2    Tani, Y.3    Yamada, H.4
  • 4
    • 29144463451 scopus 로고
    • A new enzymatic method of acrylamide production
    • Asano Y, Yasuda T, Tani Y, Yamada H (1982b) A new enzymatic method of acrylamide production. Agric Biol Chem 46:1183-1189
    • (1982) Agric Biol Chem , vol.46 , pp. 1183-1189
    • Asano, Y.1    Yasuda, T.2    Tani, Y.3    Yamada, H.4
  • 6
    • 0028303120 scopus 로고
    • Differential regulation of an auxin producing nitrilase gene family inArabidopsis thaliana
    • Bartel B, Fink GR (1994) Differential regulation of an auxin producing nitrilase gene family in Arabidopsis thaliana. Proc Natl Acad Sci USA 91:6649-6653
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 6649-6653
    • Bartel, B.1    Fink, G.R.2
  • 7
    • 0030894383 scopus 로고    scopus 로고
    • Enzymatic decontamination of aqueous polymer emulsions containing acrylonitrile
    • Battistel E, Bernardi A, Maestri P (1997) Enzymatic decontamination of aqueous polymer emulsions containing acrylonitrile. Biotechnol Lett 19:131-134
    • (1997) Biotechnol Lett , vol.19 , pp. 131-134
    • Battistel, E.1    Bernardi, A.2    Maestri, P.3
  • 8
    • 0027945902 scopus 로고
    • Enantioselective hydrolysis of racemic 2-phenylpropionitrile and other (R, S)-2-arylpropionitriles by a new bacterial isolate, Agrobacterium tumefaciens strain d3
    • Bauer R, Hirrlinger B, Layh N, Stolz A, Knackmuss H-J (1994) Enantioselective hydrolysis of racemic 2-phenylpropionitrile and other (R, S)-2-arylpropionitriles by a new bacterial isolate, Agrobacterium tumefaciens strain d3. Appl Microbiol Biotechnol 42:1-7
    • (1994) Appl Microbiol Biotechnol , vol.42 , pp. 1-7
    • Bauer, R.1    Hirrlinger, B.2    Layh, N.3    Stolz, A.4    Knackmuss, H.-J.5
  • 9
  • 10
    • 0026628701 scopus 로고
    • Asymmetric hydrolysis of alpha aminonitriles to optically active amino acids by a nitrilase of Rhodococcus rhodochrous PA-34
    • Bhalla T, Miura A, Wakamoto A, Ohba Y, Furuhashi K (1992) Asymmetric hydrolysis of alpha aminonitriles to optically active amino acids by a nitrilase of Rhodococcus rhodochrous PA-34. Appl Microbiol Biotechnol 37:184-190
    • (1992) Appl Microbiol Biotechnol , vol.37 , pp. 184-190
    • Bhalla, T.1    Miura, A.2    Wakamoto, A.3    Ohba, Y.4    Furuhashi, K.5
  • 13
    • 0034135644 scopus 로고    scopus 로고
    • Cloning of a wide spectrum amidase from Bacillus stearothermophilus BR 388 in E. coli and marked enhancement of amidase expression using directed evolution
    • Cheong T, Oriel P (2000) Cloning of a wide spectrum amidase from Bacillus stearothermophilus BR 388 in E. coli and marked enhancement of amidase expression using directed evolution. Enzyme Microb Technol 26:152-158
    • (2000) Enzyme Microb Technol , vol.26 , pp. 152-158
    • Cheong, T.1    Oriel, P.2
  • 14
    • 0028939517 scopus 로고
    • Purification and characterization of an enantioselective amidase from Pseudomonas chlororaphis B23
    • Ciskainik L, Wilczek J, Fallon R (1995) Purification and characterization of an enantioselective amidase from Pseudomonas chlororaphis B23. Appl Environ Microbiol 61:998-1003
    • (1995) Appl Environ Microbiol , vol.61 , pp. 998-1003
    • Ciskainik, L.1    Wilczek, J.2    Fallon, R.3
  • 15
    • 0020685215 scopus 로고
    • The utilization of nitriles and amides by Nocardia rhodochrous
    • Collins P, Knowles C (1983) The utilization of nitriles and amides by Nocardia rhodochrous. J Gen Microbiol 129:248-254
    • (1983) J Gen Microbiol , vol.129 , pp. 248-254
    • Collins, P.1    Knowles, C.2
  • 16
    • 0002954809 scopus 로고
    • Biosynthesis of cyanogenic glycosides
    • Vennesland B, Conn EE, Knowles CJ, Westly J, Wissing F (eds). Academic Press, London
    • Conn EE (1981) Biosynthesis of cyanogenic glycosides. In: Vennesland B, Conn EE, Knowles CJ, Westly J, Wissing F (eds) Cyanide in biology. Academic Press, London, pp 183-196
    • (1981) Cyanide in Biology , pp. 183-196
    • Conn, E.E.1
  • 19
    • 0035811975 scopus 로고    scopus 로고
    • Regioselective biotransformation of the dinitrile compounds 2-, 3-, and 4- (cyanomethyl) benzonitrile by the soil bacterium Rhodococcus rhodochrous LL100-21
    • Dadd M, Claridge T, Walton R, Pettman A, Knowles C (2001) Regioselective biotransformation of the dinitrile compounds 2-, 3-, and 4- (cyanomethyl) benzonitrile by the soil bacterium Rhodococcus rhodochrous LL100-21. Enzyme Microb Technol 29:20-27
    • (2001) Enzyme Microb Technol , vol.29 , pp. 20-27
    • Dadd, M.1    Claridge, T.2    Walton, R.3    Pettman, A.4    Knowles, C.5
  • 20
    • 0024445277 scopus 로고
    • Cyanide oxygenase and cyanase activities of Pseudomonas fluorescens NCIMB 11764
    • Dorr P, Knowles C (1989) Cyanide oxygenase and cyanase activities of Pseudomonas fluorescens NCIMB 11764. FEMS Microbiol Lett 60:289-294
    • (1989) FEMS Microbiol Lett , vol.60 , pp. 289-294
    • Dorr, P.1    Knowles, C.2
  • 21
    • 0024972056 scopus 로고
    • Nitrile hydratase of Rhodococcus sp. N-774: Purification and characterization
    • Endo I, Watanabe I (1989) Nitrile hydratase of Rhodococcus sp. N-774: purification and characterization. FEBS Lett 243:61-64
    • (1989) FEBS Lett , vol.243 , pp. 61-64
    • Endo, I.1    Watanabe, I.2
  • 22
    • 0033152216 scopus 로고    scopus 로고
    • An enzyme controlled by light: The molecular mechanism of photoreactivity in nitrile hydratase
    • Endo I, Okada M, Yohda M (1999) An enzyme controlled by light: the molecular mechanism of photoreactivity in nitrile hydratase. Trends Biotechnol 17:244-248
    • (1999) Trends Biotechnol , vol.17 , pp. 244-248
    • Endo, I.1    Okada, M.2    Yohda, M.3
  • 23
    • 0031017622 scopus 로고    scopus 로고
    • A Pseudomonas putida capable of stereoselective hydrolysis of nitriles
    • Fallon R, Stieglitz B, Turner I (1997) A Pseudomonas putida capable of stereoselective hydrolysis of nitriles. Appl Microbiol Biotechnol 47:156-161
    • (1997) Appl Microbiol Biotechnol , vol.47 , pp. 156-161
    • Fallon, R.1    Stieglitz, B.2    Turner, I.3
  • 24
    • 0031879459 scopus 로고    scopus 로고
    • Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: Formation of a wide range of hydroxamic acids
    • Fournand D, Bigey F, Arnaud A (1998) Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic acids. Appl Environ Microbiol 64:2844-2852
    • (1998) Appl Environ Microbiol , vol.64 , pp. 2844-2852
    • Fournand, D.1    Bigey, F.2    Arnaud, A.3
  • 27
    • 0024788506 scopus 로고
    • Induction, purification and characterization of the nitrilase of Fusarium oxysporum
    • Goldhust A, Bohak Z (1989) Induction, purification and characterization of the nitrilase of Fusarium oxysporum. Biotechnol Appl Biochem 11:581-601
    • (1989) Biotechnol Appl Biochem , vol.11 , pp. 581-601
    • Goldhust, A.1    Bohak, Z.2
  • 28
    • 0017668205 scopus 로고
    • Fungal degradation of aromatic nitriles: Enzymology of C-N cleavage by Fusarium solani
    • Harper D (1977a) Fungal degradation of aromatic nitriles: enzymology of C-N cleavage by Fusarium solani. Biochem J 167:685-692
    • (1977) Biochem J , vol.167 , pp. 685-692
    • Harper, D.1
  • 29
    • 0017393718 scopus 로고
    • Microbial metabolism of aromatic nitriles: Enzymology of C-N cleavage by Nocardia sp. NCIB 11216
    • Harper D (1977b) Microbial metabolism of aromatic nitriles: enzymology of C-N cleavage by Nocardia sp. NCIB 11216. J Biochem 165:309-319
    • (1977) J Biochem , vol.165 , pp. 309-319
    • Harper, D.1
  • 30
    • 0021781487 scopus 로고
    • Characterization of a nitrilase from Nocardia sp. (Rhodococcus group) NCIB 11215, using p-hydroxybenzonitrile as sole carbon source
    • Harper D (1985) Characterization of a nitrilase from Nocardia sp. (Rhodococcus group) NCIB 11215, using p-hydroxybenzonitrile as sole carbon source. Int J Biochem 17:677-683
    • (1985) Int J Biochem , vol.17 , pp. 677-683
    • Harper, D.1
  • 31
    • 0026596315 scopus 로고
    • Development of host -vector system in a Rhodococcus strain and its use for expression of the cloned nitrile hydratase gene cluster
    • Hashimoto Y, Nishiyama M, Yu F, Watanabe I, Horinouchi S, Beppu T (1992) Development of host -vector system in a Rhodococcus strain and its use for expression of the cloned nitrile hydratase gene cluster. J Gen Microbiol 138:1003-1010
    • (1992) J Gen Microbiol , vol.138 , pp. 1003-1010
    • Hashimoto, Y.1    Nishiyama, M.2    Yu, F.3    Watanabe, I.4    Horinouchi, S.5    Beppu, T.6
  • 32
    • 0029996889 scopus 로고    scopus 로고
    • Purification and characterization of an amidase from Rhodococcus erythropolis MP 50 which enantioselectively hydrolyzes 2-arylpropionamides
    • Hirrlinger B, Stolz A, Knackmuss H (1996) Purification and characterization of an amidase from Rhodococcus erythropolis MP 50 which enantioselectively hydrolyzes 2-arylpropionamides. J Bacteriol 178:3501-3507
    • (1996) J Bacteriol , vol.178 , pp. 3501-3507
    • Hirrlinger, B.1    Stolz, A.2    Knackmuss, H.3
  • 33
    • 0032215076 scopus 로고    scopus 로고
    • The nitrilase of Rhodococcus rhodochrous NCIMB 11216
    • Hoyle A, Bunch A, Knowles C (1998) The nitrilase of Rhodococcus rhodochrous NCIMB 11216. Enzyme Microb Technol 23:475-482
    • (1998) Enzyme Microb Technol , vol.23 , pp. 475-482
    • Hoyle, A.1    Bunch, A.2    Knowles, C.3
  • 34
    • 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, Schneder G, Lindqvist Y (1997) Crystal structure of nitrile hydratase reveals a novel iron centre in a novel fold. Structure 5:691-699
    • Structure , vol.5 , pp. 691-699
    • Huang, W.1    Jia, J.2    Cummings, J.3    Nelson, M.4    Schneder, G.5    Lindqvist, Y.6
  • 35
    • 0024363273 scopus 로고
    • Primary structure of NHase deduced from nucleotide sequence of a Rhodococcus sp. and its expression in E. coli
    • Ikehata O, Nishiyama M, Horinouchi S, Beppu T (1989) Primary structure of NHase deduced from nucleotide sequence of a Rhodococcus sp. and its expression in E. 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
  • 36
    • 0025802895 scopus 로고
    • Novel cyanide hydrolyzing enzyme from Alcaligenes xyloxidans subsp. denitrificans
    • Ingovorsen K, Hijer-Pedersen B, Godtfredsen S (1991) Novel cyanide hydrolyzing enzyme from Alcaligenes xyloxidans subsp. denitrificans. Appl Environ Microbiol 57:1783-1789
    • (1991) Appl Environ Microbiol , vol.57 , pp. 1783-1789
    • Ingovorsen, K.1    Hijer-Pedersen, B.2    Godtfredsen, S.3
  • 38
    • 0039466853 scopus 로고    scopus 로고
    • Nitrile hydratase involved in aldoxime metabolism from Rhodococcus sp. strain YH3-3: Purification and characterization
    • Kato Y, Tsuda T, Asano Y (1999) Nitrile hydratase involved in aldoxime metabolism from Rhodococcus sp. strain YH3-3: purification and characterization. Eur J Biochem 263:662-670
    • (1999) Eur J Biochem , vol.263 , pp. 662-670
    • Kato, Y.1    Tsuda, T.2    Asano, Y.3
  • 39
    • 0342803567 scopus 로고    scopus 로고
    • Distribution of aldoxime dehydratase in microorganisms
    • Kato Y, Ooi R, Asano Y (2000) Distribution of aldoxime dehydratase in microorganisms. Appl Environ Microbiol 66:2290-2296
    • (2000) Appl Environ Microbiol , vol.66 , pp. 2290-2296
    • Kato, Y.1    Ooi, R.2    Asano, Y.3
  • 40
    • 0032859880 scopus 로고    scopus 로고
    • Nitrile hydratase from Rhodococcus erythropolis, metabolization of steroidal compounds with a nitrile group
    • Kaufmann G, Dautzenberg H, Henkel H, Muller G, Schafer T (1999) Nitrile hydratase from Rhodococcus erythropolis, metabolization of steroidal compounds with a nitrile group. Steroids 64:535-540
    • Steroids , vol.64 , pp. 535-540
    • Kaufmann, G.1    Dautzenberg, H.2    Henkel, H.3    Muller, G.4    Schafer, T.5
  • 41
    • 0019786740 scopus 로고
    • Elude d'une l-alfa-aminoamidase particulaire de Brevibacerium sp. en vue de l'obtention d'acids alfa-amines optiquement actifs
    • Kieny-L' Homme M, Arnaud A, Glazy P (1981) Elude d'une l-alfa-aminoamidase particulaire de Brevibacerium sp. en vue de l'obtention d'acids alfa-amines optiquement actifs. J Gen Appl Microbiol 27:307-311
    • (1981) J Gen Appl Microbiol , vol.27 , pp. 307-311
    • Kieny-L' Homme, M.1    Arnaud, A.2    Glazy, P.3
  • 42
    • 0024970709 scopus 로고
    • Nitrilase of Rhodococcus rhodochrous J1: Purification and characterization
    • Kobayashi M, Nagasawa T, Yamada H (1989) Nitrilase of Rhodococcus rhodochrous J1: purification and characterization. Eur J Biochem 182:349-356
    • (1989) Eur J Biochem , vol.182 , pp. 349-356
    • Kobayashi, M.1    Nagasawa, T.2    Yamada, H.3
  • 43
    • 0025108790 scopus 로고
    • Purification and characterization of a novel nitrilase of Rhodococcus rhodochrous K22 that acts on aliphatic nitriles
    • Kobayashi M, Yanaka N, Nagasawa T, Yamada H (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
  • 44
    • 0025934442 scopus 로고
    • Cloning, nucleotide sequence and expression in E. coli of two cobalt containing NHases from R. rhodochrous J1
    • Kobayashi M, Nishiyama M, Nagasawa T, Horinouchi S, Beppu T, Yamada H (1991) Cloning, nucleotide sequence and expression in E. coli of two cobalt containing NHases from R. rhodochrous J1. Biochim Biophys Acta 1119:23-33
    • (1991) Biochim Biophys Acta , vol.1119 , pp. 23-33
    • Kobayashi, M.1    Nishiyama, M.2    Nagasawa, T.3    Horinouchi, S.4    Beppu, T.5    Yamada, H.6
  • 45
    • 0026649436 scopus 로고
    • Nitrilase from Rhodococcus rhodochrous J1: Sequencing and overexpression of the gene and identification of an essential cysteine residue
    • Kobayashi M, Komeda H, Yanaka N, Nagasawa T, Yamada H (1992a) 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
  • 46
    • 0026646050 scopus 로고
    • Primary structure of an aliphatic nitrilase from Rhodococcus rhodochrous K22 and expression of its gene and identification of its active site residue
    • Kobayashi M, Yanaka N, Nagasawa T, Yamada H (1992b) Primary structure of an aliphatic nitrilase from Rhodococcus rhodochrous K22 and expression of its gene and identification of its active site residue. Biochemistry 31:9000-9007
    • (1992) Biochemistry , vol.31 , pp. 9000-9007
    • Kobayashi, M.1    Yanaka, N.2    Nagasawa, T.3    Yamada, H.4
  • 47
    • 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, Izui H, Nagasawa T, Yamada H (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
  • 48
    • 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 S, 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, S.2    Fujita, T.3    Masuda, M.4    Shimizu, S.5
  • 49
    • 0030700490 scopus 로고    scopus 로고
    • Identification of an active site in amidase - Evolutionary relationship between amide bond and peptide bond cleaving enzymes
    • Kobayashi M, Fujiwara Y, Goda M, Komeda H, Shimizu S (1997) Identification of an active site in amidase - evolutionary relationship between amide bond and peptide bond cleaving enzymes. Proc Natl Acad Sci USA 94:11986-11991
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11986-11991
    • Kobayashi, M.1    Fujiwara, Y.2    Goda, M.3    Komeda, H.4    Shimizu, S.5
  • 50
    • 0031731022 scopus 로고    scopus 로고
    • The catalytic mechanism of amidase also involves nitrile hydrolysis
    • Kobayashi M, Goda M, Shimizu S (1998) The catalytic mechanism of amidase also involves nitrile hydrolysis. FEBS Lett 439:325-328
    • (1998) FEBS Lett , vol.439 , pp. 325-328
    • Kobayashi, M.1    Goda, M.2    Shimizu, S.3
  • 51
    • 0033573872 scopus 로고    scopus 로고
    • Nitrilase catalyzes amide hydrolysis as well as nitrile hydrolysis
    • Kobayashi M, Goda M, Shimizu S (1999) Nitrilase catalyzes amide hydrolysis as well as nitrile hydrolysis. Biochem Biophys Res Commun 255:549-553
    • (1999) Biochem Biophys Res Commun , vol.255 , pp. 549-553
    • Kobayashi, M.1    Goda, M.2    Shimizu, S.3
  • 52
    • 0034067403 scopus 로고    scopus 로고
    • Gene cloning, nucleotide sequencing, and purification and characterization of the D-stereospecific amino acid amidase from Ochrobactrum anthropi SV3
    • Komeda H, Asano Y (2000) Gene cloning, nucleotide sequencing, and purification and characterization of the D-stereospecific amino acid amidase from Ochrobactrum anthropi SV3. Eur J Biochem 267:2028-2035
    • (2000) Eur J Biochem , vol.267 , pp. 2028-2035
    • Komeda, H.1    Asano, Y.2
  • 53
    • 0029763188 scopus 로고    scopus 로고
    • Transcriptional regulation of the Rhodococcus rhodochrous J1 nitA gene encoding a nitrilase
    • Komeda H, Hori Y, Kobayashi M, Shimizu S (1996a) Transcriptional regulation of the Rhodococcus rhodochrous J1 nitA gene encoding a nitrilase. Proc Natl Acad Sci USA 93:10572-10577
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 10572-10577
    • Komeda, H.1    Hori, Y.2    Kobayashi, M.3    Shimizu, S.4
  • 54
    • 0029984895 scopus 로고    scopus 로고
    • A novel gene cluster including the R. rhodochrous J1 nhiBA genes encoding a new low molecular mass nitrile hydratase (L-NHase) induced by its reaction product
    • Komeda H, Kobayashi M, Shimizu S (1996b) A novel gene cluster including the R. rhodochrous J1 nhiBA genes encoding a new 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
  • 56
    • 0011067359 scopus 로고
    • Liberation of hydrogen cyanide from diaminomalenonitrile by Trichoderma sp. MB 519
    • Kuwahara M, Yanase H (1985) Liberation of hydrogen cyanide from diaminomalenonitrile by Trichoderma sp. MB 519. Agric Biol Chem 49:125-131
    • (1985) Agric Biol Chem , vol.49 , pp. 125-131
    • Kuwahara, M.1    Yanase, H.2
  • 57
    • 0032532430 scopus 로고    scopus 로고
    • Characterization and partial purification of an enantioselective arylacetonitrilase from Pseudomonas fluorescens DSM 7155
    • Layh N, Parratt J, Willetts A (1998) Characterization and partial purification of an enantioselective arylacetonitrilase from Pseudomonas fluorescens DSM 7155. J Mol Catal B 5:467-474
    • (1998) J Mol Catal B , vol.5 , pp. 467-474
    • Layh, N.1    Parratt, J.2    Willetts, A.3
  • 58
    • 0029154780 scopus 로고
    • Aliphatic nitrilase from a soil isolated Comamonas testoteroni sp. gene cloning and overexpression, purification and primary structure
    • Levy-Schill S, Soubrier F, Crutz-Le Coq A, Faucher D, Crouzet J, Petre D (1995) Aliphatic nitrilase from a soil isolated Comamonas testoteroni sp. gene cloning and overexpression, purification and primary structure. Gene 161:15-20
    • (1995) Gene , vol.161 , pp. 15-20
    • Levy-Schill, S.1    Soubrier, F.2    Crutz-Le Coq, A.3    Faucher, D.4    Crouzet, J.5    Petre, D.6
  • 59
    • 0031110421 scopus 로고    scopus 로고
    • The role of nitrogenase in a cyanide degrading Klebsiella oxytoca strain
    • Liu J, Liu C, Lin C (1997) The role of nitrogenase in a cyanide degrading Klebsiella oxytoca strain. Proc Natl Sci Counc Repub China 21:37-42
    • (1997) Proc Natl Sci Counc Repub China , vol.21 , pp. 37-42
    • Liu, J.1    Liu, C.2    Lin, C.3
  • 61
    • 0001735878 scopus 로고
    • Nitrilase catalyzed production of nicotinic acid from 3-cyanopyridine in Rhodococcus rhodochrous J1
    • Mathew C, Nagasawa T, Kobayashi M, Yamada H (1988) Nitrilase catalyzed 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.1    Nagasawa, T.2    Kobayashi, M.3    Yamada, H.4
  • 62
    • 0025604503 scopus 로고
    • Purification, cloning, and primary structure of an enantiomer selective amidase from Brevibacterium sp. R312: Structural evidence for genetic coupling with nitrile hydratase
    • Mayaux J, Cerbelaud E, Soubrier F, Faucher D, Petre D (1990) Purification, cloning, and primary structure of an enantiomer selective amidase from Brevibacterium sp. R312: structural evidence for genetic coupling with nitrile hydratase. J Bacteriol 172:6764-6773
    • (1990) J Bacteriol , vol.172 , pp. 6764-6773
    • Mayaux, J.1    Cerbelaud, E.2    Soubrier, F.3    Faucher, D.4    Petre, D.5
  • 63
    • 0025747960 scopus 로고    scopus 로고
    • Purification, cloning and primary structure of a new enantioselective amidase from a Rhodococcus strain: Structural evidence for a conserved genetic coupling with nitrile hydratase
    • Mayaux J, Cerbelaud E, Soubrier F, Yeh P, Blanche F, Petre D (1991) Purification, cloning and primary structure of a new enantioselective amidase from a Rhodococcus strain: structural evidence for a conserved genetic coupling with nitrile hydratase. J Bacteriol 173:6694-6704
    • J Bacteriol , vol.173 , pp. 6694-6704
    • Mayaux, J.1    Cerbelaud, E.2    Soubrier, F.3    Yeh, P.4    Blanche, F.5    Petre, D.6
  • 65
    • 0027265343 scopus 로고
    • Isolation of Brevibacterium sp. R312 mutant potentially useful for the enzymatic production of adipic acid
    • Moreau JL, Bernet N, Arnaud A, Glazy P (1993) Isolation of Brevibacterium sp. R312 mutant potentially useful for the enzymatic production of adipic acid. Can J Microbiol 39:524-528
    • (1993) Can J Microbiol , vol.39 , pp. 524-528
    • Moreau, J.L.1    Bernet, N.2    Arnaud, A.3    Glazy, P.4
  • 66
    • 0033289544 scopus 로고    scopus 로고
    • Bacterial degradation of the herbicide bromoxynil by Agrobacterium radiobacter in biofilm
    • Muller D, Gabriel J (1999) Bacterial degradation of the herbicide bromoxynil by Agrobacterium radiobacter in biofilm. Folia Microbiol 44:377-379
    • (1999) Folia Microbiol , vol.44 , pp. 377-379
    • Muller, D.1    Gabriel, J.2
  • 67
    • 0023059799 scopus 로고
    • Nitrile hydratase of Brevibacterium R312: Purification and characterization
    • Nagasawa T, Ryuno K, Yamada H (1986) Nitrile hydratase of Brevibacterium R312: purification and characterization. Biochem Biophys Res Commun 139:1305-1312
    • (1986) Biochem Biophys Res Commun , vol.139 , pp. 1305-1312
    • Nagasawa, T.1    Ryuno, K.2    Yamada, H.3
  • 68
    • 0023118310 scopus 로고
    • Nitrile hydratase of Pseudomonas chlororaphis B23: Purification and characterization
    • Nagasawa T, Nanba H, Ryuno K, Takeuchi K, Yamada H (1987) Nitrile hydratase of Pseudomonas chlororaphis B23: purification and characterization. Eur J Biochem 162:691-698
    • (1987) Eur J Biochem , vol.162 , pp. 691-698
    • Nagasawa, T.1    Nanba, H.2    Ryuno, K.3    Takeuchi, K.4    Yamada, H.5
  • 69
    • 0002587167 scopus 로고
    • Optimum culture conditions for the production of benzonitrilase by Rhodococcus rhodochrous J1
    • Nagasawa T, Kobayashi M, Yamada H (1988) Optimum culture conditions for the production of benzonitrilase by Rhodococcus rhodochrous J1. Arch Microbiol 150:89-94
    • (1988) Arch Microbiol , vol.150 , pp. 89-94
    • Nagasawa, T.1    Kobayashi, M.2    Yamada, H.3
  • 70
    • 0025690724 scopus 로고
    • Novel nitrilase, arylacetonitrilase, of Alcaligenes faecalis JM3, purification and characterization
    • Nagasawa T, Mauger J, Yamada H (1990) Novel nitrilase, arylacetonitrilase, of Alcaligenes faecalis JM3, purification and characterization. Biochemistry 194:765-772
    • (1990) Biochemistry , vol.194 , pp. 765-772
    • Nagasawa, T.1    Mauger, J.2    Yamada, H.3
  • 71
    • 0025962966 scopus 로고
    • Characterization of a new cobalt containing nitrile hydratase purified from urea induced cells of R. rhodochrous J1
    • Nagasawa T, Takeuchu K, Yamada H (1991) Characterization of a new cobalt containing nitrile hydratase purified from urea induced cells of R. rhodochrous J1. Eur J Biochem 196:581-589
    • (1991) Eur J Biochem , vol.196 , pp. 581-589
    • Nagasawa, T.1    Takeuchu, K.2    Yamada, H.3
  • 72
    • 0033962871 scopus 로고    scopus 로고
    • Nitrilase of Rhodococcus rhodochrous J1, conversion into the active form by subunit association
    • Nagasawa T, Wieser M, Nakamura T, Iwahara H, Yoshida T, Gekko K (2000) Nitrilase of Rhodococcus rhodochrous J1, conversion into the active form by subunit association. Eur J Biochem 267:138-144
    • (2000) Eur J Biochem , vol.267 , pp. 138-144
    • Nagasawa, T.1    Wieser, M.2    Nakamura, T.3    Iwahara, H.4    Yoshida, T.5    Gekko, K.6
  • 74
    • 0029882153 scopus 로고    scopus 로고
    • Physical, biochemical, and immunological characterization of a thermostable amidase from Klebsiella pneumoniae NCTR 1
    • Nawaz M, Khan A, Bhattacharya D, Sittoneu P, Cerniglia C (1996) Physical, biochemical, and immunological characterization of a thermostable amidase from Klebsiella pneumoniae NCTR 1. J Bacteriol 178:2397-2401
    • (1996) J Bacteriol , vol.178 , pp. 2397-2401
    • Nawaz, M.1    Khan, A.2    Bhattacharya, D.3    Sittoneu, P.4    Cerniglia, C.5
  • 75
    • 85004575713 scopus 로고
    • Microbial synthesis of tranexamic acid intermediate from dinitrile
    • Nishise H, Kurihara M, Tani Y (1987) Microbial synthesis of tranexamic acid intermediate from dinitrile. Agric Biol Chem 51:2613-2616
    • (1987) Agric Biol Chem , vol.51 , pp. 2613-2616
    • Nishise, H.1    Kurihara, M.2    Tani, Y.3
  • 76
    • 0025761763 scopus 로고
    • Cloning and characterization of genes responsible for metabolism of nitrile compounds from P. chlororaphis B23
    • Nishiyama M, Horinouchi S, Kobayashi M, Nagasawa T, Yamada H, Beppu T (1991) Cloning and characterization of genes responsible for metabolism of nitrile compounds from P. 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
  • 77
    • 0029074567 scopus 로고
    • Pseudomonas aeruginosa aliphatic amidase is related to nitrilase/cyanide hydratase enzyme family and Cys166 is predicted to be the active site nucleophile of the catalytic mechanism
    • Novo C, Tata R, Clemente A, Brown P (1995) Pseudomonas aeruginosa aliphatic amidase is related to nitrilase/cyanide hydratase enzyme family and Cys166 is predicted to be the active site nucleophile of the catalytic mechanism. FEBS Lett 367:275-279
    • (1995) FEBS Lett , vol.367 , pp. 275-279
    • Novo, C.1    Tata, R.2    Clemente, A.3    Brown, P.4
  • 79
    • 0036159384 scopus 로고    scopus 로고
    • Characterization and synthetic applications of recombinant AtNIT1 from Arabidopsis thaliana
    • Osswald S, Wajant H, Effenberger F (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
  • 80
    • 0034705440 scopus 로고    scopus 로고
    • Clarifying the catalytic roles of conserved residues in the amidase signature family
    • Patricelli MP, Cravatt BF (2000) Clarifying the catalytic roles of conserved residues in the amidase signature family. J Biol Chem 275:19177-19184
    • (2000) J Biol Chem , vol.275 , pp. 19177-19184
    • Patricelli, M.P.1    Cravatt, B.F.2
  • 83
    • 0035951786 scopus 로고    scopus 로고
    • The Arabidopsis thaliana isogene NIT4 and its orthologs in tobacco encode β-cyano-L-alanine hydratase/nitrilase
    • Piotrowski M, Schönfelder S, Weiler WE (2001) The Arabidopsis thaliana isogene NIT4 and its orthologs in tobacco encode β-cyano-L-alanine hydratase/nitrilase. J Biol Chem 276:2616-2621
    • (2001) J Biol Chem , vol.276 , pp. 2616-2621
    • Piotrowski, M.1    Schönfelder, S.2    Weiler, W.E.3
  • 87
    • 0034486851 scopus 로고    scopus 로고
    • Metabolism of benzonitrile by Cryptococcus sp. UFMG- Y28
    • Rezende R, Dias J, Ferraz V, Linardi V (2000) Metabolism of benzonitrile by Cryptococcus sp. UFMG- Y28. J Basic Microbiol 40:389-392
    • (2000) J Basic Microbiol , vol.40 , pp. 389-392
    • Rezende, R.1    Dias, J.2    Ferraz, V.3    Linardi, V.4
  • 88
    • 0021662385 scopus 로고
    • -)-induced autoxygenation of organic substrates: A model chemical system for cytochrome P-450-catalyzed monoxygenation and dehydrogenation by dioxygen
    • -)-induced autoxygenation of organic substrates: a model chemical system for cytochrome P-450-catalyzed monoxygenation and dehydrogenation by dioxygen. Proc Natl Acad Sci USA 81:8025-8027
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 8025-8027
    • Sawyer, D.T.1    Sugimoto, H.2    Calderwood, T.S.3
  • 89
    • 0000163181 scopus 로고
    • Cyanide as a metabolic inhibitor
    • Vennesland B, Conn EE, Knowles CJ, Westly J, Wissing F (eds). Academic Press, London
    • Solomonson LP, Spehar AM (1981) Cyanide as a metabolic inhibitor. In: Vennesland B, Conn EE, Knowles CJ, Westly J, Wissing F (eds) Cyanide in Biology. Academic Press, London, pp 11-28
    • (1981) Cyanide in Biology , pp. 11-28
    • Solomonson, L.P.1    Spehar, A.M.2
  • 90
    • 0034016236 scopus 로고    scopus 로고
    • A novel amidase (half-amidase) for half-amide hydrolysis involved in the bacterial metabolism of cyclic imides
    • Soong C, Ogawa J, Shimizu S (2000) A novel amidase (half-amidase) for half-amide hydrolysis involved in the bacterial metabolism of cyclic imides. Appl Environ Microbiol 66:1947-1952
    • (2000) Appl Environ Microbiol , vol.66 , pp. 1947-1952
    • Soong, C.1    Ogawa, J.2    Shimizu, S.3
  • 91
    • 0023144333 scopus 로고
    • Cloning and expression in E. coli of a Klebsiella ozaenae plasmid borne gene encoding a nitrilase specific for the herbicide bromoxynil
    • Stalker D, McBride K (1987) Cloning and expression in E. coli of a Klebsiella ozaenae plasmid borne gene encoding a nitrilase specific for the herbicide bromoxynil. J Bacteriol 169:955-960
    • (1987) J Bacteriol , vol.169 , pp. 955-960
    • Stalker, D.1    McBride, K.2
  • 92
    • 0023927955 scopus 로고
    • Purification and properties of a nitrilase specific for the herbicide bromoxynil and corresponding nucleotide sequence analysis of the bxn gene
    • Stalker D, Malyj L, McBride K (1988a) Purification and properties of a nitrilase specific for the herbicide bromoxynil and corresponding nucleotide sequence analysis of the bxn gene. J Biol Chem 263:6310-6314
    • (1988) J Biol Chem , vol.263 , pp. 6310-6314
    • Stalker, D.1    Malyj, L.2    McBride, K.3
  • 93
    • 0023808282 scopus 로고
    • Herbicide resistance in transgenic plants expressing a bacterial detoxification gene
    • Stalker D, McBride K, Malyj L (1988b) Herbicide resistance in transgenic plants expressing a bacterial detoxification gene. Science 242:419-423
    • (1988) Science , vol.242 , pp. 419-423
    • Stalker, D.1    McBride, K.2    Malyj, L.3
  • 94
    • 0029616106 scopus 로고
    • Purification and characterization of a newly screened microbial peptide amidase
    • Stelkes-Ritter U, Wyzgol K, Kula M (1995) Purification and characterization of a newly screened microbial peptide amidase. Appl Microbiol Biotechnol 44:393-398
    • (1995) Appl Microbiol Biotechnol , vol.44 , pp. 393-398
    • Stelkes-Ritter, U.1    Wyzgol, K.2    Kula, M.3
  • 96
    • 0023229582 scopus 로고
    • Nitrile hydratase: The first non-heme iron enzyme with a typical low spin Fe(III) active centre
    • Sugiura Y, Kuwahara J, Nagasawa T, Yamada H (1987) Nitrile hydratase: the first non-heme iron enzyme with a typical low spin Fe(III) active centre. J Am Chem Soc 109:5848-5850
    • (1987) J Am Chem Soc , vol.109 , pp. 5848-5850
    • Sugiura, Y.1    Kuwahara, J.2    Nagasawa, T.3    Yamada, H.4
  • 97
    • 0034127002 scopus 로고    scopus 로고
    • Nitrile hydratase and amidase from Rhodococcus rhodochrous hydrolyze acrylic fibers and granular polyacrylonitriles
    • Tauber M, Cavaco-Paulo A, Robra K, Gubitz G (2000) Nitrile hydratase and amidase from Rhodococcus rhodochrous hydrolyze acrylic fibers and granular polyacrylonitriles. Appl Environ Microbiol 66:1634-1638
    • (2000) Appl Environ Microbiol , vol.66 , pp. 1634-1638
    • Tauber, M.1    Cavaco-Paulo, A.2    Robra, K.3    Gubitz, G.4
  • 98
    • 50549217552 scopus 로고
    • Nitrilase II, its substrate specificity and possible mode of action
    • Thimann K, Mahadevan S (1964) Nitrilase II, its substrate specificity and possible mode of action. Arch Biochem Biophys 107:62-68
    • (1964) Arch Biochem Biophys , vol.107 , pp. 62-68
    • Thimann, K.1    Mahadevan, S.2
  • 99
    • 0034927277 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of an enantioselective amidase from Agrobacterium tumefaciens strain d3
    • Trott S, Bauer R, Knackmuss H, Stolz A (2001) Genetic and biochemical characterization of an enantioselective amidase from Agrobacterium tumefaciens strain d3. Microbiology 147:1815-1824
    • (2001) Microbiology , vol.147 , pp. 1815-1824
    • Trott, S.1    Bauer, R.2    Knackmuss, H.3    Stolz, A.4
  • 101
    • 0026471564 scopus 로고
    • Purification and characterization of cyanide hydratase from phytopathogenic fungus Gloeocercospora sorghi
    • Wang P, Matthews D, Van Etten H (1992) Purification and characterization of cyanide hydratase from phytopathogenic fungus Gloeocercospora sorghi. Arch Biochem Biophys 298:569-575
    • (1992) Arch Biochem Biophys , vol.298 , pp. 569-575
    • Wang, P.1    Matthews, D.2    Van Etten, H.3
  • 103
    • 0029102389 scopus 로고
    • Microbial degradation of acrylonitrile waste effluents: The degradation of effluents and condensates from the manufacture of acrylonitrile
    • Wyatt J, Knowles C (1995) Microbial degradation of acrylonitrile waste effluents: the degradation of effluents and condensates from the manufacture of acrylonitrile. Int Biodeterior Biodegrad 35:227-248
    • (1995) Int Biodeterior Biodegrad , vol.35 , pp. 227-248
    • Wyatt, J.1    Knowles, C.2
  • 104
    • 0030250538 scopus 로고    scopus 로고
    • Nitrile hydratase and its application to industrial production of acrylamide
    • 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
  • 105
    • 0011150433 scopus 로고
    • Process for biological production of amides with R. rhodochrous J1. US Patent 5334519
    • Yamada H, Nagasawa T (1994) Process for biological production of amides with R. rhodochrous J1. US Patent 5334519
    • (1994)
    • Yamada, H.1    Nagasawa, T.2
  • 106
    • 0030944711 scopus 로고    scopus 로고
    • Cloning and sequencing of a nitrile hydratase gene from Pseudonocardia thermophila JCM3095
    • Yamaki T, Olikawa T, Ito K, Nakamura T (1997) Cloning and sequencing of a nitrile hydratase gene from Pseudonocardia thermophila JCM3095. J Ferment Bioeng 83:474-477
    • (1997) J Ferment Bioeng , vol.83 , pp. 474-477
    • Yamaki, T.1    Olikawa, T.2    Ito, K.3    Nakamura, T.4
  • 107
    • 0026178875 scopus 로고
    • Purification and characterization of nitrilase responsible for the hydrolysis from Acinetobacter sp. AK 226
    • Yamamoto K, Komatsu K (1991) Purification and characterization of nitrilase responsible for the hydrolysis from Acinetobacter sp. AK 226. Agric Biol Chem 55:1459-1466
    • (1991) Agric Biol Chem , vol.55 , pp. 1459-1466
    • Yamamoto, K.1    Komatsu, K.2
  • 108
    • 0025166753 scopus 로고    scopus 로고
    • Production of S-(+)- Ibuprofen from a nitrile compound by Acinetobacter sp. strain AK226
    • Yamamoto K, Ueno Y, Otsubo K, Kawakami K, Komatsu K (1990) Production of S-(+)- Ibuprofen from a nitrile compound by Acinetobacter sp. strain AK226. Appl Environ Microbiol 56:3125-3129
    • Appl Environ Microbiol , vol.56 , pp. 3125-3129
    • Yamamoto, K.1    Ueno, Y.2    Otsubo, K.3    Kawakami, K.4    Komatsu, K.5
  • 109
    • 0025953031 scopus 로고
    • Production of R-(-)- mandelic acid from mandelonitrile by Alcaligenes faecalis ATCC 8750
    • Yamamoto K, Oishi K, Fujimatsu I, Komatsu K (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.4
  • 110
    • 0026632716 scopus 로고
    • Purification and characterization of the nitrilase from Alcaligenes faecalis ATCC 8750 responsible for enantioselective hydrolysis of mandelonitrile
    • Yamamoto K, Fujimatsu I, Komatsu K (1992a) 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.3
  • 111
    • 0026549043 scopus 로고
    • Efficient conversion of dinitrile to mononitrile-monocarboxylic acid by Corynebacterium sp. C5 cells during tranexamic acid synthesis
    • Yamamoto K, Ueno Y, Otsubo K, Yamane H, Komatsu K, Tani Y (1992b) Efficient conversion of dinitrile to mononitrile-monocarboxylic acid by Corynebacterium sp. C5 cells during tranexamic acid synthesis. J Ferment Bioeng 73:125-129
    • (1992) J Ferment Bioeng , vol.73 , pp. 125-129
    • Yamamoto, K.1    Ueno, Y.2    Otsubo, K.3    Yamane, H.4    Komatsu, K.5    Tani, Y.6
  • 112
    • 0011131695 scopus 로고    scopus 로고
    • Nitrilase gene. US Patent 5872000
    • Yu F (1999) Nitrilase gene. US Patent 5872000
    • (1999)
    • Yu, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.