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Volumn 43, Issue 30, 2004, Pages 9620-9628

Spectroscopic and X-ray crystallographic characterization of bestatin bound to the aminopeptidase from Aeromonas (Vibrio) proteolytica

Author keywords

[No Author keywords available]

Indexed keywords

ABS RESINS; CRYSTALLOGRAPHY; HYDROPHOBICITY; PROTEINS; SPECTROSCOPIC ANALYSIS;

EID: 3342926039     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049126p     Document Type: Article
Times cited : (32)

References (63)
  • 1
    • 0027479013 scopus 로고
    • Aminopeptidases: Structure and function
    • Taylor, A. (1993) Aminopeptidases: Structure and Function, FASEB J. 7, 290.
    • (1993) FASEB J. , vol.7 , pp. 290
    • Taylor, A.1
  • 2
    • 0002239755 scopus 로고    scopus 로고
    • Aminopeptidases
    • (Taylor, A., Ed.), R. G. Landes Co., Austin, TX
    • Taylor, A. (1996) Aminopeptidases, in Molecular Biology Intelligence Unit (Taylor, A., Ed.) pp 1, R. G. Landes Co., Austin, TX.
    • (1996) Molecular Biology Intelligence Unit , pp. 1
    • Taylor, A.1
  • 3
    • 0030200482 scopus 로고    scopus 로고
    • Bacterial aminopeptidases: Properties and functions
    • Gonzales, T., and Bobert-Baudouy, J. (1996) Bacterial Aminopeptidases: Properties and Functions, FEMS Microbiol. Rev. 18, 319.
    • (1996) FEMS Microbiol. Rev. , vol.18 , pp. 319
    • Gonzales, T.1    Bobert-Baudouy, J.2
  • 4
    • 0030842583 scopus 로고    scopus 로고
    • N-acetylaspartylglutamate, N-acetylaspartate, and N-acetylated α-linked acidic dipeptidase in human brain and their alterations in Huntington and Alzheimer's diseases
    • Passani, L. A., Vonsattel, J. P., Carter, R. E., and Coyle, J. T. (1997) N-Acetylaspartylglutamate, N-Acetylaspartate, and N-Acetylated α-Linked Acidic Dipeptidase in Human Brain and Their Alterations in Huntington and Alzheimer's Diseases, Mol. Chem. Neuropathol. 31, 97.
    • (1997) Mol. Chem. Neuropathol. , vol.31 , pp. 97
    • Passani, L.A.1    Vonsattel, J.P.2    Carter, R.E.3    Coyle, J.T.4
  • 6
    • 0031465286 scopus 로고    scopus 로고
    • Bestatin-mediated inhibition of leucine aminopeptidase may hinder hiv infection
    • Pulido-Cejudo, G., Conway, B., Proulx, P., Brown, R., and Izaguirre, C. A. (1997) Bestatin-Mediated Inhibition of Leucine Aminopeptidase May Hinder Hiv Infection, Antiviral Res. 36, 167.
    • (1997) Antiviral Res. , vol.36 , pp. 167
    • Pulido-Cejudo, G.1    Conway, B.2    Proulx, P.3    Brown, R.4    Izaguirre, C.A.5
  • 7
    • 0030048006 scopus 로고    scopus 로고
    • Inhibition of tumor cell invasion and matrix degradation by aminopeptidase inhibitors
    • Fujii, H., Nakajima, M., Aoyagi, T., and Tsuruo, T. (1996) Inhibition of Tumor Cell Invasion and Matrix Degradation by Aminopeptidase Inhibitors, Biol. Pharm. Bull. 19, 6.
    • (1996) Biol. Pharm. Bull. , vol.19 , pp. 6
    • Fujii, H.1    Nakajima, M.2    Aoyagi, T.3    Tsuruo, T.4
  • 8
    • 0037396256 scopus 로고    scopus 로고
    • Co-catalytic metallopeptidases as pharmaceutical targets
    • Holz, R. C., Bzymek, K., and Swierczek, S. I. (2003) Co-Catalytic Metallopeptidases as Pharmaceutical Targets, Cur. Opin. Chem. Biol. 7, 197.
    • (2003) Cur. Opin. Chem. Biol. , vol.7 , pp. 197
    • Holz, R.C.1    Bzymek, K.2    Swierczek, S.I.3
  • 9
    • 0013292073 scopus 로고    scopus 로고
    • Methionine aminopeptidases and angiogenesis
    • Bradshaw, R., and Yi, E. (2002) Methionine Aminopeptidases and Angiogenesis, Essays Biol. Med. 38, 65.
    • (2002) Essays Biol. Med. , vol.38 , pp. 65
    • Bradshaw, R.1    Yi, E.2
  • 10
    • 0035839131 scopus 로고    scopus 로고
    • Expansion of the zinc metallo-hydrolase family of the L-lactamase fold
    • Daiyasua, H., Osakaa, K., Ishinob, Y., and Toha, H. (2001) Expansion of the Zinc Metallo-Hydrolase Family of the L-Lactamase Fold, FEBS Lett. 503, 1.
    • (2001) FEBS Lett. , vol.503 , pp. 1
    • Daiyasua, H.1    Osakaa, K.2    Ishinob, Y.3    Toha, H.4
  • 11
    • 7744244599 scopus 로고    scopus 로고
    • Recent advances in zinc enzymology
    • Lipscomb, W. N., and Sträter, N. (1996) Recent Advances in Zinc Enzymology, Chem. Rev. 96, 2375.
    • (1996) Chem. Rev. , vol.96 , pp. 2375
    • Lipscomb, W.N.1    Sträter, N.2
  • 12
    • 0001431264 scopus 로고    scopus 로고
    • Binuclear metallohydrolases
    • Wilcox, D. E. (1996) Binuclear Metallohydrolases, Chem. Rev. 96, 2435.
    • (1996) Chem. Rev. , vol.96 , pp. 2435
    • Wilcox, D.E.1
  • 13
    • 0000063535 scopus 로고    scopus 로고
    • Manganese enzymes with binuclear active sites
    • Dismukes, G. C. (1996) Manganese Enzymes with Binuclear Active Sites, Chem. Rev. 96, 2909.
    • (1996) Chem. Rev. , vol.96 , pp. 2909
    • Dismukes, G.C.1
  • 14
    • 0036783898 scopus 로고    scopus 로고
    • The aminopeptidase from Aeromonas proteolytica: Structure and mechanism of co-catalytic metal centers involved in peptide hydrolysis
    • Holz, R. C. (2002) The Aminopeptidase from Aeromonas proteolytica: Structure and Mechanism of Co-Catalytic Metal Centers Involved in Peptide Hydrolysis, Coord. Chem. Rev. 232, 5.
    • (2002) Coord. Chem. Rev. , vol.232 , pp. 5
    • Holz, R.C.1
  • 16
    • 0036789272 scopus 로고    scopus 로고
    • Molecular evolution of the lysine biosynthetic pathways
    • Velasco, A. M., Leguina, J. I., and Lazcano, A. (2002) Molecular Evolution of the Lysine Biosynthetic Pathways, J. Mol. Evol. 55, 445.
    • (2002) J. Mol. Evol. , vol.55 , pp. 445
    • Velasco, A.M.1    Leguina, J.I.2    Lazcano, A.3
  • 17
    • 0034881189 scopus 로고    scopus 로고
    • Structure of the bacillus subtilis D-aminopeptidase Dppa reveals a novel selfcompartmentalizing protease
    • Remaut, H., Bompard-Gilles, C., Goffin, C., Frere, J.-M., and Van Beeumen, J. (2001) Structure of the Bacillus subtilis D-Aminopeptidase Dppa Reveals a Novel Selfcompartmentalizing Protease, Nat. Struct. Biol. 8, 674.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 674
    • Remaut, H.1    Bompard-Gilles, C.2    Goffin, C.3    Frere, J.-M.4    Van Beeumen, J.5
  • 18
    • 0028773280 scopus 로고
    • Crystal structure of aeromonas proteolytica aminopeptidase: A prototypical member of the co-catalytic zinc enzyme family
    • Chevrier, B., Schalk, C., D'Orchymont, H., Rondeau, J.-M., Moras, D., and Tarnus, C. (1994) Crystal Structure of Aeromonas proteolytica Aminopeptidase: A Prototypical Member of the Co-Catalytic Zinc Enzyme Family, Structure 2, 283.
    • (1994) Structure , vol.2 , pp. 283
    • Chevrier, B.1    Schalk, C.2    D'Orchymont, H.3    Rondeau, J.-M.4    Moras, D.5    Tarnus, C.6
  • 19
    • 3342970070 scopus 로고    scopus 로고
    • The 0.95 Å resolution and low pH crystal structures of the aminopeptidase from Aeromonas proteolytica
    • in press
    • Desmarais, W., Bienvenue, L. D., Bzymek, K., Holz, R. C., Petsko, A. G., and Ringe, D. (2002) The 0.95 Å Resolution and Low pH Crystal Structures of the Aminopeptidase from Aeromonas proteolytica, Biochemistry, in press.
    • (2002) Biochemistry
    • Desmarais, W.1    Bienvenue, L.D.2    Bzymek, K.3    Holz, R.C.4    Petsko, A.G.5    Ringe, D.6
  • 20
    • 0036691521 scopus 로고    scopus 로고
    • The 1.2 Å resolution crystal structure of the aminopeptidase from Aeromonas proteolytica complexed with tris: A Tale of buffer inhibition
    • Desmarais, W., Bienvenue, L. D., Bzymek, K., Holz, R. C., Petsko, A. G., and Ringe, D. (2002) The 1.2 Å Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica Complexed with Tris: A Tale of Buffer Inhibition, Structure 10, 1063.
    • (2002) Structure , vol.10 , pp. 1063
    • Desmarais, W.1    Bienvenue, L.D.2    Bzymek, K.3    Holz, R.C.4    Petsko, A.G.5    Ringe, D.6
  • 21
    • 0000946342 scopus 로고
    • Aeromonas aminopeptidase: pH dependence and a transition-state-analogue inhibitor
    • Baker, J. O., and Prescott, J. M. (1983) Aeromonas Aminopeptidase: pH Dependence and a Transition-State-Analogue Inhibitor, Biochemistry 22, 5322.
    • (1983) Biochemistry , vol.22 , pp. 5322
    • Baker, J.O.1    Prescott, J.M.2
  • 22
    • 0021113193 scopus 로고
    • Hydroxamates and aliphatic boronic acids: Marker inhibitors for aminopeptidase
    • Baker, J. O., Wilkes, S. H., Bayliss, M. E., and Prescott, J. M. (1983) Hydroxamates and Aliphatic Boronic Acids: Marker Inhibitors for Aminopeptidase, Biochemistry 22, 2098.
    • (1983) Biochemistry , vol.22 , pp. 2098
    • Baker, J.O.1    Wilkes, S.H.2    Bayliss, M.E.3    Prescott, J.M.4
  • 23
    • 0022214373 scopus 로고
    • A transition-state-analogue inhibitor infuences zinc-binding by Aeromonas aminopeptidase
    • Baker, J. O., and Prescott, J. M. (1985) A Transition-State-Analogue Inhibitor Infuences Zinc-Binding by Aeromonas Aminopeptidase, Biochem. Biophys. Res. Commun. 130, 1154.
    • (1985) Biochem. Biophys. Res. Commun. , vol.130 , pp. 1154
    • Baker, J.O.1    Prescott, J.M.2
  • 25
    • 0024566919 scopus 로고
    • Inhibition of aminopeptidases by aminophosphonates
    • Lejczak, B., Kafarski, P., and Zygmunt, J. (1989) Inhibition of Aminopeptidases by Aminophosphonates, Biochemistry 28, 3549.
    • (1989) Biochemistry , vol.28 , pp. 3549
    • Lejczak, B.1    Kafarski, P.2    Zygmunt, J.3
  • 26
    • 0032567158 scopus 로고    scopus 로고
    • Inhibition of the aminopeptidase from Aeromonas proteolytica by L-leucinephosphonic acid, a transition state analouge of peptide hydrolysis
    • Bennett, B., and Holz, R. C. (1998) Inhibition of the Aminopeptidase from Aeromonas proteolytica by L-Leucinephosphonic Acid, a Transition State Analouge of Peptide Hydrolysis, J. Am. Chem. Soc. 120, 12139.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 12139
    • Bennett, B.1    Holz, R.C.2
  • 27
    • 0029116127 scopus 로고
    • Transition state analogue L-leucinephosphonic acid bound to bovine lens leucine aminopeptidase: X-ray structure at 1.65 Å resolution in a new crystal form
    • Sträter, N., and Lipscomb, W. N. (1995) Transition State Analogue L-Leucinephosphonic Acid Bound to Bovine Lens Leucine Aminopeptidase: X-ray Structure at 1.65 Å Resolution in a New Crystal Form, Biochemisty 34, 9200.
    • (1995) Biochemisty , vol.34 , pp. 9200
    • Sträter, N.1    Lipscomb, W.N.2
  • 28
    • 0021051363 scopus 로고
    • Stereospecifity of amino acid hydroxamate inhibition of aminopeptidases
    • Wilkes, S. H., and Prescott, J. M. (1983) Stereospecifity of Amino Acid Hydroxamate Inhibition of Aminopeptidases, J. Biol. Chem. 258, 13517.
    • (1983) J. Biol. Chem. , vol.258 , pp. 13517
    • Wilkes, S.H.1    Prescott, J.M.2
  • 29
    • 0023664606 scopus 로고
    • Hydroxamate-induced spectral perturbations of cobalt Aeromonas aminopeptidase
    • Wilkes, S. H., and Prescott, J. M. (1987) Hydroxamate-Induced Spectral Perturbations of Cobalt Aeromonas Aminopeptidase, J. Biol. Chem. 262, 8621.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8621
    • Wilkes, S.H.1    Prescott, J.M.2
  • 30
    • 0020490879 scopus 로고
    • Inhibition of leucine Aminopeptidase by amino acid hydroxamates
    • Chan, W. W.-C., Dennis, P., Demmer, W., and Brand, K. (1982) Inhibition of Leucine Aminopeptidase by Amino Acid Hydroxamates, J. Biol. Chem. 257, 7955.
    • (1982) J. Biol. Chem. , vol.257 , pp. 7955
    • Chan, W.W.-C.1    Dennis, P.2    Demmer, W.3    Brand, K.4
  • 31
    • 0017236348 scopus 로고
    • Bestatin, an inhibitor of aminopeptidase B, produced by actinomycetes
    • Umezawa, H. T., Aoyagi, T., Suda, H., Hamada, M., and Takeuchi, T. (1976) Bestatin, An Inhibitor of Aminopeptidase B, Produced by Actinomycetes, J. Antibiot. 29, 97.
    • (1976) J. Antibiot. , vol.29 , pp. 97
    • Umezawa, H.T.1    Aoyagi, T.2    Suda, H.3    Hamada, M.4    Takeuchi, T.5
  • 32
    • 0027403231 scopus 로고
    • Inhibition of bovine lens leucine aminopeptidase by bestatin: Number of binding sites and slow binding of this inhibitor
    • Taylor, A., Peltier, C. Z., Torre, F. J., and Hakamian, N. (1993) Inhibition of Bovine Lens Leucine Aminopeptidase by Bestatin: Number of Binding Sites and Slow Binding of This Inhibitor, Biochemistry 32, 784.
    • (1993) Biochemistry , vol.32 , pp. 784
    • Taylor, A.1    Peltier, C.Z.2    Torre, F.J.3    Hakamian, N.4
  • 33
    • 0033598769 scopus 로고    scopus 로고
    • Slow-binding inhibition of the aminopeptidase from Aeromonas proteolytica by peptide thiols: Synthesis and spectral characterization
    • Huntington, K. M., Bienvenue, D., Wei, Y., Bennett, B., Holz, R. C., and Pei, D. (1999) Slow-Binding Inhibition of the Aminopeptidase from Aeromonas proteolytica by Peptide Thiols: Synthesis and Spectral Characterization, Biochemistry 38, 15587.
    • (1999) Biochemistry , vol.38 , pp. 15587
    • Huntington, K.M.1    Bienvenue, D.2    Wei, Y.3    Bennett, B.4    Holz, R.C.5    Pei, D.6
  • 34
    • 0022400582 scopus 로고
    • The slow, tight binding of bestatin and amastatin to aminopeptidases
    • Wilkes, S. H., and Prescott, J. M. (1985) The Slow, Tight Binding of Bestatin and Amastatin to Aminopeptidases, J. Biol. Chem. 260, 13154.
    • (1985) J. Biol. Chem. , vol.260 , pp. 13154
    • Wilkes, S.H.1    Prescott, J.M.2
  • 35
    • 0026602711 scopus 로고
    • Structure determination and refinement of bovine lens leucine aminopeptidase and its complex with bestatin
    • Burley, S. K., David, P. R., Sweet, R. M., Taylor, A., and Lipscomb, W. N. (1992) Structure Determination and Refinement of Bovine Lens Leucine Aminopeptidase and Its Complex with Bestatin, J. Mol. Biol. 224, 113.
    • (1992) J. Mol. Biol. , vol.224 , pp. 113
    • Burley, S.K.1    David, P.R.2    Sweet, R.M.3    Taylor, A.4    Lipscomb, W.N.5
  • 37
    • 0030950429 scopus 로고    scopus 로고
    • Mechanistic studies on the aminopeptidase from Aeromonas proteolytica: A two-metal ion mechanism for peptide hydrolysis
    • Chen, G., Edwards, T., D'souza, V. M., and Holz, R. C. (1997) Mechanistic Studies on the Aminopeptidase from Aeromonas proteolytica: A Two-Metal Ion Mechanism for Peptide Hydrolysis, Biochemistry 36, 4278.
    • (1997) Biochemistry , vol.36 , pp. 4278
    • Chen, G.1    Edwards, T.2    D'souza, V.M.3    Holz, R.C.4
  • 38
    • 0015239267 scopus 로고
    • Aeromonas aminopeptidase improved isolation and some physical properties
    • Prescott, J. M., Wilkes, S. H., Wagner, F. W., and Wilson, K. J. (1971) Aeromonas Aminopeptidase Improved Isolation and Some Physical Properties, J. Biol. Chem. 246, 1756.
    • (1971) J. Biol. Chem. , vol.246 , pp. 1756
    • Prescott, J.M.1    Wilkes, S.H.2    Wagner, F.W.3    Wilson, K.J.4
  • 39
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch, H. (1967) Spectroscopic Determination of Tryptophan and Tyrosine in Proteins, Biochemistry 6, 1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 40
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C., and von Hippel, P. H. (1989) Calculation of Protein Extinction Coefficients from Amino Acid Sequence Data, Anal. Biochem. 182, 319-366.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-366
    • Gill, S.C.1    Von Hippel, P.H.2
  • 41
    • 0025080295 scopus 로고
    • Thermodynamic analysis of the transcription cycle in E. coli
    • Gill, S. C., Yager, T. D., and von Hippel, P. H. (1990) Thermodynamic Analysis of the Transcription Cycle in E. coli, Biophys. Chem. 37, 239-250.
    • (1990) Biophys. Chem. , vol.37 , pp. 239-250
    • Gill, S.C.1    Yager, T.D.2    Von Hippel, P.H.3
  • 42
    • 0022392470 scopus 로고
    • Spectral and kinetic studies of metal-substituted aeromonas aminopeptidase: Nonidentical, interacting metal-binding sites
    • Prescott, J. M., Wagner, F. W., Holmquist, B., and Vallee, B. L. (1985) Spectral and Kinetic Studies of Metal-Substituted Aeromonas Aminopeptidase: Nonidentical, Interacting Metal-Binding Sites, Biochemistry 24, 5350.
    • (1985) Biochemistry , vol.24 , pp. 5350
    • Prescott, J.M.1    Wagner, F.W.2    Holmquist, B.3    Vallee, B.L.4
  • 43
    • 0030934626 scopus 로고    scopus 로고
    • Epr studies on the mono- and dicobalt(II)-substituted forms of the aminopeptidase from Aeromonas proteolytica. Insight into the catalytic mechanism of dinuclear hydrolases
    • Bennett, B., and Holz, R. C. (1997) Epr Studies on the Mono- and Dicobalt(II)-Substituted Forms of the Aminopeptidase from Aeromonas proteolytica. Insight into the Catalytic Mechanism of Dinuclear Hydrolases, J. Am. Chem. Soc. 119, 1923.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 1923
    • Bennett, B.1    Holz, R.C.2
  • 44
    • 0030878054 scopus 로고    scopus 로고
    • Spectroscopically distinct cobalt(II) sites in heterodimetallic forms of the aminopeptidase from Aeromonas proteolytica: Characterization of substrate binding
    • Bennett, B., and Holz, R. C. (1997) Spectroscopically Distinct Cobalt(II) Sites in Heterodimetallic Forms of the Aminopeptidase from Aeromonas proteolytica: Characterization of Substrate Binding, Biochemistry 36, 9837.
    • (1997) Biochemistry , vol.36 , pp. 9837
    • Bennett, B.1    Holz, R.C.2
  • 45
    • 0028587831 scopus 로고
    • Mo(V) electron paramagnetic resonance signals from the periplasmic nitrate reductase of thiosphaera pantotropha
    • Bennett, B., Berks, B. C., Ferguson, S. J., Thomson, A. J., and Richardson, D. J. (1994) Mo(V) Electron Paramagnetic Resonance Signals from the Periplasmic Nitrate Reductase of Thiosphaera pantotropha, Eur. J. Biochem. 226, 789.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 789
    • Bennett, B.1    Berks, B.C.2    Ferguson, S.J.3    Thomson, A.J.4    Richardson, D.J.5
  • 49
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brunger, A. T. (1992) Free R Value: A Novel Statistical Quantity for Assessing the Accuracy of Crystal Structures, Nature 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brunger, A.T.1
  • 50
    • 0024373643 scopus 로고
    • Carboxylate-histidine-zinc interactions in protein structure and function
    • Christianson, D. W., and Alexander, R. S. (1989) Carboxylate-Histidine- Zinc Interactions in Protein Structure and Function, J. Am. Chem. Soc. 111, 6412.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 6412
    • Christianson, D.W.1    Alexander, R.S.2
  • 51
    • 0032567158 scopus 로고    scopus 로고
    • Inhibition of the aminopeptidase from Aeromonas proteolytica by L-leucinephosphonic acid, a transition state analogue of peptide hydrolysis
    • Bennett, B., and Holz, R. C. (1998) Inhibition of the Aminopeptidase from Aeromonas proteolytica by L-Leucinephosphonic Acid, a Transition State Analogue of Peptide Hydrolysis, J. Am. Chem. Soc. 120, 12139.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 12139
    • Bennett, B.1    Holz, R.C.2
  • 52
    • 0035912827 scopus 로고    scopus 로고
    • Inhibition of the aminopeptidase from Aeromonas proteolytica by L-leucinephosphonic acid. Spectroscopic and crystallographic characterization of the transition state of peptide hydrolysis
    • in press
    • Stamper, C., Bennett, B., Edwards, T., Holz, R. C., Ringe, D., and Petsko, G. (2001) Inhibition of the Aminopeptidase from Aeromonas proteolytica by L-Leucinephosphonic Acid. Spectroscopic and Crystallographic Characterization of the Transition State of Peptide Hydrolysis, Biochemistry 40, in press.
    • (2001) Biochemistry 40
    • Stamper, C.1    Bennett, B.2    Edwards, T.3    Holz, R.C.4    Ringe, D.5    Petsko, G.6
  • 53
    • 0001555681 scopus 로고
    • Structures of di-m-acetato-(O,O′)-M-aqua-bis[acetato(n,n,n′, n′-tetramethylethylenediamine)cobalt(ii) and m-Aqua-di-m-chloroacetato(O, O′)-bis [chloroacetato(N,N,N′,N′-tetramethylethylenediamine) cobalt(II)
    • Turpeinen, U., Ahlgren, M., and Hämäläinen, R. (1982) Structures of Di-m-acetato-(O,O′)-m-aqua-bis[acetato(N,N,N′, N′-tetramethylethylenediamine)cobalt(II) and m-Aqua-di-m-chloroacetato(O, O′)-bis [chloroacetato(N,N,N′,N′-tetramethylethylenediamine) cobalt(II), Acta Crystallogr., Sect. B 32, 1580.
    • (1982) Acta Crystallogr., Sect. B , vol.32 , pp. 1580
    • Turpeinen, U.1    Ahlgren, M.2    Hämäläinen, R.3
  • 54
    • 0000575466 scopus 로고
    • The dinnuclear unit m-aqua-bis(m-carboxylato)dimetal. X-ray structure and magnetism of cobalt and nickel(II) compounds containing bridging carboxylato groups and a bridging water molecule
    • Turpeinen, U., Hämäläinen, R., and Reedijk, J. (1987) The Dinnuclear Unit m-Aqua-bis(m-carboxylato)dimetal. X-ray Structure and Magnetism of Cobalt and Nickel(II) Compounds Containing Bridging Carboxylato Groups and a Bridging Water Molecule, Polyhedron 6, 1603.
    • (1987) Polyhedron , vol.6 , pp. 1603
    • Turpeinen, U.1    Hämäläinen, R.2    Reedijk, J.3
  • 56
    • 33751155031 scopus 로고
    • Magnetic exchange through oxalate bridges: Synthesis and characterization of (m-oxalato)dimetal(II) complexes of manganese, iron, cobalt, nickel, copper, and zinc
    • Glerup, J., Goodson, P. A., Hodgson, D. J., and Michelsen, K. (1995) Magnetic Exchange through Oxalate Bridges: Synthesis and Characterization of (m-Oxalato)dimetal(II) Complexes of Manganese, Iron, Cobalt, Nickel, Copper, and Zinc, Inorg. Chem. 34, 6255.
    • (1995) Inorg. Chem. , vol.34 , pp. 6255
    • Glerup, J.1    Goodson, P.A.2    Hodgson, D.J.3    Michelsen, K.4
  • 58
    • 37049068865 scopus 로고
    • Magnetic and spectroscopic study of some binuclear ans trinuclear cobalt(II) carboxylate complexes
    • Little, I. R., Straughan, B. P., and Thornton, P. (1986) Magnetic and Spectroscopic Study of Some Binuclear Ans Trinuclear Cobalt(II) Carboxylate Complexes, J. Chem. Soc., Dalton. Trans., 2211.
    • (1986) J. Chem. Soc., Dalton. Trans. , pp. 2211
    • Little, I.R.1    Straughan, B.P.2    Thornton, P.3
  • 59
    • 0029960042 scopus 로고    scopus 로고
    • The structure of the Aeromonas proteolytica aminopeptidase complexed with a hydroxamate inhibitor. Involvement in catalysis of glu 151 and two zinc ions of the cocatalytic unit
    • Chevrier, B., D'Orchymont, H., Schalk, C., Tamus, C., and Moras, D. (1996) The Structure of the Aeromonas proteolytica Aminopeptidase Complexed with a Hydroxamate Inhibitor. Involvement in Catalysis of Glu 151 and Two Zinc Ions of the Cocatalytic Unit, Eur. J. Biochem. 237, 393.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 393
    • Chevrier, B.1    D'Orchymont, H.2    Schalk, C.3    Tamus, C.4    Moras, D.5
  • 60
    • 0033621079 scopus 로고    scopus 로고
    • Inhibition of the aminopeptidase from Aeromonas proteolytica by aliphatic alcholols. Characterization of the hydrophobic substrate recognition site
    • Ustynyuk, L., Bennett, B., Edwards, T., and Holz, R. C. (1999) Inhibition of the Aminopeptidase from Aeromonas proteolytica by Aliphatic Alcholols. Characterization of the Hydrophobic Substrate Recognition Site, Biochemistry 38, 11433.
    • (1999) Biochemistry , vol.38 , pp. 11433
    • Ustynyuk, L.1    Bennett, B.2    Edwards, T.3    Holz, R.C.4
  • 61
    • 0034651135 scopus 로고    scopus 로고
    • Inhibition of the aminopeptidase from Aeromonas proteolytica by L-leucinethiol: Kinetic and spectroscopic characterization of a slow, tight-binding inhibitor-enzyme complex
    • Bienvenue, D., Bennett, B., and Holz, R. C. (2000) Inhibition of the Aminopeptidase from Aeromonas proteolytica by L-Leucinethiol: Kinetic and Spectroscopic Characterization of a Slow, Tight-Binding Inhibitor-Enzyme Complex, J. Inorg. Biochem. 78, 43.
    • (2000) J. Inorg. Biochem. , vol.78 , pp. 43
    • Bienvenue, D.1    Bennett, B.2    Holz, R.C.3
  • 62
    • 0037133523 scopus 로고    scopus 로고
    • Hydrolysis of thiopeptides by the aminopeptidase from Aeromonas proteolytica
    • Bienvenue, D., Gilner, D., and Holz, R. C. (2002) Hydrolysis of Thiopeptides by the Aminopeptidase from Aeromonas proteolytica, Biochemistry 41, 3712.
    • (2002) Biochemistry , vol.41 , pp. 3712
    • Bienvenue, D.1    Gilner, D.2    Holz, R.C.3
  • 63
    • 0036370771 scopus 로고    scopus 로고
    • The aminopeptidase from Aeromonas proteolytica can function as an esterase
    • Bienvenue, D. L., Mathew, R. S., Ringe, D., and Holz, R. C. (2002) The Aminopeptidase from Aeromonas proteolytica Can Function as an Esterase, J. Biol. Inorg. Chem. 7, 129.
    • (2002) J. Biol. Inorg. Chem. , vol.7 , pp. 129
    • Bienvenue, D.L.1    Mathew, R.S.2    Ringe, D.3    Holz, R.C.4


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