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Volumn 9, Issue 8, 2014, Pages 1718-1725

Substrate specificity of the lanthipeptide peptidase ElxP and the oxidoreductase ElxO

Author keywords

[No Author keywords available]

Indexed keywords

DEHYDROALANINE; LANTHIPEPTIDE PEPTIDASE ELXP; OXIDOREDUCTASE; OXIDOREDUCTASE ELXO; PEPTIDASE; UNCLASSIFIED DRUG; PEPTIDE HYDROLASE;

EID: 84906219597     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb5002526     Document Type: Article
Times cited : (32)

References (47)
  • 2
    • 0023912839 scopus 로고
    • Prepeptide sequence of epidermin, a ribosomally synthesized antibiotic with four sulphide-rings
    • Schnell, N., Entian, K.-D., Schneider, U., Götz, F., Zahner, H., Kellner, R., and Jung, G. (1988) Prepeptide sequence of epidermin, a ribosomally synthesized antibiotic with four sulphide-rings Nature 333, 276-278
    • (1988) Nature , vol.333 , pp. 276-278
    • Schnell, N.1    Entian, K.-D.2    Schneider, U.3    Götz, F.4    Zahner, H.5    Kellner, R.6    Jung, G.7
  • 3
    • 0028017962 scopus 로고
    • Influence of amino acid substitutions in the nisin leader peptide on biosynthesis and secretion of nisin by Lactococcus lactis
    • van der Meer, J. R., Rollema, H. S., Siezen, R. J., Beerthuyzen, M. M., Kuipers, O. P., and de Vos, W. M. (1994) Influence of amino acid substitutions in the nisin leader peptide on biosynthesis and secretion of nisin by Lactococcus lactis J. Biol. Chem. 269, 3555-3562
    • (1994) J. Biol. Chem. , vol.269 , pp. 3555-3562
    • Van Der Meer, J.R.1    Rollema, H.S.2    Siezen, R.J.3    Beerthuyzen, M.M.4    Kuipers, O.P.5    De Vos, W.M.6
  • 4
    • 33644854595 scopus 로고    scopus 로고
    • Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis
    • Li, B., Yu, J. P., Brunzelle, J. S., Moll, G. N., van der Donk, W. A., and Nair, S. K. (2006) Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis Science 311, 1464-1467
    • (2006) Science , vol.311 , pp. 1464-1467
    • Li, B.1    Yu, J.P.2    Brunzelle, J.S.3    Moll, G.N.4    Van Der Donk, W.A.5    Nair, S.K.6
  • 6
    • 15544386920 scopus 로고    scopus 로고
    • Isolation and structural characterization of epilancin 15X, a novel lantibiotic from a clinical strain of Staphylococcus epidermidis
    • Ekkelenkamp, M. B., Hanssen, M., Danny Hsu, S. T., de Jong, A., Milatovic, D., Verhoef, J., and van Nuland, N. A. (2005) Isolation and structural characterization of epilancin 15X, a novel lantibiotic from a clinical strain of Staphylococcus epidermidis FEBS Lett. 579, 1917-1922
    • (2005) FEBS Lett. , vol.579 , pp. 1917-1922
    • Ekkelenkamp, M.B.1    Hanssen, M.2    Danny Hsu, S.T.3    De Jong, A.4    Milatovic, D.5    Verhoef, J.6    Van Nuland, N.A.7
  • 7
    • 79960963680 scopus 로고    scopus 로고
    • Biosynthesis of the antimicrobial peptide epilancin 15X and its unusual N-terminal lactate moiety
    • Velásquez, J. E., Zhang, X., and van der Donk, W. A. (2011) Biosynthesis of the antimicrobial peptide epilancin 15X and its unusual N-terminal lactate moiety Chem. Biol. 18, 857-867
    • (2011) Chem. Biol. , vol.18 , pp. 857-867
    • Velásquez, J.E.1    Zhang, X.2    Van Der Donk, W.A.3
  • 8
    • 84861649020 scopus 로고    scopus 로고
    • Discovery, biosynthesis, and engineering of lantipeptides
    • Knerr, P. J. and van der Donk, W. A. (2012) Discovery, biosynthesis, and engineering of lantipeptides Annu. Rev. Biochem. 81, 479-505
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 479-505
    • Knerr, P.J.1    Van Der Donk, W.A.2
  • 10
    • 0029013783 scopus 로고
    • A family of bacteriocin ABC transporters carry out proteolytic processing of their substrates concomitant with export
    • Håvarstein, L. S., Diep, D. B., and Nes, I. F. (1995) A family of bacteriocin ABC transporters carry out proteolytic processing of their substrates concomitant with export Mol. Microbiol. 16, 229-240
    • (1995) Mol. Microbiol. , vol.16 , pp. 229-240
    • Håvarstein, L.S.1    Diep, D.B.2    Nes, I.F.3
  • 11
    • 74049115080 scopus 로고    scopus 로고
    • Follow the leader: The use of leader peptides to guide natural product biosynthesis
    • Oman, T. J. and van der Donk, W. A. (2010) Follow the leader: The use of leader peptides to guide natural product biosynthesis Nat. Chem. Biol. 6, 9-18
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 9-18
    • Oman, T.J.1    Van Der Donk, W.A.2
  • 12
    • 2942578482 scopus 로고    scopus 로고
    • Peptide signal molecules and bacteriocins in Gram-negative bacteria: A genome-wide in silico screening for peptides containing a double-glycine leader sequence and their cognate transporters
    • Dirix, G., Monsieurs, P., Dombrecht, B., Daniels, R., Marchal, K., Vanderleyden, J., and Michiels, J. (2004) Peptide signal molecules and bacteriocins in Gram-negative bacteria: A genome-wide in silico screening for peptides containing a double-glycine leader sequence and their cognate transporters Peptides 25, 1425-1440
    • (2004) Peptides , vol.25 , pp. 1425-1440
    • Dirix, G.1    Monsieurs, P.2    Dombrecht, B.3    Daniels, R.4    Marchal, K.5    Vanderleyden, J.6    Michiels, J.7
  • 14
    • 33646179437 scopus 로고    scopus 로고
    • Expression and characterization of the peptidase domain of Streptococcus pneumoniae ComA, a bifunctional ATP-binding cassette transporter involved in quorum sensing pathway
    • Ishii, S., Yano, T., and Hayashi, H. (2006) Expression and characterization of the peptidase domain of Streptococcus pneumoniae ComA, a bifunctional ATP-binding cassette transporter involved in quorum sensing pathway J. Biol. Chem. 281, 4726-4731
    • (2006) J. Biol. Chem. , vol.281 , pp. 4726-4731
    • Ishii, S.1    Yano, T.2    Hayashi, H.3
  • 15
    • 47249093322 scopus 로고    scopus 로고
    • In vitro reconstitution and substrate specificity of a lantibiotic protease
    • Furgerson Ihnken, L. A., Chatterjee, C., and van der Donk, W. A. (2008) In vitro reconstitution and substrate specificity of a lantibiotic protease Biochemistry 47, 7352-7363
    • (2008) Biochemistry , vol.47 , pp. 7352-7363
    • Furgerson Ihnken, L.A.1    Chatterjee, C.2    Van Der Donk, W.A.3
  • 16
    • 79953197608 scopus 로고    scopus 로고
    • Lantibiotic transporter requires cooperative functioning of the peptidase domain and the ATP binding domain
    • Nishie, M., Sasaki, M., Nagao, J., Zendo, T., Nakayama, J., and Sonomoto, K. (2011) Lantibiotic transporter requires cooperative functioning of the peptidase domain and the ATP binding domain J. Biol. Chem. 286, 11163-11169
    • (2011) J. Biol. Chem. , vol.286 , pp. 11163-11169
    • Nishie, M.1    Sasaki, M.2    Nagao, J.3    Zendo, T.4    Nakayama, J.5    Sonomoto, K.6
  • 17
    • 84878244288 scopus 로고    scopus 로고
    • Involvement and unusual substrate specificity of a prolyl oligopeptidase in class III lanthipeptide maturation
    • Völler, G. H., Krawczyk, B., Ensle, P., and Süssmuth, R. D. (2013) Involvement and unusual substrate specificity of a prolyl oligopeptidase in class III lanthipeptide maturation J. Am. Chem. Soc. 135, 7426-7429
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 7426-7429
    • Völler, G.H.1    Krawczyk, B.2    Ensle, P.3    Süssmuth, R.D.4
  • 18
    • 0028946940 scopus 로고
    • Homology modeling of the Lactococcus lactis leader peptidase NisP and its interaction with the precursor of the lantibiotic nisin
    • Siezen, R. J., Rollema, H. S., Kuipers, O. P., and de Vos, W. M. (1995) Homology modeling of the Lactococcus lactis leader peptidase NisP and its interaction with the precursor of the lantibiotic nisin Protein Eng. 8, 117-125
    • (1995) Protein Eng. , vol.8 , pp. 117-125
    • Siezen, R.J.1    Rollema, H.S.2    Kuipers, O.P.3    De Vos, W.M.4
  • 19
    • 2542432896 scopus 로고    scopus 로고
    • NisT, the transporter of the lantibiotic nisin, can transport fully modified, dehydrated, and unmodified prenisin and fusions of the leader peptide with non-lantibiotic peptides
    • Kuipers, A., de Boef, E., Rink, R., Fekken, S., Kluskens, L. D., Driessen, A. J., Leenhouts, K., Kuipers, O. P., and Moll, G. N. (2004) NisT, the transporter of the lantibiotic nisin, can transport fully modified, dehydrated, and unmodified prenisin and fusions of the leader peptide with non-lantibiotic peptides J. Biol. Chem. 279, 22176-22182
    • (2004) J. Biol. Chem. , vol.279 , pp. 22176-22182
    • Kuipers, A.1    De Boef, E.2    Rink, R.3    Fekken, S.4    Kluskens, L.D.5    Driessen, A.J.6    Leenhouts, K.7    Kuipers, O.P.8    Moll, G.N.9
  • 20
    • 0027309021 scopus 로고
    • Characterization of the Lactococcus lactis nisin A operon genes nisP, encoding a subtilisin-like serine protease involved in precursor processing, and nisR, encoding a regulatory protein involved in nisin biosynthesis
    • van der Meer, J. R., Polman, J., Beerthuyzen, M. M., Siezen, R. J., Kuipers, O. P., and de Vos, W. M. (1993) Characterization of the Lactococcus lactis nisin A operon genes nisP, encoding a subtilisin-like serine protease involved in precursor processing, and nisR, encoding a regulatory protein involved in nisin biosynthesis J. Bacteriol. 175, 2578-2588
    • (1993) J. Bacteriol. , vol.175 , pp. 2578-2588
    • Van Der Meer, J.R.1    Polman, J.2    Beerthuyzen, M.M.3    Siezen, R.J.4    Kuipers, O.P.5    De Vos, W.M.6
  • 21
    • 79551491572 scopus 로고    scopus 로고
    • Requirements of the engineered leader peptide of nisin for inducing modification, export, and cleavage
    • Plat, A., Kluskens, L. D., Kuipers, A., Rink, R., and Moll, G. N. (2011) Requirements of the engineered leader peptide of nisin for inducing modification, export, and cleavage Appl. Environ. Microbiol. 77, 604-611
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 604-611
    • Plat, A.1    Kluskens, L.D.2    Kuipers, A.3    Rink, R.4    Moll, G.N.5
  • 22
    • 0027205659 scopus 로고
    • Biosynthesis and secretion of a precursor of nisin Z by Lactococcus lactis, directed by the leader peptide of the homologous lantibiotic subtilin from Bacillus subtilis
    • Kuipers, O. P., Rollema, H. S., de Vos, W. M., and Siezen, R. J. (1993) Biosynthesis and secretion of a precursor of nisin Z by Lactococcus lactis, directed by the leader peptide of the homologous lantibiotic subtilin from Bacillus subtilis FEBS Lett. 330, 23-27
    • (1993) FEBS Lett. , vol.330 , pp. 23-27
    • Kuipers, O.P.1    Rollema, H.S.2    De Vos, W.M.3    Siezen, R.J.4
  • 23
    • 80052238993 scopus 로고    scopus 로고
    • Substrate recognition and specificity of the NisB protein, the lantibiotic dehydratase involved in nisin biosynthesis
    • Mavaro, A., Abts, A., Bakkes, P. J., Moll, G. N., Driessen, A. J., Smits, S. H., and Schmitt, L. (2011) Substrate recognition and specificity of the NisB protein, the lantibiotic dehydratase involved in nisin biosynthesis J. Biol. Chem. 286, 30552-30560
    • (2011) J. Biol. Chem. , vol.286 , pp. 30552-30560
    • Mavaro, A.1    Abts, A.2    Bakkes, P.J.3    Moll, G.N.4    Driessen, A.J.5    Smits, S.H.6    Schmitt, L.7
  • 25
    • 84878791111 scopus 로고    scopus 로고
    • Identification of distinct nisin leader peptide regions that determine interactions with the modification enzymes NisB and NisC
    • Khusainov, R., Moll, G. N., and Kuipers, O. P. (2013) Identification of distinct nisin leader peptide regions that determine interactions with the modification enzymes NisB and NisC FEBS Open Bio 3, 237-242
    • (2013) FEBS Open Bio , vol.3 , pp. 237-242
    • Khusainov, R.1    Moll, G.N.2    Kuipers, O.P.3
  • 26
    • 80054845759 scopus 로고    scopus 로고
    • Determining sites of interaction between prenisin and its modification enzymes NisB and NisC
    • Khusainov, R., Heils, R., Lubelski, J., Moll, G. N., and Kuipers, O. P. (2011) Determining sites of interaction between prenisin and its modification enzymes NisB and NisC Mol. Microbiol. 82, 706-718
    • (2011) Mol. Microbiol. , vol.82 , pp. 706-718
    • Khusainov, R.1    Heils, R.2    Lubelski, J.3    Moll, G.N.4    Kuipers, O.P.5
  • 27
    • 84878560267 scopus 로고    scopus 로고
    • Ribosomally synthesized and post-translationally modified peptide natural products: New insights into the role of leader and core peptides during biosynthesis
    • Yang, X. and van der Donk, W. A. (2013) Ribosomally synthesized and post-translationally modified peptide natural products: new insights into the role of leader and core peptides during biosynthesis Chem.-Eur. J. 19, 7662-7677
    • (2013) Chem.-Eur. J. , vol.19 , pp. 7662-7677
    • Yang, X.1    Van Der Donk, W.A.2
  • 28
    • 84924229934 scopus 로고    scopus 로고
    • Recognition sequences and substrate evolution in cyanobactin biosynthesis
    • 10.1021/sb500019b
    • Sardar, D., Pierce, E., McIntosh, J. A., and Schmidt, E. W. (2014) Recognition sequences and substrate evolution in cyanobactin biosynthesis ACS Synth. Biol. 10.1021/sb500019b
    • (2014) ACS Synth. Biol.
    • Sardar, D.1    Pierce, E.2    McIntosh, J.A.3    Schmidt, E.W.4
  • 29
    • 0024388398 scopus 로고
    • Pep5, a new lantibiotic: Structural gene isolation and prepeptide sequence
    • Kaletta, C., Entian, K. D., Kellner, R., Jung, G., Reis, M., and Sahl, H. G. (1989) Pep5, a new lantibiotic: Structural gene isolation and prepeptide sequence Arch. Microbiol. 152, 16-19
    • (1989) Arch. Microbiol. , vol.152 , pp. 16-19
    • Kaletta, C.1    Entian, K.D.2    Kellner, R.3    Jung, G.4    Reis, M.5    Sahl, H.G.6
  • 31
    • 0033621484 scopus 로고    scopus 로고
    • Extensive post-translational modification, including serine to d -alanine conversion, in the two-component lantibiotic, lacticin 3147
    • Ryan, M. P., Jack, R. W., Josten, M., Sahl, H. G., Jung, G., Ross, R. P., and Hill, C. (1999) Extensive post-translational modification, including serine to d -alanine conversion, in the two-component lantibiotic, lacticin 3147 J. Biol. Chem. 274, 37544-37550
    • (1999) J. Biol. Chem. , vol.274 , pp. 37544-37550
    • Ryan, M.P.1    Jack, R.W.2    Josten, M.3    Sahl, H.G.4    Jung, G.5    Ross, R.P.6    Hill, C.7
  • 32
    • 69449094338 scopus 로고    scopus 로고
    • Identification of a novel two-peptide lantibiotic, lichenicidin, following rational genome mining for LanM proteins
    • Begley, M., Cotter, P. D., Hill, C., and Ross, R. P. (2009) Identification of a novel two-peptide lantibiotic, lichenicidin, following rational genome mining for LanM proteins Appl. Environ. Microbiol. 75, 5451-5460
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 5451-5460
    • Begley, M.1    Cotter, P.D.2    Hill, C.3    Ross, R.P.4
  • 33
    • 69449097013 scopus 로고    scopus 로고
    • Production of the novel two-peptide lantibiotic lichenicidin by Bacillus licheniformis DSM 13
    • Dischinger, J., Josten, M., Szekat, C., Sahl, H. G., and Bierbaum, G. (2009) Production of the novel two-peptide lantibiotic lichenicidin by Bacillus licheniformis DSM 13 PLoS One 4, e6788
    • (2009) PLoS One , vol.4 , pp. 6788
    • Dischinger, J.1    Josten, M.2    Szekat, C.3    Sahl, H.G.4    Bierbaum, G.5
  • 35
    • 79251579302 scopus 로고    scopus 로고
    • Heterologous expression, biosynthesis, and mutagenesis of type II lantibiotics from Bacillus licheniformis in Escherichia coli
    • Caetano, T., Krawczyk, J. M., Mosker, E., Süssmuth, R. D., and Mendo, S. (2011) Heterologous expression, biosynthesis, and mutagenesis of type II lantibiotics from Bacillus licheniformis in Escherichia coli Chem. Biol. 18, 90-100
    • (2011) Chem. Biol. , vol.18 , pp. 90-100
    • Caetano, T.1    Krawczyk, J.M.2    Mosker, E.3    Süssmuth, R.D.4    Mendo, S.5
  • 37
    • 27644527461 scopus 로고    scopus 로고
    • Efficient synthesis of C-terminal modified peptide ketones for chemical ligations
    • Marceau, P., Bure, C., and Delmas, A. F. (2005) Efficient synthesis of C-terminal modified peptide ketones for chemical ligations Bioorg. Med. Chem. Lett. 15, 5442-5445
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 5442-5445
    • Marceau, P.1    Bure, C.2    Delmas, A.F.3
  • 38
    • 0025872592 scopus 로고
    • Purification and amino acid sequence of lactocin S, a bacteriocin produced by Lactobacillus sake L45
    • Mortvedt, C. I., Nissen-Meyer, J., Sletten, K., and Nes, I. F. (1991) Purification and amino acid sequence of lactocin S, a bacteriocin produced by Lactobacillus sake L45 Appl. Environ. Microbiol. 57, 1829-1834
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 1829-1834
    • Mortvedt, C.I.1    Nissen-Meyer, J.2    Sletten, K.3    Nes, I.F.4
  • 39
    • 74949129896 scopus 로고    scopus 로고
    • Synthesis of the lantibiotic lactocin S using peptide cyclizations on solid phase
    • Ross, A. C., Liu, H., Pattabiraman, V. R., and Vederas, J. C. (2010) Synthesis of the lantibiotic lactocin S using peptide cyclizations on solid phase J. Am. Chem. Soc. 132, 462-463
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 462-463
    • Ross, A.C.1    Liu, H.2    Pattabiraman, V.R.3    Vederas, J.C.4
  • 41
    • 0034405702 scopus 로고    scopus 로고
    • Crystal structure of the peptidyl-cysteine decarboxylase EpiD complexed with a pentapeptide substrate
    • Blaesse, M., Kupke, T., Huber, R., and Steinbacher, S. (2000) Crystal structure of the peptidyl-cysteine decarboxylase EpiD complexed with a pentapeptide substrate EMBO J. 19, 6299-6310
    • (2000) EMBO J. , vol.19 , pp. 6299-6310
    • Blaesse, M.1    Kupke, T.2    Huber, R.3    Steinbacher, S.4
  • 43
    • 58149133711 scopus 로고    scopus 로고
    • Medium- and short-chain dehydrogenase/reductase gene and protein families: The SDR superfamily: Functional and structural diversity within a family of metabolic and regulatory enzymes
    • Kavanagh, K. L., Jörnvall, H., Persson, B., and Oppermann, U. (2008) Medium- and short-chain dehydrogenase/reductase gene and protein families: The SDR superfamily: Functional and structural diversity within a family of metabolic and regulatory enzymes Cell. Mol. Life Sci. 65, 3895-3906
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 3895-3906
    • Kavanagh, K.L.1    Jörnvall, H.2    Persson, B.3    Oppermann, U.4
  • 45
    • 0035022533 scopus 로고    scopus 로고
    • SDR: Structure, mechanism of action, and substrate recognition
    • Tanaka, N., Nonaka, T., Nakamura, K. T., and Hara, A. (2001) SDR: Structure, mechanism of action, and substrate recognition Curr. Org. Chem. 5, 89-111
    • (2001) Curr. Org. Chem. , vol.5 , pp. 89-111
    • Tanaka, N.1    Nonaka, T.2    Nakamura, K.T.3    Hara, A.4
  • 46
    • 0029927410 scopus 로고    scopus 로고
    • Improved method for quantification of the bacteriocin nisin
    • Wolf, C. E. and Gibbons, W. R. (1996) Improved method for quantification of the bacteriocin nisin J. Appl. Bacteriol. 80, 453-457
    • (1996) J. Appl. Bacteriol. , vol.80 , pp. 453-457
    • Wolf, C.E.1    Gibbons, W.R.2
  • 47
    • 0028914567 scopus 로고
    • A comparison of methods for the measurement of bacteriocin activity
    • Parente, E., Brienza, C., Moles, M., and Ricciardi, A. (1995) A comparison of methods for the measurement of bacteriocin activity J. Microbiol. Methods 22, 95-108
    • (1995) J. Microbiol. Methods , vol.22 , pp. 95-108
    • Parente, E.1    Brienza, C.2    Moles, M.3    Ricciardi, A.4


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