메뉴 건너뛰기




Volumn 289, Issue 5, 1999, Pages 1445-1457

Substrate recognition and selectivity of peptide deformylase. Similarities and differences with metzincins and thermolysin

Author keywords

Catalytic mechanism; Metzincins; S1' pocket; Thermolysin; Thiorphan

Indexed keywords

ALKYL GROUP; FORMYLPEPTIDE; ISOLEUCINE; LEUCINE; METHIONINE; NORLEUCINE; THERMOLYSIN;

EID: 0033603628     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2832     Document Type: Article
Times cited : (57)

References (38)
  • 2
    • 0032496227 scopus 로고    scopus 로고
    • Structure of peptide deformylase and identification of the substrate binding site
    • Becker A., Schlichting I., Kabsch W., Schultz S., Wagner A. F. V. Structure of peptide deformylase and identification of the substrate binding site. J. Biol. Chem. 273:1998b;11413-11416.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11413-11416
    • Becker, A.1    Schlichting, I.2    Kabsch, W.3    Schultz, S.4    Wagner, A.F.V.5
  • 3
  • 4
    • 0028242962 scopus 로고
    • MC-Fit: Using Monte-Carlo methods to get accurate confidence limits on enzyme parameters
    • Dardel F. MC-Fit: using Monte-Carlo methods to get accurate confidence limits on enzyme parameters. Comput. Appl. Biosci. 10:1994;273-275.
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 273-275
    • Dardel, F.1
  • 7
    • 0028915695 scopus 로고
    • X-ray structures of human collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design
    • Grams F., Reinemer P., Powers J. C., Kleine T., Pieper M., Tschesche H., Huber R., Bode W. X-ray structures of human collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design. Eur. J. Biochem. 228:1995;830-841.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 830-841
    • Grams, F.1    Reinemer, P.2    Powers, J.C.3    Kleine, T.4    Pieper, M.5    Tschesche, H.6    Huber, R.7    Bode, W.8
  • 9
    • 0024340114 scopus 로고
    • New method for generating deletions and gene replacements in Escherichia coli
    • Hamilton C. M., Aldea M., Washburn B. K., Babitzke P., Kushner S. R. New method for generating deletions and gene replacements in Escherichia coli. J. Bacteriol. 171:1989;4617-4622.
    • (1989) J. Bacteriol. , vol.171 , pp. 4617-4622
    • Hamilton, C.M.1    Aldea, M.2    Washburn, B.K.3    Babitzke, P.4    Kushner, S.R.5
  • 10
    • 0033547751 scopus 로고    scopus 로고
    • Determination of substrate specificity for peptide deformylase through the screening of a combinatorial peptide library
    • Huy Y. J., Wei Y., Zhou Y., Rajagopalan P. T. R., Pei D. Determination of substrate specificity for peptide deformylase through the screening of a combinatorial peptide library. Biochemistry. 38:1999;643-650.
    • (1999) Biochemistry , vol.38 , pp. 643-650
    • Huy, Y.J.1    Wei, Y.2    Zhou, Y.3    Rajagopalan, P.T.R.4    Pei, D.5
  • 11
    • 0029155961 scopus 로고
    • Development of highly potent and selective phosphinic peptide inhibitors of zinc endopeptidase 24-15 using combinatorial chemistry
    • Jiracek J., Yiotakis A., Vincent B., Lecoq A., Nicolaou A., Checler F., Dive V. Development of highly potent and selective phosphinic peptide inhibitors of zinc endopeptidase 24-15 using combinatorial chemistry. J. Biol. Chem. 270:1995;21701-21706.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21701-21706
    • Jiracek, J.1    Yiotakis, A.2    Vincent, B.3    Lecoq, A.4    Nicolaou, A.5    Checler, F.6    Dive, V.7
  • 12
    • 0029741201 scopus 로고    scopus 로고
    • Development of the first potent selective inhibitor of the zinc endopeptidase neurolysin using a systematic approach based on combinatorial chemistry of phosphinic peptides
    • Jiracek J., Yiotakis A., Vincent b., Checler F., Dive V. Development of the first potent selective inhibitor of the zinc endopeptidase neurolysin using a systematic approach based on combinatorial chemistry of phosphinic peptides. J. Biol. Chem. 271:1996;19606-19611.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19606-19611
    • Jiracek, J.1    Yiotakis, A.2    Vincent, B.3    Checler, F.4    Dive, V.5
  • 13
    • 0014904642 scopus 로고
    • Studies on the ability of norleucine to replace methionine in the initiation of protein synthesis in E. coli
    • Kerwar S. S., Weissbach H. Studies on the ability of norleucine to replace methionine in the initiation of protein synthesis in E. coli. Arch. Biochem. Biophys. 141:1970;525-532.
    • (1970) Arch. Biochem. Biophys. , vol.141 , pp. 525-532
    • Kerwar, S.S.1    Weissbach, H.2
  • 14
    • 0031025121 scopus 로고    scopus 로고
    • Formate dehydrogenase-coupled spectrophotometric assay of peptide deformylase
    • Lazennec C., Meinnel T. Formate dehydrogenase-coupled spectrophotometric assay of peptide deformylase. Anal. Biochem. 244:1997;180-182.
    • (1997) Anal. Biochem. , vol.244 , pp. 180-182
    • Lazennec, C.1    Meinnel, T.2
  • 15
    • 33845280830 scopus 로고
    • Structural basis of the action of thermolysin and related zinc peptidases
    • Matthews B. W. Structural basis of the action of thermolysin and related zinc peptidases. Acc. Chem. Res. 21:1988;333-340.
    • (1988) Acc. Chem. Res. , vol.21 , pp. 333-340
    • Matthews, B.W.1
  • 16
    • 0028053015 scopus 로고
    • Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation
    • Mazel D., Pochet S., Marlière P. Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation. EMBO J. 13:1994;914-923.
    • (1994) EMBO J. , vol.13 , pp. 914-923
    • Mazel, D.1    Pochet, S.2    Marlière, P.3
  • 17
    • 0344983194 scopus 로고    scopus 로고
    • Toward a rational design for new antibacterial agents
    • Meinnel T. Toward a rational design for new antibacterial agents. Pathol. Biol. 1999.
    • (1999) Pathol. Biol.
    • Meinnel, T.1
  • 18
    • 0027369819 scopus 로고
    • fformyltransferase are encoded within the same operon in Escherichia coli
    • fformyltransferase are encoded within the same operon in Escherichia coli. J. Bacteriol. 175:1993;7737-7740.
    • (1993) J. Bacteriol. , vol.175 , pp. 7737-7740
    • Meinnel, T.1    Blanquet, S.2
  • 20
    • 0028916186 scopus 로고
    • Enzymatic properties of Escherichia coli peptide deformylase
    • Meinnel T., Blanquet S. Enzymatic properties of Escherichia coli peptide deformylase. J. Bacteriol. 177:1995;1883-1887.
    • (1995) J. Bacteriol. , vol.177 , pp. 1883-1887
    • Meinnel, T.1    Blanquet, S.2
  • 21
    • 0027882514 scopus 로고
    • Methionine as translation start signal: A review of the enzymes of the pathway in Escherichia coli
    • Meinnel T., Mechulam Y., Blanquet S. Methionine as translation start signal: a review of the enzymes of the pathway in Escherichia coli. Biochimie (Paris). 75:1993;1061-1075.
    • (1993) Biochimie (Paris) , vol.75 , pp. 1061-1075
    • Meinnel, T.1    Mechulam, Y.2    Blanquet, S.3
  • 22
    • 0028790271 scopus 로고
    • Mapping of the active site zinc ligands of peptide deformylase
    • Meinnel T., Lazennec C., Blanquet S. Mapping of the active site zinc ligands of peptide deformylase. J. Mol. Biol. 254:1995;175-183.
    • (1995) J. Mol. Biol. , vol.254 , pp. 175-183
    • Meinnel, T.1    Lazennec, C.2    Blanquet, S.3
  • 23
    • 0030603915 scopus 로고    scopus 로고
    • A new subclass of the zinc metalloproteases family revealed by the solution structure of peptide deformylase
    • Meinnel T., Blanquet S., Dardel F. A new subclass of the zinc metalloproteases family revealed by the solution structure of peptide deformylase. J. Mol. Biol. 262:1996a;375-386.
    • (1996) J. Mol. Biol. , vol.262 , pp. 375-386
    • Meinnel, T.1    Blanquet, S.2    Dardel, F.3
  • 24
    • 0030004178 scopus 로고    scopus 로고
    • The C-terminal domain of peptide deformylase is disordered and dispensable for activity
    • Meinnel T., Lazennec C., Dardel F., Schmitter J.-M., Blanquet S. The C-terminal domain of peptide deformylase is disordered and dispensable for activity. FEBS Letters. 385:1996b;91-95.
    • (1996) FEBS Letters , vol.385 , pp. 91-95
    • Meinnel, T.1    Lazennec, C.2    Dardel, F.3    Schmitter, J.-M.4    Blanquet, S.5
  • 25
    • 0031552348 scopus 로고    scopus 로고
    • Structure-function relationships of the peptide deformylase family. Evidence for a common tertiary fold of the active site built around three conserved motifs and a metal ion
    • Meinnel T., Lazennec C., Villoing S., Blanquet S. Structure-function relationships of the peptide deformylase family. Evidence for a common tertiary fold of the active site built around three conserved motifs and a metal ion. J. Mol. Biol. 267:1997;749-761.
    • (1997) J. Mol. Biol. , vol.267 , pp. 749-761
    • Meinnel, T.1    Lazennec, C.2    Villoing, S.3    Blanquet, S.4
  • 26
    • 0033528708 scopus 로고    scopus 로고
    • Design and synthesis of substrate analogue inhibitors of peptide deformylase
    • Meinnel T., Patiny L., Ragusa S., Blanquet S. Design and synthesis of substrate analogue inhibitors of peptide deformylase. Biochemistry. 38:1999;4287-4295.
    • (1999) Biochemistry , vol.38 , pp. 4287-4295
    • Meinnel, T.1    Patiny, L.2    Ragusa, S.3    Blanquet, S.4
  • 27
    • 0018884041 scopus 로고
    • An E. coli gene product required for λ site-specific recombination
    • Miller H. I., Friedman D. I. An E. coli gene product required for λ site-specific recombination. Cell. 20:1980;711-719.
    • (1980) Cell , vol.20 , pp. 711-719
    • Miller, H.I.1    Friedman, D.I.2
  • 28
    • 0020476130 scopus 로고
    • Structure of a mercaptan-thermolysin complex illustrates mode of inhibition of proteases by substrate-analogue mercaptans
    • Monzingo A. F., Matthews B. W. Structure of a mercaptan-thermolysin complex illustrates mode of inhibition of proteases by substrate-analogue mercaptans. Biochemistry. 21:1982;3390-3394.
    • (1982) Biochemistry , vol.21 , pp. 3390-3394
    • Monzingo, A.F.1    Matthews, B.W.2
  • 29
    • 0014828815 scopus 로고
    • Thermolysin: Kinetic study with oligopeptides
    • Morihara K., Tsuzuki H. Thermolysin: kinetic study with oligopeptides. Eur. J. Biochem. 15:1970;374-380.
    • (1970) Eur. J. Biochem. , vol.15 , pp. 374-380
    • Morihara, K.1    Tsuzuki, H.2
  • 30
    • 0014410525 scopus 로고
    • Comparison of the specificities of various neutral proteinases from microorganisms
    • Morihara K., Tsuzuki H., Oka T. Comparison of the specificities of various neutral proteinases from microorganisms. Arch. Biochem. Biophys. 123:1968;572-588.
    • (1968) Arch. Biochem. Biophys. , vol.123 , pp. 572-588
    • Morihara, K.1    Tsuzuki, H.2    Oka, T.3
  • 31
    • 0032579501 scopus 로고    scopus 로고
    • Membrane type-1 metalloprotease and stromelysin-3 clease more efficiently synthetic substrates containing unusual amino acids in their P1′ position
    • Mucha A., Cuniasse P., Kannan R., Beau F., Yiotakis A., Basset P., Dive V. Membrane type-1 metalloprotease and stromelysin-3 clease more efficiently synthetic substrates containing unusual amino acids in their P1′ position. J. Biol. Chem. 273:1998;2763-2768.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2763-2768
    • Mucha, A.1    Cuniasse, P.2    Kannan, R.3    Beau, F.4    Yiotakis, A.5    Basset, P.6    Dive, V.7
  • 33
    • 0032540979 scopus 로고    scopus 로고
    • Control of peptide deformylase activity by metal cations
    • Ragusa S., Blanquet S., Meinnel T. Control of peptide deformylase activity by metal cations. J. Mol. Biol. 280:1998;515-523.
    • (1998) J. Mol. Biol. , vol.280 , pp. 515-523
    • Ragusa, S.1    Blanquet, S.2    Meinnel, T.3
  • 34
    • 0000296163 scopus 로고    scopus 로고
    • Peptide deformylase: A new type of mononuclear iron protein
    • Rajagopalan P. T. R., Yu X. C., Pei D. Peptide deformylase: a new type of mononuclear iron protein. J. Am. Chem. Soc. 119:1997;12418-12419.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 12418-12419
    • Rajagopalan, P.T.R.1    Yu, X.C.2    Pei, D.3
  • 35
    • 0029036451 scopus 로고
    • Evolutionary families of metallopeptidases
    • Rawlings N. D., Barrett A. J. Evolutionary families of metallopeptidases. Methods Enzymol. 248:1995;183-228.
    • (1995) Methods Enzymol. , vol.248 , pp. 183-228
    • Rawlings, N.D.1    Barrett, A.J.2
  • 36
    • 0024580983 scopus 로고
    • Thiorphan and tetro -thiorphan display equivalent interactions when bound to crystalline thermolysin
    • Roderick S. L., Fournie-Zaluski M. C., Roques B. P., Matthews B. W. Thiorphan and tetro -thiorphan display equivalent interactions when bound to crystalline thermolysin. Biochemistry. 28:1989;1493-1497.
    • (1989) Biochemistry , vol.28 , pp. 1493-1497
    • Roderick, S.L.1    Fournie-Zaluski, M.C.2    Roques, B.P.3    Matthews, B.W.4
  • 37
    • 0025303335 scopus 로고
    • Zinc coordination, function, and structure of zinc enzymes and other proteins
    • Vallee B. L., Auld D. S. Zinc coordination, function, and structure of zinc enzymes and other proteins. Biochemistry. 29:1990;5647-5659.
    • (1990) Biochemistry , vol.29 , pp. 5647-5659
    • Vallee, B.L.1    Auld, D.S.2
  • 38
    • 0029666453 scopus 로고    scopus 로고
    • Understanding the P1′ specificity of the matrix metalloproteinases: Effect of S1′ pocket mutations in matrylisin and stromelysin-1
    • Welch A. R., Holman C. M., Huber M., Brenner M. C., Browner M. F., Van Wart H. E. Understanding the P1′ specificity of the matrix metalloproteinases: effect of S1′ pocket mutations in matrylisin and stromelysin-1. Biochemistry. 35:1996;10103-10109.
    • (1996) Biochemistry , vol.35 , pp. 10103-10109
    • Welch, A.R.1    Holman, C.M.2    Huber, M.3    Brenner, M.C.4    Browner, M.F.5    Van Wart, H.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.