메뉴 건너뛰기




Volumn 74, Issue 6, 2007, Pages 1197-1204

Bacterial β-peptidyl aminopeptidases: On the hydrolytic degradation of β-peptides

Author keywords

Aminopeptidase; Beta amino acid; Beta peptide; Proteobacteria

Indexed keywords

AMINOPEPTIDASE; BETA-AMINO ACID; BETA-PEPTIDES; PROTEOBACTERIA;

EID: 34247586161     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-007-0872-5     Document Type: Short Survey
Times cited : (33)

References (55)
  • 1
    • 0033104816 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of a new L-aminopeptidase-D-amidase/D-esterase activated by a Gly-Ser peptide bond hydrolysis
    • Bompard-Gilles C, Villeret V, Fanuel L, Joris B, Frère JM, Van Beeumen J (1999) Crystallization and preliminary X-ray analysis of a new L-aminopeptidase-D-amidase/D-esterase activated by a Gly-Ser peptide bond hydrolysis. Acta Crystallogr D Biol Crystallogr 55(Pt 3):699-701
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , Issue.PART 3 , pp. 699-701
    • Bompard-Gilles, C.1    Villeret, V.2    Fanuel, L.3    Joris, B.4    Frère, J.M.5    Van Beeumen, J.6
  • 3
    • 0034651632 scopus 로고    scopus 로고
    • A new variant of the Ntn hydrolase fold revealed by the crystal structure of L-aminopeptidase D-ala-esterase/ amidase from Ochrobactrum anthropi
    • Bompard-Gilles C, Villeret V, Davies GJ, Fanuel L, Joris B, Frère JM, Van Beeumen J (2000b) A new variant of the Ntn hydrolase fold revealed by the crystal structure of L-aminopeptidase D-ala-esterase/ amidase from Ochrobactrum anthropi. Structure Fold Des 8:153-162
    • (2000) Structure Fold Des , vol.8 , pp. 153-162
    • Bompard-Gilles, C.1    Villeret, V.2    Davies, G.J.3    Fanuel, L.4    Joris, B.5    Frère, J.M.6    Van Beeumen, J.7
  • 4
    • 0029805739 scopus 로고    scopus 로고
    • Enzymatic pathway for the bacterial degradation of the cyanobacterial cyclic peptide toxin microcystin LR
    • Bourne DG, Jones GJ, Blakeley RL, Jones A, Negri AP, Riddles P (1996) Enzymatic pathway for the bacterial degradation of the cyanobacterial cyclic peptide toxin microcystin LR. Appl Environ Microbiol 62:4086-4094
    • (1996) Appl Environ Microbiol , vol.62 , pp. 4086-4094
    • Bourne, D.G.1    Jones, G.J.2    Blakeley, R.L.3    Jones, A.4    Negri, A.P.5    Riddles, P.6
  • 5
    • 0035203008 scopus 로고    scopus 로고
    • Characterisation of a gene cluster involved in bacterial degradation of the cyanobacterial toxinmicrocystin LR
    • Bourne DG, Riddles P, Jones GJ, Smith W, Blakeley RL (2001) Characterisation of a gene cluster involved in bacterial degradation of the cyanobacterial toxinmicrocystin LR. Environ Toxicol 16:523-534
    • (2001) Environ Toxicol , vol.16 , pp. 523-534
    • Bourne, D.G.1    Riddles, P.2    Jones, G.J.3    Smith, W.4    Blakeley, R.L.5
  • 8
    • 22244434225 scopus 로고    scopus 로고
    • DOM-fold: A structure with crossing loops found in DmpA, ornithine acetyltransferase, and molybdenum cofactor-binding domain
    • Cheng H, Grishin NV (2005) DOM-fold: a structure with crossing loops found in DmpA, ornithine acetyltransferase, and molybdenum cofactor-binding domain. Protein Sci 14:1902-1910
    • (2005) Protein Sci , vol.14 , pp. 1902-1910
    • Cheng, H.1    Grishin, N.V.2
  • 9
    • 0028773280 scopus 로고
    • Crystal structure of Aeromonas proteolytica aminopeptidase: A prototypical member of the co-catalytic zinc enzyme family
    • Chévrier B, Schalk C, D'Orchymont H, Rondeau JM, Moras D, Tarnus C (1994) Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family. Structure 2:283-291
    • (1994) Structure , vol.2 , pp. 283-291
    • Chévrier, B.1    Schalk, C.2    D'Orchymont, H.3    Rondeau, J.M.4    Moras, D.5    Tarnus, C.6
  • 11
    • 17644445604 scopus 로고    scopus 로고
    • Epidemiological investigation of Ochrobactrum anthropi strains isolated from a haematology unit
    • Delière E, Vu-Thien H, Lévy V, Barquins S, Schlegel L, Bouvet A (2000) Epidemiological investigation of Ochrobactrum anthropi strains isolated from a haematology unit. J Hosp Infect 44:173-178
    • (2000) J Hosp Infect , vol.44 , pp. 173-178
    • Delière, E.1    Vu-Thien, H.2    Lévy, V.3    Barquins, S.4    Schlegel, L.5    Bouvet, A.6
  • 12
    • 12844283915 scopus 로고    scopus 로고
    • X-ray crystal structure of ornithine acetyltransferase from the clavulanic acid biosynthesis gene cluster
    • Elkins JM, Kershaw NJ, Schofield CJ (2005) X-ray crystal structure of ornithine acetyltransferase from the clavulanic acid biosynthesis gene cluster. Biochem J 385:565-573
    • (2005) Biochem J , vol.385 , pp. 565-573
    • Elkins, J.M.1    Kershaw, N.J.2    Schofield, C.J.3
  • 14
  • 16
    • 0035382627 scopus 로고    scopus 로고
    • The outstanding biological stability of β- and γ-peptides toward proteolytic enzymes: An in vitro investigation with fifteen peptidases
    • Frackenpohl J, Arvidsson PI, Schreiber JV, Seebach D (2001) The outstanding biological stability of β- and γ-peptides toward proteolytic enzymes: an in vitro investigation with fifteen peptidases. Chembiochem 2:445-455
    • (2001) Chembiochem , vol.2 , pp. 445-455
    • Frackenpohl, J.1    Arvidsson, P.I.2    Schreiber, J.V.3    Seebach, D.4
  • 18
    • 24344438618 scopus 로고    scopus 로고
    • A novel β-peptidyl aminopeptidase (BapA) from strain 3-2W4 cleaves peptide bonds of synthetic β-tri-and β-dipeptides
    • Geueke B, Namoto K, Seebach D, Kohler HPE (2005) A novel β-peptidyl aminopeptidase (BapA) from strain 3-2W4 cleaves peptide bonds of synthetic β-tri-and β-dipeptides. J Bacteriol 187:5910-5917
    • (2005) J Bacteriol , vol.187 , pp. 5910-5917
    • Geueke, B.1    Namoto, K.2    Seebach, D.3    Kohler, H.P.E.4
  • 19
    • 33751117982 scopus 로고    scopus 로고
    • Bacterial β-peptidyl aminopeptidases with unique substrate specificities for β- and mixed β/α-oligopeptides
    • Geueke B, Heck T, Limbach M, Seebach D, Kohler HPE (2006) Bacterial β-peptidyl aminopeptidases with unique substrate specificities for β- and mixed β/α-oligopeptides. FEBS J 273:5261-5272
    • (2006) FEBS J , vol.273 , pp. 5261-5272
    • Geueke, B.1    Heck, T.2    Limbach, M.3    Seebach, D.4    Kohler, H.P.E.5
  • 20
    • 33846506148 scopus 로고    scopus 로고
    • Description of Sphingosinicella xenopeptidilytica sp. nov., a β-peptide degrading strain, and emended descriptions of the genus Sphingosinicella and the species Sphingosinicella microcystinivorans
    • Geueke B, Busse HJ, Fleischmann T, Kämpfer P, Kohler HPE (2007) Description of Sphingosinicella xenopeptidilytica sp. nov., a β-peptide degrading strain, and emended descriptions of the genus Sphingosinicella and the species Sphingosinicella microcystinivorans. Int J Syst Evol Microbiol 57:107-113
    • (2007) Int J Syst Evol Microbiol , vol.57 , pp. 107-113
    • Geueke, B.1    Busse, H.J.2    Fleischmann, T.3    Kämpfer, P.4    Kohler, H.P.E.5
  • 21
    • 0037472666 scopus 로고    scopus 로고
    • Proteolytic stability of b-peptide bonds probed using quenched fluorescent substrates incorporating a hemoglobin cleavage site
    • Gopi HN, Ravindra G, Pal PP, Pattanaik P, Balaram H, Balaram P (2003) Proteolytic stability of b-peptide bonds probed using quenched fluorescent substrates incorporating a hemoglobin cleavage site. FEBS Lett 535:175-178
    • (2003) FEBS Lett , vol.535 , pp. 175-178
    • Gopi, H.N.1    Ravindra, G.2    Pal, P.P.3    Pattanaik, P.4    Balaram, H.5    Balaram, P.6
  • 23
    • 0001161293 scopus 로고
    • Carnosinase: An enzyme of swine kidney
    • Hanson HT, Smith EL (1949) Carnosinase: an enzyme of swine kidney. J Biol Chem 179:789-801
    • (1949) J Biol Chem , vol.179 , pp. 789-801
    • Hanson, H.T.1    Smith, E.L.2
  • 25
    • 0000466569 scopus 로고    scopus 로고
    • The biological stability of β-petides: No interactions between α-and β-peptidic structures?
    • Hintermann T, Seebach D (1997) The biological stability of β-petides: no interactions between α-and β-peptidic structures? Chimia 50:244-247
    • (1997) Chimia , vol.50 , pp. 244-247
    • Hintermann, T.1    Seebach, D.2
  • 26
    • 4544288081 scopus 로고    scopus 로고
    • Probing the proteolytic stability of ?-peptides containing α-fluoro- and α-hydroxy-β-amino acids
    • Hook DF, Gessier F, Noti C, Kast P, Seebach D (2004) Probing the proteolytic stability of ?-peptides containing α-fluoro- and α-hydroxy-β-amino acids. Chembiochem 5:691-706
    • (2004) Chembiochem , vol.5 , pp. 691-706
    • Hook, D.F.1    Gessier, F.2    Noti, C.3    Kast, P.4    Seebach, D.5
  • 27
    • 0036045592 scopus 로고    scopus 로고
    • Crystal structure of the dinuclear zinc aminopeptidase PepV from Lactobacillus delbrueckii unravels its preference for dipeptides
    • Jozic D, Bourenkow G, Bartunik H, Scholze H, Dive V, Henrich B, Huber R, Bode W, Maskos K (2002) Crystal structure of the dinuclear zinc aminopeptidase PepV from Lactobacillus delbrueckii unravels its preference for dipeptides. Structure 10:1097-1106
    • (2002) Structure , vol.10 , pp. 1097-1106
    • Jozic, D.1    Bourenkow, G.2    Bartunik, H.3    Scholze, H.4    Dive, V.5    Henrich, B.6    Huber, R.7    Bode, W.8    Maskos, K.9
  • 28
    • 0345151817 scopus 로고    scopus 로고
    • Recent advances in the enantioselective synthesis of β-amino acids
    • Juaristi E, Lopez-Ruiz H (1999) Recent advances in the enantioselective synthesis of β-amino acids. Curr Med Chem 6:983-1004
    • (1999) Curr Med Chem , vol.6 , pp. 983-1004
    • Juaristi, E.1    Lopez-Ruiz, H.2
  • 29
    • 14744280119 scopus 로고    scopus 로고
    • 100 years of peptide synthesis': Ligation methods for peptide and protein synthesis with applications to β-peptide assemblies
    • Kimmerlin T, Seebach D (2005) '100 years of peptide synthesis': ligation methods for peptide and protein synthesis with applications to β-peptide assemblies. J Pept Res 65:229-260
    • (2005) J Pept Res , vol.65 , pp. 229-260
    • Kimmerlin, T.1    Seebach, D.2
  • 30
    • 21344443668 scopus 로고    scopus 로고
    • A DmpA-homologous protein from Pseudomonas sp. is a dipeptidase specific for b-alanyl dipeptides
    • Komeda H, Asano Y (2005) A DmpA-homologous protein from Pseudomonas sp. is a dipeptidase specific for b-alanyl dipeptides. FEBS J 272:3075-3084
    • (2005) FEBS J , vol.272 , pp. 3075-3084
    • Komeda, H.1    Asano, Y.2
  • 31
    • 2142757279 scopus 로고    scopus 로고
    • A novel R-stereoselective amidase from Pseudomonas sp. MCI3434 acting on piperazine-2-tert-butylcarboxamide
    • Komeda H, Harada H, Washika S, Sakamoto T, Ueda M, Asano Y (2004) A novel R-stereoselective amidase from Pseudomonas sp. MCI3434 acting on piperazine-2-tert-butylcarboxamide. Eur J Biochem 271:1580-1590
    • (2004) Eur J Biochem , vol.271 , pp. 1580-1590
    • Komeda, H.1    Harada, H.2    Washika, S.3    Sakamoto, T.4    Ueda, M.5    Asano, Y.6
  • 32
    • 33749057884 scopus 로고    scopus 로고
    • Design and synthesis of β-peptides with biological activity
    • Koyack MJ, Cheng RP (2006) Design and synthesis of β-peptides with biological activity. Methods Mol Biol 340:95-109
    • (2006) Methods Mol Biol , vol.340 , pp. 95-109
    • Koyack, M.J.1    Cheng, R.P.2
  • 33
    • 0347087483 scopus 로고    scopus 로고
    • Synthesis, CD spectra, and enzymatic stability of β2-oligoazapeptides prepared from (S)-2-hydrazino carboxylic acids carrying the side chains of Val, Ala, and Leu
    • Lelais G, Seebach D (2003) Synthesis, CD spectra, and enzymatic stability of β2-oligoazapeptides prepared from (S)-2-hydrazino carboxylic acids carrying the side chains of Val, Ala, and Leu. Helv Chim Acta 86:4152-4168
    • (2003) Helv Chim Acta , vol.86 , pp. 4152-4168
    • Lelais, G.1    Seebach, D.2
  • 34
    • 4043089374 scopus 로고    scopus 로고
    • β2-Amino acids-syntheses, occurrence in natural products, and components of β-peptides
    • Lelais G, Seebach D (2004) β2-Amino acids-syntheses, occurrence in natural products, and components of β-peptides. Biopolymers 76:206-243
    • (2004) Biopolymers , vol.76 , pp. 206-243
    • Lelais, G.1    Seebach, D.2
  • 35
    • 33646565623 scopus 로고    scopus 로고
    • Biocatalysis as a profound tool in the preparation of highly enantiopure β-amino acids
    • Liljeblad A, Kanerva LT (2006) Biocatalysis as a profound tool in the preparation of highly enantiopure β-amino acids. Tetrahedron 62:5831-5854
    • (2006) Tetrahedron , vol.62 , pp. 5831-5854
    • Liljeblad, A.1    Kanerva, L.T.2
  • 36
    • 14744276599 scopus 로고    scopus 로고
    • Comparative metabolism of α-and β-peptides in the insect Heliothis virescens and in plant cells of black Mexican sweet maize
    • Lind R, Greenhow D, Perry S, Kimmerlin T, Seebach D (2004) Comparative metabolism of α-and β-peptides in the insect Heliothis virescens and in plant cells of black Mexican sweet maize. Chem Biodiv 1:1391-1400
    • (2004) Chem Biodiv , vol.1 , pp. 1391-1400
    • Lind, R.1    Greenhow, D.2    Perry, S.3    Kimmerlin, T.4    Seebach, D.5
  • 37
    • 0037201534 scopus 로고    scopus 로고
    • Recent advances in the stereoselective synthesis of β-amino acids
    • Liu M, Sibi MP (2002) Recent advances in the stereoselective synthesis of β-amino acids. Tetrahedron 58:7991-8035
    • (2002) Tetrahedron , vol.58 , pp. 7991-8035
    • Liu, M.1    Sibi, M.P.2
  • 38
    • 0032472380 scopus 로고    scopus 로고
    • Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: A prototype for the prolyl oligopeptidase family
    • Medrano FJ, Alonso J, Garcia JL, Romero A, Bode W, Gomis-Ruth FX (1998) Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: a prototype for the prolyl oligopeptidase family. EMBO J 17:1-9
    • (1998) EMBO J , vol.17 , pp. 1-9
    • Medrano, F.J.1    Alonso, J.2    Garcia, J.L.3    Romero, A.4    Bode, W.5    Gomis-Ruth, F.X.6
  • 39
    • 3943112253 scopus 로고    scopus 로고
    • Separation of enantiomers of non-protein amino acids by high-performance liquid chromatography on a chiral ligand-exchange column
    • Miyazawa T, Minowa H, Imagawa K, Yamada T (2004) Separation of enantiomers of non-protein amino acids by high-performance liquid chromatography on a chiral ligand-exchange column. Chromatographia 60:45-50
    • (2004) Chromatographia , vol.60 , pp. 45-50
    • Miyazawa, T.1    Minowa, H.2    Imagawa, K.3    Yamada, T.4
  • 40
    • 4143054876 scopus 로고    scopus 로고
    • Microbial degradation of poly(amino acid)s
    • Obst M, Steinbüchel A (2004) Microbial degradation of poly(amino acid)s. Biomacromolecules 5:1166-1176
    • (2004) Biomacromolecules , vol.5 , pp. 1166-1176
    • Obst, M.1    Steinbüchel, A.2
  • 41
    • 0026558390 scopus 로고
    • Direct separation of enantiomers by high-liquid performance liquid chromatography on a new chiral ligand-exchange phase
    • Oi N, Kitahara H, Kira R (1992) Direct separation of enantiomers by high-liquid performance liquid chromatography on a new chiral ligand-exchange phase. J Chromatogr 592:291-296
    • (1992) J Chromatogr , vol.592 , pp. 291-296
    • Oi, N.1    Kitahara, H.2    Kira, R.3
  • 42
    • 0034495297 scopus 로고    scopus 로고
    • Structural comparison of Ntn-hydrolases
    • Oinonen C, Rouvinen J (2000) Structural comparison of Ntn-hydrolases. Protein Sci 9:2329-2337
    • (2000) Protein Sci , vol.9 , pp. 2329-2337
    • Oinonen, C.1    Rouvinen, J.2
  • 43
    • 0027006712 scopus 로고
    • Carnosine: Its properties, functions and potential therapeutic applications
    • Quinn PJ, Boldyrev AA, Formazuyk VE (1992) Carnosine: its properties, functions and potential therapeutic applications. Mol Aspects Med 13:379-444
    • (1992) Mol Aspects Med , vol.13 , pp. 379-444
    • Quinn, P.J.1    Boldyrev, A.A.2    Formazuyk, V.E.3
  • 45
    • 0027273988 scopus 로고
    • Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: A new type of proteolytic enzyme
    • Roderick SL, Matthews BW (1993) Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme. Biochemistry 32:3907-3912
    • (1993) Biochemistry , vol.32 , pp. 3907-3912
    • Roderick, S.L.1    Matthews, B.W.2
  • 47
    • 0029953285 scopus 로고    scopus 로고
    • β-Peptides: Synthesis by Arndt-Eistert homologation with concomitant peptide coupling. Structure determination by NMR and CD spectroscopy and by X-ray crystallography. Helical secondary structure of a β-hexapeptide in solution and its stability towards pepsin
    • Seebach D, Overhand M, Kühnle FNM, Martinoni B, Oberer L, Hommel U, Widmer H (1996) β-Peptides: synthesis by Arndt-Eistert homologation with concomitant peptide coupling. Structure determination by NMR and CD spectroscopy and by X-ray crystallography. Helical secondary structure of a β-hexapeptide in solution and its stability towards pepsin. Helv Chim Acta 76:913-941
    • (1996) Helv Chim Acta , vol.76 , pp. 913-941
    • Seebach, D.1    Overhand, M.2    Kühnle, F.N.M.3    Martinoni, B.4    Oberer, L.5    Hommel, U.6    Widmer, H.7
  • 49
    • 9444226868 scopus 로고    scopus 로고
    • The world of β- and γ-peptides comprised of homologated proteinogenic amino acids and other components
    • Seebach D, Beck AK, Bierbaum DJ (2004) The world of β- and γ-peptides comprised of homologated proteinogenic amino acids and other components. Chem Biodiv 1:1111-1239
    • (2004) Chem Biodiv , vol.1 , pp. 1111-1239
    • Seebach, D.1    Beck, A.K.2    Bierbaum, D.J.3
  • 51
    • 0033780306 scopus 로고    scopus 로고
    • Structural organization of microcystin biosynthesis in Microcystis aeruginosa PCC7806: An integrated peptide-polyketide synthetase system
    • Tillett D, Dittmann E, Erhard M, von Dohren H, Borner T, Neilan BA (2000) Structural organization of microcystin biosynthesis in Microcystis aeruginosa PCC7806: an integrated peptide-polyketide synthetase system. Chem Biol 7:753-764
    • (2000) Chem Biol , vol.7 , pp. 753-764
    • Tillett, D.1    Dittmann, E.2    Erhard, M.3    von Dohren, H.4    Borner, T.5    Neilan, B.A.6
  • 52
    • 0027943760 scopus 로고
    • Cloning and nucleotide sequence analysis of pepV, a carnosinase gene from Lactobacillus delbrueckii subsp. lactis DSM 7290, and partial characterization of the enzyme
    • Vongerichten KF, Klein JR, Matern H, Plapp R (1994) Cloning and nucleotide sequence analysis of pepV, a carnosinase gene from Lactobacillus delbrueckii subsp. lactis DSM 7290, and partial characterization of the enzyme. Microbiology 140:2591-2600
    • (1994) Microbiology , vol.140 , pp. 2591-2600
    • Vongerichten, K.F.1    Klein, J.R.2    Matern, H.3    Plapp, R.4
  • 55
    • 0019879441 scopus 로고
    • Purification of carnosine synthetase from avian muscle by affinity chromatography and determination of its subunit structure
    • Wood MR, Johnson P (1981) Purification of carnosine synthetase from avian muscle by affinity chromatography and determination of its subunit structure. Biochim Biophys Acta 662:138-144
    • (1981) Biochim Biophys Acta , vol.662 , pp. 138-144
    • Wood, M.R.1    Johnson, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.