메뉴 건너뛰기




Volumn 92, Issue 7, 2010, Pages 779-788

Characterization of a unique proline iminopeptidase from white-rot basidiomycetes Phanerochaete chrysosporium

Author keywords

Characterization; Mutation; Phanerochaete chrysosporium; Proline iminopeptidase; Transcription

Indexed keywords

4 NITROANILIDE TRIFLUOROACETATE; ALANYLALANYLPROLYLLEUCINE; ALANYLALANYLVALINE; ALANYLALANYLVALYLALANINE; ALUMINUM; AMINO ACID DERIVATIVE; BARIUM; CALCIUM; COBALT; COMPLEMENTARY DNA; COPPER; FERRIC ION; FERROUS ION; HISTIDINE; LEUCINE; LYSINE; MAGNESIUM; MANGANESE; MERCURY; NICKEL; OLIGOPEPTIDE; PEPTIDE DERIVATIVE; PHENYLALANINE; PROLINE IMINOPEPTIDASE; RECOMBINANT ENZYME; TRIFLUOROACETIC ACID; TRIGLYCINE; TYROSINE; UNCLASSIFIED DRUG; ZINC; AMINOPEPTIDASE; METAL; PEPTIDE;

EID: 77953503349     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2010.02.022     Document Type: Article
Times cited : (21)

References (58)
  • 3
    • 0034773313 scopus 로고    scopus 로고
    • Proteolytic degradation of cereal prolamins-the problem with proline
    • Simpson D.J. Proteolytic degradation of cereal prolamins-the problem with proline. Plant Sci. 2001, 161:825-838.
    • (2001) Plant Sci. , vol.161 , pp. 825-838
    • Simpson, D.J.1
  • 4
    • 0027368493 scopus 로고
    • Molecular cloning and characterization of a proline iminopeptidase gene from Neisseria gonorrhoeae
    • Albertson N.H., Koomey M. Molecular cloning and characterization of a proline iminopeptidase gene from Neisseria gonorrhoeae. Mol. Microbiol. 1993, 9:1203-1211.
    • (1993) Mol. Microbiol. , vol.9 , pp. 1203-1211
    • Albertson, N.H.1    Koomey, M.2
  • 5
    • 0030878785 scopus 로고    scopus 로고
    • Prolyl aminopeptidase from Serratia marcescens: cloning of the enzyme gene and crystallization of the expressed enzyme
    • Kabashima T., Kitazono A., Kitano A., Ito K., Yoshimoto T. Prolyl aminopeptidase from Serratia marcescens: cloning of the enzyme gene and crystallization of the expressed enzyme. J. Biochem. 1997, 122:601-605.
    • (1997) J. Biochem. , vol.122 , pp. 601-605
    • Kabashima, T.1    Kitazono, A.2    Kitano, A.3    Ito, K.4    Yoshimoto, T.5
  • 6
    • 0030001703 scopus 로고    scopus 로고
    • Prolyl aminopeptidase is also present in Enterobacteriaceae: cloning and sequencing of the Hafnia alvei enzyme-gene and characterization of the expressed enzyme
    • Kitazono A., Kitano A., Kabashima T., Ito K., Yoshimoto T. Prolyl aminopeptidase is also present in Enterobacteriaceae: cloning and sequencing of the Hafnia alvei enzyme-gene and characterization of the expressed enzyme. J. Biochem. 1996, 119:468-474.
    • (1996) J. Biochem. , vol.119 , pp. 468-474
    • Kitazono, A.1    Kitano, A.2    Kabashima, T.3    Ito, K.4    Yoshimoto, T.5
  • 7
    • 0037224855 scopus 로고    scopus 로고
    • Purification and characterization of a prolyl aminopeptidase from Debaryomyces hansenii
    • Bolumar T., Sanz Y., Aristoy M.C., Toldra F. Purification and characterization of a prolyl aminopeptidase from Debaryomyces hansenii. Appl. Environ. Microbiol. 2003, 69:227-232.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 227-232
    • Bolumar, T.1    Sanz, Y.2    Aristoy, M.C.3    Toldra, F.4
  • 9
    • 0028131772 scopus 로고
    • Rapid detection of proline iminopeptidase as an indicator of Eikenella corrodens periodontal infection
    • Allaker R.P., Young K.A., Hardie J.M. Rapid detection of proline iminopeptidase as an indicator of Eikenella corrodens periodontal infection. Lett. Appl. Microbiol. 1994, 19:325-327.
    • (1994) Lett. Appl. Microbiol. , vol.19 , pp. 325-327
    • Allaker, R.P.1    Young, K.A.2    Hardie, J.M.3
  • 10
    • 34250638945 scopus 로고    scopus 로고
    • A proline iminopeptidase gene upregulated in planta by a LuxR homologue is essential for pathogenicity of Xanthomonas campestris pv. Campestris
    • Zhang L., Jia Y., Wang L., Wang R. A proline iminopeptidase gene upregulated in planta by a LuxR homologue is essential for pathogenicity of Xanthomonas campestris pv. Campestris. Mol. Microbiol. 2007, 65:121-136.
    • (2007) Mol. Microbiol. , vol.65 , pp. 121-136
    • Zhang, L.1    Jia, Y.2    Wang, L.3    Wang, R.4
  • 12
    • 31644441857 scopus 로고    scopus 로고
    • Enzymatic debittering of food protein hydrolysates
    • FitzGerald R.J., O'Cuinn G. Enzymatic debittering of food protein hydrolysates. Biotechnol. Adv. 2006, 24:234-237.
    • (2006) Biotechnol. Adv. , vol.24 , pp. 234-237
    • FitzGerald, R.J.1    O'Cuinn, G.2
  • 14
    • 0031767739 scopus 로고    scopus 로고
    • Cloning, expression, and chromosomal stabilization of the Propionibacterium shermanii proline iminopeptidase gene (pip) for food-grade application in Lactococcus lactis
    • Leenhouts K., Bolhuis A., Boot J., Deutz I., Toonen M., Venema G., Kok J., Ledeboer A. Cloning, expression, and chromosomal stabilization of the Propionibacterium shermanii proline iminopeptidase gene (pip) for food-grade application in Lactococcus lactis. Appl. Environ. Microbiol. 1998, 64:4736-4742.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 4736-4742
    • Leenhouts, K.1    Bolhuis, A.2    Boot, J.3    Deutz, I.4    Toonen, M.5    Venema, G.6    Kok, J.7    Ledeboer, A.8
  • 15
    • 0034847821 scopus 로고    scopus 로고
    • Debittering and hydrolysis of a tryptic hydrolasate of β-casein with purified general and proline specific aminopeptidases from Lactococcus lactis ssp. Cremoris AM2
    • Bouchier P.J., O'Cuinn G., Harrington D., FitzGerald R.J. Debittering and hydrolysis of a tryptic hydrolasate of β-casein with purified general and proline specific aminopeptidases from Lactococcus lactis ssp. Cremoris AM2. J. Food Sci. 2006, 66:816-820.
    • (2006) J. Food Sci. , vol.66 , pp. 816-820
    • Bouchier, P.J.1    O'Cuinn, G.2    Harrington, D.3    FitzGerald, R.J.4
  • 16
    • 33845956242 scopus 로고    scopus 로고
    • Extracellular oxidative systems of the lignin-degrading basidiomycete Phanerochaete chrysosporium
    • Kersten P., Cullen D. Extracellular oxidative systems of the lignin-degrading basidiomycete Phanerochaete chrysosporium. Fung. Genet. Biol. 2007, 44:77-87.
    • (2007) Fung. Genet. Biol. , vol.44 , pp. 77-87
    • Kersten, P.1    Cullen, D.2
  • 17
    • 0027180067 scopus 로고
    • Molecular biology of the lignin-degrading basidiomycete Phanerochaete chrysosporium
    • Gold M.H., Alic M. Molecular biology of the lignin-degrading basidiomycete Phanerochaete chrysosporium. Microbiol. Rev. 1993, 57:605-622.
    • (1993) Microbiol. Rev. , vol.57 , pp. 605-622
    • Gold, M.H.1    Alic, M.2
  • 18
    • 0026547329 scopus 로고
    • Purification and characterization of a novel protease from solid substrate cultures of Phanerochaete chrysosporium
    • Datta A. Purification and characterization of a novel protease from solid substrate cultures of Phanerochaete chrysosporium. J. Biochem. 1992, 267:728-736.
    • (1992) J. Biochem. , vol.267 , pp. 728-736
    • Datta, A.1
  • 19
    • 0028914389 scopus 로고
    • Extracellular proteases produced by the wood-degrading fungus Phanerochaete chrysosporium under ligninolytic and non-ligninolytic conditions
    • Dass B.S., Dosoretz C.G., Reddy C.A., Grethlein H.E. Extracellular proteases produced by the wood-degrading fungus Phanerochaete chrysosporium under ligninolytic and non-ligninolytic conditions. Arch. Microbiol. 1995, 163:254-258.
    • (1995) Arch. Microbiol. , vol.163 , pp. 254-258
    • Dass, B.S.1    Dosoretz, C.G.2    Reddy, C.A.3    Grethlein, H.E.4
  • 20
    • 34948842973 scopus 로고    scopus 로고
    • Expression analysis of extracellular proteins from Phanerochaete chrysosporium grown on different liquid and solid substrates
    • Sato S., Liu F., Koc H., Tien M. Expression analysis of extracellular proteins from Phanerochaete chrysosporium grown on different liquid and solid substrates. Microbiology 2007, 153:3023-3033.
    • (2007) Microbiology , vol.153 , pp. 3023-3033
    • Sato, S.1    Liu, F.2    Koc, H.3    Tien, M.4
  • 21
    • 69749084914 scopus 로고
    • Lignin peroxidase of Phanerochaete chrysosporium
    • Tien M., Kirk T.K. Lignin peroxidase of Phanerochaete chrysosporium. Meth. Enzymol. 1988, 161:238-249.
    • (1988) Meth. Enzymol. , vol.161 , pp. 238-249
    • Tien, M.1    Kirk, T.K.2
  • 22
    • 20444407690 scopus 로고    scopus 로고
    • Analysis of 5'-upstream regulatory sequences of lignin peroxidase (LIP) genes of Phanerochaete chrysosporium
    • Feng H., Zhang Y.Z. Analysis of 5'-upstream regulatory sequences of lignin peroxidase (LIP) genes of Phanerochaete chrysosporium. Acta Biochim. Biophys. Sin. 1999, 31:669-674.
    • (1999) Acta Biochim. Biophys. Sin. , vol.31 , pp. 669-674
    • Feng, H.1    Zhang, Y.Z.2
  • 24
    • 70350680581 scopus 로고    scopus 로고
    • Substrate specificity and thermostability of the dehairing alkaline protease from Bacillus pumilus
    • Wan M.Y., Wang H.Y., Zhang Y.Z., Feng H. Substrate specificity and thermostability of the dehairing alkaline protease from Bacillus pumilus. Appl. Biochem. Biotechnol. 2009, 59:394-403.
    • (2009) Appl. Biochem. Biotechnol. , vol.59 , pp. 394-403
    • Wan, M.Y.1    Wang, H.Y.2    Zhang, Y.Z.3    Feng, H.4
  • 26
    • 0035172280 scopus 로고    scopus 로고
    • The characterization of a (nutritionally important) proline iminopeptidase from Eikenella corrodens
    • Gully N.J., Rogers A.H. The characterization of a (nutritionally important) proline iminopeptidase from Eikenella corrodens. Oral Microbiol. Immunol. 2001, 16:370-375.
    • (2001) Oral Microbiol. Immunol. , vol.16 , pp. 370-375
    • Gully, N.J.1    Rogers, A.H.2
  • 27
    • 0021992352 scopus 로고
    • Proline iminopeptidase from Bacillus coagulans: purification and enzymatic properties
    • Yoshimoto T., Tsuru D. Proline iminopeptidase from Bacillus coagulans: purification and enzymatic properties. J. Biochem. 1985, 97:1477-1485.
    • (1985) J. Biochem. , vol.97 , pp. 1477-1485
    • Yoshimoto, T.1    Tsuru, D.2
  • 28
    • 70450230325 scopus 로고    scopus 로고
    • Characterization of a multimeric, eukaryotic prolyl aminopeptidase: an inducible and highly specific intracellular peptidase from the non-pathogenic fungus Talaromyces emersonii
    • Mathon C.S., O'Donoghue A.J., Goetz D.H., Murray P.G., Craik C.S., Tuohy M.G. Characterization of a multimeric, eukaryotic prolyl aminopeptidase: an inducible and highly specific intracellular peptidase from the non-pathogenic fungus Talaromyces emersonii. Microbiology 2009, 155:3673-3682.
    • (2009) Microbiology , vol.155 , pp. 3673-3682
    • Mathon, C.S.1    O'Donoghue, A.J.2    Goetz, D.H.3    Murray, P.G.4    Craik, C.S.5    Tuohy, M.G.6
  • 30
    • 0034285515 scopus 로고    scopus 로고
    • Alpha/beta-hydrolase fold enzymes: structures, functions and mechanisms
    • Holmquist M. Alpha/beta-hydrolase fold enzymes: structures, functions and mechanisms. Curr. Protein Pept. Sci. 2000, 1:209-235.
    • (2000) Curr. Protein Pept. Sci. , vol.1 , pp. 209-235
    • Holmquist, M.1
  • 31
    • 0032472380 scopus 로고    scopus 로고
    • Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: a prototype for the prolyl oligopeptidase family
    • Medrano F.J., Alonso J., Garca J.L., Romero A., Bode W., Gomis-Ruth F.X. Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: a prototype for the prolyl oligopeptidase family. EMBO J. 1998, 17:1-9.
    • (1998) EMBO J. , vol.17 , pp. 1-9
    • Medrano, F.J.1    Alonso, J.2    Garca, J.L.3    Romero, A.4    Bode, W.5    Gomis-Ruth, F.X.6
  • 33
    • 0028019592 scopus 로고
    • Prolyl aminopeptidase is not a sulfhydryl enzyme: identification of the active serine residue by site-directed mutagenesis
    • Kitazono A., Ito K., Yoshimoto T. Prolyl aminopeptidase is not a sulfhydryl enzyme: identification of the active serine residue by site-directed mutagenesis. J. Biochem. 1994, 116:943-945.
    • (1994) J. Biochem. , vol.116 , pp. 943-945
    • Kitazono, A.1    Ito, K.2    Yoshimoto, T.3
  • 34
    • 0032897197 scopus 로고    scopus 로고
    • The prolyl aminopeptidase from Lactobacillus delbrueckii subsp. bulgaricus belongs to the α/β hydrolase fold family
    • Morel F., Gilbert C., Geourjon C., Frot-Coutaz J., Portalier R., Atlan D. The prolyl aminopeptidase from Lactobacillus delbrueckii subsp. bulgaricus belongs to the α/β hydrolase fold family. Biochem. Biophys. Acta 1999, 1429:501-505.
    • (1999) Biochem. Biophys. Acta , vol.1429 , pp. 501-505
    • Morel, F.1    Gilbert, C.2    Geourjon, C.3    Frot-Coutaz, J.4    Portalier, R.5    Atlan, D.6
  • 35
    • 85013711829 scopus 로고
    • Purification and characterization of proline iminopeptidase from Lactobacillus casei sp. casei LLG
    • Habibi-najaf M.B., Lee B.H. Purification and characterization of proline iminopeptidase from Lactobacillus casei sp. casei LLG. J. Dairy Sci. 1995, 78:251-259.
    • (1995) J. Dairy Sci. , vol.78 , pp. 251-259
    • Habibi-najaf, M.B.1    Lee, B.H.2
  • 36
    • 1842738109 scopus 로고    scopus 로고
    • Purification and properties of iminopeptidase from peanut seeds
    • Oviedo M.E.O., Isola M.C., Maldonado A.M., Franzon L. Purification and properties of iminopeptidase from peanut seeds. Plant Sci. 2004, 166:1143-1148.
    • (2004) Plant Sci. , vol.166 , pp. 1143-1148
    • Oviedo, M.E.O.1    Isola, M.C.2    Maldonado, A.M.3    Franzon, L.4
  • 37
    • 0026690122 scopus 로고
    • Cloning, sequencing, and high expression of the proline iminopeptidase gene from Bacillus coagulans
    • Kitazono A., Yoshimoto T., Tsuru D. Cloning, sequencing, and high expression of the proline iminopeptidase gene from Bacillus coagulans. J. Bacteriol. 1992, 174:7919-7925.
    • (1992) J. Bacteriol. , vol.174 , pp. 7919-7925
    • Kitazono, A.1    Yoshimoto, T.2    Tsuru, D.3
  • 38
    • 0032774442 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular proline iminopeptidase from Arthrobacter nicotianae 9458
    • Smacchi E., Gobbetti M., Lanciotti R., Fox P.F. Purification and characterization of an extracellular proline iminopeptidase from Arthrobacter nicotianae 9458. FEMS Microbiol. Lett. 1999, 178:191-197.
    • (1999) FEMS Microbiol. Lett. , vol.178 , pp. 191-197
    • Smacchi, E.1    Gobbetti, M.2    Lanciotti, R.3    Fox, P.F.4
  • 40
    • 33747107401 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of a methionyl aminopeptidase from a hyperthermophilic archaeon Thermococcus sp NA1
    • Lee H.S., Kim Y.J., Bae S.S., Jeon J.H., Lim J.K., Jeong B.C., Kang S.G., Lee J.H. Cloning, expression, and characterization of a methionyl aminopeptidase from a hyperthermophilic archaeon Thermococcus sp NA1. Mar. Biotechnol. 2006, 8:425-432.
    • (2006) Mar. Biotechnol. , vol.8 , pp. 425-432
    • Lee, H.S.1    Kim, Y.J.2    Bae, S.S.3    Jeon, J.H.4    Lim, J.K.5    Jeong, B.C.6    Kang, S.G.7    Lee, J.H.8
  • 41
    • 0038162378 scopus 로고    scopus 로고
    • Overexpression, purification, and characterization of the recombinant leucine aminopeptidase II of Bacillus stearothermophilus
    • Kuo L.Y., Hwang G.Y., Lai Y.J., Yang S.L., Lin L.L. Overexpression, purification, and characterization of the recombinant leucine aminopeptidase II of Bacillus stearothermophilus. Curr. Microbiol. 2007, 47:40-45.
    • (2007) Curr. Microbiol. , vol.47 , pp. 40-45
    • Kuo, L.Y.1    Hwang, G.Y.2    Lai, Y.J.3    Yang, S.L.4    Lin, L.L.5
  • 43
    • 0035104615 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular proline iminopeptidase from Corynebacterium variabilis NCDO 2101
    • Gobbetti M., Smacchi E., Semeraro M., Fox P.F., Lanciotti R., Cogan T. Purification and characterization of an extracellular proline iminopeptidase from Corynebacterium variabilis NCDO 2101. J. Appl. Microbiol. 2001, 90:449-456.
    • (2001) J. Appl. Microbiol. , vol.90 , pp. 449-456
    • Gobbetti, M.1    Smacchi, E.2    Semeraro, M.3    Fox, P.F.4    Lanciotti, R.5    Cogan, T.6
  • 44
    • 0001184770 scopus 로고
    • Purification and characterization of an iminopeptidase from the primary leaf of wheat (Triticum aestivum L.)
    • Waters S.P., Dalling M.J. Purification and characterization of an iminopeptidase from the primary leaf of wheat (Triticum aestivum L.). Plant Physiol. 1983, 73:1048-1054.
    • (1983) Plant Physiol. , vol.73 , pp. 1048-1054
    • Waters, S.P.1    Dalling, M.J.2
  • 45
    • 33846399265 scopus 로고    scopus 로고
    • The molecular and biochemical characteristics of proline iminopeptidase from rye seed lings (Secale cereale L.)
    • Szawłowska U., Prus W., Bielawski W. The molecular and biochemical characteristics of proline iminopeptidase from rye seed lings (Secale cereale L.). Acta Physiol. Plant. 2006, 8:517-524.
    • (2006) Acta Physiol. Plant. , vol.8 , pp. 517-524
    • Szawłowska, U.1    Prus, W.2    Bielawski, W.3
  • 46
    • 0020170306 scopus 로고
    • Purification and properties of a proline iminopeptidase from apricot seeds
    • Nnomiya K., Kawatani K., Tanaka S., Kawata S., Makjsumi S. Purification and properties of a proline iminopeptidase from apricot seeds. J. Biochem. 1982, 92:413-421.
    • (1982) J. Biochem. , vol.92 , pp. 413-421
    • Nnomiya, K.1    Kawatani, K.2    Tanaka, S.3    Kawata, S.4    Makjsumi, S.5
  • 47
    • 32444445819 scopus 로고    scopus 로고
    • Unusual extra space at the active site and high activity for acetylated hydroxyproline of prolyl aminopeptidase from Serratia marcescens
    • Nakajima Y., Ito K., Sakata M., Xu Y., Nakashima K., Matsubara F., Hatakeyama S., Yoshimoto T. Unusual extra space at the active site and high activity for acetylated hydroxyproline of prolyl aminopeptidase from Serratia marcescens. J. Bacteriol. 2006, 188:1599-1606.
    • (2006) J. Bacteriol. , vol.188 , pp. 1599-1606
    • Nakajima, Y.1    Ito, K.2    Sakata, M.3    Xu, Y.4    Nakashima, K.5    Matsubara, F.6    Hatakeyama, S.7    Yoshimoto, T.8
  • 48
    • 0003456106 scopus 로고    scopus 로고
    • Isolation and characterization of proline iminopeptidase from Propionibacterium freudenreichii ATCC 9614
    • Stepaniak L. Isolation and characterization of proline iminopeptidase from Propionibacterium freudenreichii ATCC 9614. Nahrung 2000, 44:102-106.
    • (2000) Nahrung , vol.44 , pp. 102-106
    • Stepaniak, L.1
  • 49
    • 0030021821 scopus 로고    scopus 로고
    • Proline iminopeptidase from the outer cell envelope of the human oral spirochete Treponema denticola ATCC 35405
    • Mäkinen K.K., Chen C.Y., Mäkinen P.L. Proline iminopeptidase from the outer cell envelope of the human oral spirochete Treponema denticola ATCC 35405. Infect. Immun. 1996, 64:702-708.
    • (1996) Infect. Immun. , vol.64 , pp. 702-708
    • Mäkinen, K.K.1    Chen, C.Y.2    Mäkinen, P.L.3
  • 53
    • 49849100967 scopus 로고    scopus 로고
    • Proteomic and metabolomic analyses of the white-rot fungus Phanerochaete chrysosporium exposed to exogenous benzoic acid
    • Matsuzaki F., Shimizu M., Wariishi H. Proteomic and metabolomic analyses of the white-rot fungus Phanerochaete chrysosporium exposed to exogenous benzoic acid. J. Proteome Res. 2008, 7:2342-2350.
    • (2008) J. Proteome Res. , vol.7 , pp. 2342-2350
    • Matsuzaki, F.1    Shimizu, M.2    Wariishi, H.3
  • 54
    • 68349105832 scopus 로고    scopus 로고
    • Gene expression analysis of Phanerochaete chrysosporium during the transition time from primary growth to second metabolism
    • Jiang M.F., Li X., Zhang L., Feng H., Zhang Y.Z. Gene expression analysis of Phanerochaete chrysosporium during the transition time from primary growth to second metabolism. J. Microbiol. 2009, 47:308-318.
    • (2009) J. Microbiol. , vol.47 , pp. 308-318
    • Jiang, M.F.1    Li, X.2    Zhang, L.3    Feng, H.4    Zhang, Y.Z.5
  • 57
    • 0036189875 scopus 로고    scopus 로고
    • Debittering of enzymatic hydrolysates using an aminopeptidase from the edible basidiomycetes Grifola frondosa
    • Nishiwaki T., Yoshimizu S., Furuta M., Hayashi K. Debittering of enzymatic hydrolysates using an aminopeptidase from the edible basidiomycetes Grifola frondosa. J. Biosci. Bioeng. 2002, 93:60-63.
    • (2002) J. Biosci. Bioeng. , vol.93 , pp. 60-63
    • Nishiwaki, T.1    Yoshimizu, S.2    Furuta, M.3    Hayashi, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.