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Volumn 346, Issue 1, 2005, Pages 49-58

Application of Fourier transform infrared spectroscopy for monitoring hydrolysis and synthesis reactions catalyzed by a recombinant amidase

Author keywords

Amides; Fourier transform infrared spectroscopy; Hydrolysis; Hydroxamic acids; Kinetics; Recombinant amidase; Synthesis

Indexed keywords

AMIDES; AMINES; AMINO ACIDS; CATALYSIS; ENZYME ACTIVITY; ENZYME KINETICS; ESTERS; HYDROLYSIS; SUBSTRATES; SYNTHESIS (CHEMICAL);

EID: 26844556854     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2005.07.027     Document Type: Article
Times cited : (36)

References (56)
  • 1
    • 0030700490 scopus 로고    scopus 로고
    • Identification of active sites in amidase: Evolutionary relationship between amide bond- and peptide bond-cleaving enzymes
    • M. Kobayashi, Y. Fujiwara, M. Goda, H. Komeda, and S. Shimizu Identification of active sites in amidase: evolutionary relationship between amide bond- and peptide bond-cleaving enzymes Proc. Natl. Acad. Sci. USA 94 1997 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
  • 2
    • 0025779290 scopus 로고
    • Simultaneous degradation of acetonitrile and biphenyl by Pseudomonas aeruginosa
    • M.S. Nawaz, and K.D. Chapatwala Simultaneous degradation of acetonitrile and biphenyl by Pseudomonas aeruginosa Can. J. Microbiol. 37 1991 411 418
    • (1991) Can. J. Microbiol. , vol.37 , pp. 411-418
    • Nawaz, M.S.1    Chapatwala, K.D.2
  • 5
    • 0029904838 scopus 로고    scopus 로고
    • Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides
    • B.F. Cravatt, D.K. Giang, S.P. Mayfield, D.L. Boger, R.A. Lerner, and N.B. Gilula Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides Nature 384 1996 83 87
    • (1996) Nature , vol.384 , pp. 83-87
    • Cravatt, B.F.1    Giang, D.K.2    Mayfield, S.P.3    Boger, D.L.4    Lerner, R.A.5    Gilula, N.B.6
  • 6
    • 0001048154 scopus 로고    scopus 로고
    • Distribution of anandamide amidohydrolase in rat tissues with special reference to small intestine
    • K. Katayama, N. Ueda, Y. Kuraishi, H. Suzuki, S. Yamamoto, and I. Kato Distribution of anandamide amidohydrolase in rat tissues with special reference to small intestine Biochim. Biophys. Acta 1347 1997 212 218
    • (1997) Biochim. Biophys. Acta , vol.1347 , pp. 212-218
    • Katayama, K.1    Ueda, N.2    Kuraishi, Y.3    Suzuki, H.4    Yamamoto, S.5    Kato, I.6
  • 9
    • 0022397667 scopus 로고
    • Nucleotide sequences of the Pseudomonas savastanoi indoleacetic acid genes show homology with Agrobacterium tumefaciens T-DNA
    • T. Yamada, C.J. Palm, B. Brooks, and T. Kosuge Nucleotide sequences of the Pseudomonas savastanoi indoleacetic acid genes show homology with Agrobacterium tumefaciens T-DNA Proc. Natl. Acad. Sci. USA 82 1985 6522 6526
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 6522-6526
    • Yamada, T.1    Palm, C.J.2    Brooks, B.3    Kosuge, T.4
  • 10
    • 0024979246 scopus 로고
    • Transfer and function of T-DNA genes from Agrobacterium Ti and Ri plasmids in plants
    • P. Zambryski, J. Tempe, and J. Schell Transfer and function of T-DNA genes from Agrobacterium Ti and Ri plasmids in plants Cell 56 1989 193 201
    • (1989) Cell , vol.56 , pp. 193-201
    • Zambryski, P.1    Tempe, J.2    Schell, J.3
  • 11
    • 0031879561 scopus 로고    scopus 로고
    • Metalloenzyme nitrile hydratase: Structure, regulation, and application to biotechnology
    • M. Kobayashi, and S. Shimizu Metalloenzyme nitrile hydratase: structure, regulation, and application to biotechnology Nat. Biotechnol. 16 1998 733 736
    • (1998) Nat. Biotechnol. , vol.16 , pp. 733-736
    • Kobayashi, M.1    Shimizu, S.2
  • 12
    • 0030250538 scopus 로고    scopus 로고
    • Nitrile hydratase and its application to industrial production of acrylamide
    • H. Yamada, and M. Kobayashi Nitrile hydratase and its application to industrial production of acrylamide Biosci. Biotechnol. Biochem. 60 1996 1391 1400
    • (1996) Biosci. Biotechnol. Biochem. , vol.60 , pp. 1391-1400
    • Yamada, H.1    Kobayashi, M.2
  • 13
    • 0026480892 scopus 로고
    • Enzymatic synthesis of acrylamide: A success story not yet over
    • M. Kobayashi, T. Nagasawa, and H. Yamada Enzymatic synthesis of acrylamide: a success story not yet over Trends Biotechnol. 10 1992 402 408
    • (1992) Trends Biotechnol. , vol.10 , pp. 402-408
    • Kobayashi, M.1    Nagasawa, T.2    Yamada, H.3
  • 14
    • 2642639983 scopus 로고
    • Biocatalyst production
    • J.M.S. Cabral D. Best L. Boross J. Tramper Harwood Academic Chur, Switzerland
    • W.J.J. Van den Tweel, D. Leak, B. Bielecki, and S. Pedersen Biocatalyst production J.M.S. Cabral D. Best L. Boross J. Tramper Applied Biocatalysis 1994 Harwood Academic Chur, Switzerland 157 237
    • (1994) Applied Biocatalysis , pp. 157-237
    • Van Den Tweel, W.J.J.1    Leak, D.2    Bielecki, B.3    Pedersen, S.4
  • 15
    • 0029616106 scopus 로고
    • Purification and characterization of a newly screened microbial peptide amidase
    • U. Stelkes-Ritter, K. Wyzgol, and M.R. Kula Purification and characterization of a newly screened microbial peptide amidase Appl. Microbiol. Biotechnol. 44 1995 393 398
    • (1995) Appl. Microbiol. Biotechnol. , vol.44 , pp. 393-398
    • Stelkes-Ritter, U.1    Wyzgol, K.2    Kula, M.R.3
  • 17
    • 0015912114 scopus 로고
    • The subunit structure of the aliphatic amidase from P. aeruginosa
    • P.R. Brown, M.J. Smyth, P.H. Clarke, and M.A. Rosemeyer The subunit structure of the aliphatic amidase from P. aeruginosa Eur. J. Biochem. 34 1973 177 187
    • (1973) Eur. J. Biochem. , vol.34 , pp. 177-187
    • Brown, P.R.1    Smyth, M.J.2    Clarke, P.H.3    Rosemeyer, M.A.4
  • 18
    • 0037450059 scopus 로고    scopus 로고
    • Enhancement of the thermalstability and catalytic activity of d-stereospecific amino-acid amidase from Ochrobacterium anthropi SV3 by directed evolution
    • H. Komeda, N. Ishikawa, and Y. Asano Enhancement of the thermalstability and catalytic activity of d-stereospecific amino-acid amidase from Ochrobacterium anthropi SV3 by directed evolution J. Mol. Catalysis B Enzymatic 21 2003 283 290
    • (2003) J. Mol. Catalysis B Enzymatic , vol.21 , pp. 283-290
    • Komeda, H.1    Ishikawa, N.2    Asano, Y.3
  • 19
    • 0037413411 scopus 로고    scopus 로고
    • New thermostable d-methioninamidase from Brevibacillus borstelensis BCS-1 and its application for d-phenylalanine production
    • D.H. Baek, J.J. Sing, S.-G. Lee, S.J. Kwon, Y. Asano, and M.-H. Sung New thermostable d-methioninamidase from Brevibacillus borstelensis BCS-1 and its application for d-phenylalanine production Enzyme Microbiol. Technol. 32 2003 131 139
    • (2003) Enzyme Microbiol. Technol. , vol.32 , pp. 131-139
    • Baek, D.H.1    Sing, J.J.2    Lee, S.-G.3    Kwon, S.J.4    Asano, Y.5    Sung, M.-H.6
  • 21
    • 0014552729 scopus 로고
    • Butyramide-utilizing mutants of Pseudomonas aeruginosa 8602 which produce an amidase with altered substrate specificity
    • J.E. Brown, P.R. Brown, and P.H. Clarke Butyramide-utilizing mutants of Pseudomonas aeruginosa 8602 which produce an amidase with altered substrate specificity J. Gen. Microbiol. 57 1969 273 295
    • (1969) J. Gen. Microbiol. , vol.57 , pp. 273-295
    • Brown, J.E.1    Brown, P.R.2    Clarke, P.H.3
  • 22
    • 0014914964 scopus 로고
    • Mutations in a regulator gene allowing P. aeruginosa 8602 to grow on butyramide
    • J.E. Brown, and P.H. Clarke Mutations in a regulator gene allowing P. aeruginosa 8602 to grow on butyramide J. Gen. Microbiol. 64 1970 329 342
    • (1970) J. Gen. Microbiol. , vol.64 , pp. 329-342
    • Brown, J.E.1    Clarke, P.H.2
  • 23
    • 0015328697 scopus 로고
    • Amino acid substitution in an amidase produced by an acetanilide- utilizing mutant of Pseudomonas aeruginosa
    • P.R. Brown, and P.H. Clarke Amino acid substitution in an amidase produced by an acetanilide-utilizing mutant of Pseudomonas aeruginosa J. Gen. Microbiol. 70 1972 287 298
    • (1972) J. Gen. Microbiol. , vol.70 , pp. 287-298
    • Brown, P.R.1    Clarke, P.H.2
  • 24
    • 0015427221 scopus 로고
    • Selective evolution of phenylacetamide-utilizing strains of Pseudomonas aeruginosa
    • J.L. Betz, and P.H. Clarke Selective evolution of phenylacetamide- utilizing strains of Pseudomonas aeruginosa J. Gen. Microbiol. 73 1972 161 174
    • (1972) J. Gen. Microbiol. , vol.73 , pp. 161-174
    • Betz, J.L.1    Clarke, P.H.2
  • 25
    • 0028201442 scopus 로고
    • Arg-188 and Trp-144 are implicated in the binding of urea and acetamide to the active site of the amidase from Pseudomonas aeruginosa
    • R. Tata, P. Marsh, and P.R. Brown Arg-188 and Trp-144 are implicated in the binding of urea and acetamide to the active site of the amidase from Pseudomonas aeruginosa Biochim. Biophys. Acta 1205 1994 139 145
    • (1994) Biochim. Biophys. Acta , vol.1205 , pp. 139-145
    • Tata, R.1    Marsh, P.2    Brown, P.R.3
  • 26
    • 0036684532 scopus 로고    scopus 로고
    • Support for a three dimensional structure predicting a Cys-Glu-Lys catalytic triad for Pseudomonas aeruginosa amidase comes from site-directed mutagenesis and mutations altering substrate specificity
    • C. Novo, S. Farnaud, R. Tata, A. Clemente, and P.R. Brown Support for a three dimensional structure predicting a Cys-Glu-Lys catalytic triad for Pseudomonas aeruginosa amidase comes from site-directed mutagenesis and mutations altering substrate specificity Biochem. J. 365 2002 731 738
    • (2002) Biochem. J. , vol.365 , pp. 731-738
    • Novo, C.1    Farnaud, S.2    Tata, R.3    Clemente, A.4    Brown, P.R.5
  • 27
    • 0034966202 scopus 로고    scopus 로고
    • Substitutions of Thr-103-Ile and Trp-138-Gly in amidase from Pseudomonas aeruginosa are responsible for altered kinetics properties and enzyme instability
    • A. Karmali, R. Pacheco, R. Tata, and P.R. Brown Substitutions of Thr-103-Ile and Trp-138-Gly in amidase from Pseudomonas aeruginosa are responsible for altered kinetics properties and enzyme instability Mol. Biotechnol. 17 2001 200 212
    • (2001) Mol. Biotechnol. , vol.17 , pp. 200-212
    • Karmali, A.1    Pacheco, R.2    Tata, R.3    Brown, P.R.4
  • 28
    • 0022724718 scopus 로고
    • Enzymes that work in organic solvents
    • A.M. Klibanov Enzymes that work in organic solvents Chemtech. 16 1986 354 359
    • (1986) Chemtech. , vol.16 , pp. 354-359
    • Klibanov, A.M.1
  • 29
    • 1842479434 scopus 로고    scopus 로고
    • Biocatalysis and biotransformation: Probing the potential usefulness and the mechanisms of action of some novel biocatalysts
    • B. Hauer, and S.M. Roberts Biocatalysis and biotransformation: probing the potential usefulness and the mechanisms of action of some novel biocatalysts Curr. Opin. Chem. Biol. 8 2004 103 105
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 103-105
    • Hauer, B.1    Roberts, S.M.2
  • 30
    • 0035313031 scopus 로고    scopus 로고
    • Biocatalysis and biotransformation: From discovery to application
    • W.D. Fessner, and J.B. Jones Biocatalysis and biotransformation: from discovery to application Curr. Opin. Chem. Biol. 5 2001 103
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 103
    • Fessner, W.D.1    Jones, J.B.2
  • 31
    • 0000611901 scopus 로고
    • An inducible amidase produced by a strain of Pseudomonas aeruginosa
    • M. Kelly, and P.H. Clarke An inducible amidase produced by a strain of Pseudomonas aeruginosa J. Gen. Microbiol. 27 1962 305 316
    • (1962) J. Gen. Microbiol. , vol.27 , pp. 305-316
    • Kelly, M.1    Clarke, P.H.2
  • 32
  • 33
    • 0000527093 scopus 로고
    • Induction and repression of Pseudomonas aeruginosa amidase
    • W.J. Brammar, and P.H. Clarke Induction and repression of Pseudomonas aeruginosa amidase J. Gen. Microbiol. 37 1964 307 319
    • (1964) J. Gen. Microbiol. , vol.37 , pp. 307-319
    • Brammar, W.J.1    Clarke, P.H.2
  • 35
    • 0034113199 scopus 로고    scopus 로고
    • Real-time monitoring of nitrile biotransformations by mid-infrared spectroscopy
    • M.R. Dadd, D.C. Sharp, A.J. Pettman, and C.J. Knowles Real-time monitoring of nitrile biotransformations by mid-infrared spectroscopy J. Microbiol. Methods 41 2000 69 75
    • (2000) J. Microbiol. Methods , vol.41 , pp. 69-75
    • Dadd, M.R.1    Sharp, D.C.2    Pettman, A.J.3    Knowles, C.J.4
  • 36
    • 0037045841 scopus 로고    scopus 로고
    • Application of infrared spectroscopy (attenuated total reflection) for monitoring enzymatic activity on substrate films
    • T. Snabe, and S.B. Petersen Application of infrared spectroscopy (attenuated total reflection) for monitoring enzymatic activity on substrate films J. Biotechnol. 95 2002 145 155
    • (2002) J. Biotechnol. , vol.95 , pp. 145-155
    • Snabe, T.1    Petersen, S.B.2
  • 37
    • 0036670581 scopus 로고    scopus 로고
    • Direct measurement of enzyme activity with infrared spectroscopy
    • D. Thoenges, and A. Barth Direct measurement of enzyme activity with infrared spectroscopy J. Biomol. Screen. 7 2002 353 357
    • (2002) J. Biomol. Screen. , vol.7 , pp. 353-357
    • Thoenges, D.1    Barth, A.2
  • 38
    • 0028533668 scopus 로고
    • Fourier-transform infrared assay of bile salt-stimulated lipase activity in reversed micelles
    • C.J. O'Connor, and D.R. Cleverly Fourier-transform infrared assay of bile salt-stimulated lipase activity in reversed micelles J. Chem. Technol. Biotechnol. 61 1994 209 214
    • (1994) J. Chem. Technol. Biotechnol. , vol.61 , pp. 209-214
    • O'Connor, C.J.1    Cleverly, D.R.2
  • 39
    • 0032546860 scopus 로고    scopus 로고
    • Simultaneous determination of α-amylase and amyloglucosidase activities using flow injection analysis with FTIR detection and partial least-squares data treatment
    • R. Schindler, B. Lendl, and R. Kellner Simultaneous determination of α-amylase and amyloglucosidase activities using flow injection analysis with FTIR detection and partial least-squares data treatment Anal. Chim. Acta 366 1998 35 43
    • (1998) Anal. Chim. Acta , vol.366 , pp. 35-43
    • Schindler, R.1    Lendl, B.2    Kellner, R.3
  • 40
    • 0032918774 scopus 로고    scopus 로고
    • Simultaneous determination of enzyme activities by FTIR-spectroscopy in a one-step assay
    • R. Schindler, and B. Lendl Simultaneous determination of enzyme activities by FTIR-spectroscopy in a one-step assay Anal. Chim. Acta 391 1999 19 28
    • (1999) Anal. Chim. Acta , vol.391 , pp. 19-28
    • Schindler, R.1    Lendl, B.2
  • 41
    • 0031423671 scopus 로고    scopus 로고
    • Infrared spectroscopy: A new frontier in medicine
    • M. Jackson, M.G. Sowa, and H.H. Mantsch Infrared spectroscopy: a new frontier in medicine Biophys. Chem. 68 1997 109 125
    • (1997) Biophys. Chem. , vol.68 , pp. 109-125
    • Jackson, M.1    Sowa, M.G.2    Mantsch, H.H.3
  • 42
    • 0032818805 scopus 로고    scopus 로고
    • FTIR spectroscopy characterization of protein structure in aqueous and non-aqueous media
    • P.I. Haris, and F. Severcan FTIR spectroscopy characterization of protein structure in aqueous and non-aqueous media J. Mol. Catalysis B Enzymatic 7 1999 207 221
    • (1999) J. Mol. Catalysis B Enzymatic , vol.7 , pp. 207-221
    • Haris, P.I.1    Severcan, F.2
  • 43
    • 0142257962 scopus 로고    scopus 로고
    • Measuring enzymatic activity of a recombinant amidase using fourier transform infrared spectroscopy
    • R. Pacheco, M.L.M. Serralheiro, A. Karmali, and P.I. Haris Measuring enzymatic activity of a recombinant amidase using fourier transform infrared spectroscopy Anal. Biochem. 322 2003 208 214
    • (2003) Anal. Biochem. , vol.322 , pp. 208-214
    • Pacheco, R.1    Serralheiro, M.L.M.2    Karmali, A.3    Haris, P.I.4
  • 44
    • 0015816669 scopus 로고
    • Transition-state analogs of an aliphatic amidase
    • J. Findlater, and B. Orsi Transition-state analogs of an aliphatic amidase FEBS Lett. 35 1973 109 111
    • (1973) FEBS Lett. , vol.35 , pp. 109-111
    • Findlater, J.1    Orsi, B.2
  • 46
    • 0001328722 scopus 로고
    • Aliphatic nitrile hydratase from Arthrobacter sp. J-1: Purification and characterization
    • Y. Asano, K. Fujishiro, Y. Tani, and H. Yamada Aliphatic nitrile hydratase from Arthrobacter sp. J-1: purification and characterization Agric. Biol. Chem. 46 1982 1165 1181
    • (1982) Agric. Biol. Chem. , vol.46 , pp. 1165-1181
    • Asano, Y.1    Fujishiro, K.2    Tani, Y.3    Yamada, H.4
  • 47
    • 0022764953 scopus 로고
    • Purification and characterization of N,N-dimethylformamidase from Pseudomonas DMF 3/3
    • H.P. Schar, W. Holzmann, G.M. Ramos Tombo, and O. Ghisalb Purification and characterization of N,N-dimethylformamidase from Pseudomonas DMF 3/3 Eur. J. Biochem. 158 1986 469 475
    • (1986) Eur. J. Biochem. , vol.158 , pp. 469-475
    • Schar, H.P.1    Holzmann, W.2    Ramos Tombo, G.M.3    Ghisalb, O.4
  • 49
    • 0018399804 scopus 로고
    • Inhibition of the aliphatic amidase from Pseudomonas aeruginosa by urea and related compounds
    • M. Gregoriou, and P.R. Brown Inhibition of the aliphatic amidase from Pseudomonas aeruginosa by urea and related compounds Eur. J. Biochem. 96 1979 101 108
    • (1979) Eur. J. Biochem. , vol.96 , pp. 101-108
    • Gregoriou, M.1    Brown, P.R.2
  • 51
    • 0001245278 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 101 1976 200 203
    • (1976) Anal. Biochem. , vol.101 , pp. 200-203
    • Bradford, M.M.1
  • 52
    • 0001232852 scopus 로고
    • An introduction to polyacrylamide gel electrophoresis
    • B.D. Hames D. Rickwood IRL Press Oxford, UK
    • B.D. Hames An introduction to polyacrylamide gel electrophoresis B.D. Hames D. Rickwood Gel Electrophoresis of Proteins: A Practical Approach 1981 IRL Press Oxford, UK 1 86
    • (1981) Gel Electrophoresis of Proteins: A Practical Approach , pp. 1-86
    • Hames, B.D.1
  • 53
    • 0004139637 scopus 로고
    • fourth ed. Ellis Horwood/Prentice Hall New York
    • T. Palmer Understanding Enzymes fourth ed. 1995 Ellis Horwood/Prentice Hall New York
    • (1995) Understanding Enzymes
    • Palmer, T.1
  • 54
    • 0029585123 scopus 로고
    • Atom/Fragment contribution method for estimating octanol-water partition coefficients
    • W.M. Meylan, and P.H. Howard Atom/Fragment contribution method for estimating octanol-water partition coefficients J. Pharm. Sci. 84 1995 83 92
    • (1995) J. Pharm. Sci. , vol.84 , pp. 83-92
    • Meylan, W.M.1    Howard, P.H.2
  • 55
    • 0031879459 scopus 로고    scopus 로고
    • Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: Formation of a wide range of hydroxamic acids
    • D. Fournand, F. Bigey, and A. Arnaud Acyl transfer activity of an amidase from Rhodococcus sp. strain R312: formation of a wide range of hydroxamic acids Appl. Environ. Microbiol. 64 1998 2844 2852
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 2844-2852
    • Fournand, D.1    Bigey, F.2    Arnaud, A.3
  • 56
    • 0014211618 scopus 로고
    • On the size of the active site in proteases: I. papain
    • I. Schechter, and A. Berger On the size of the active site in proteases: I. papain Biochem. Biophys. Res. Commun. 27 1967 157 162
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2


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