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Volumn 36, Issue 4, 1997, Pages 812-822

Spectroscopic properties of Escherichia coli UDP-N- acetylenolpyruvylglucosamine reductase

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BUFFER; DITHIONITE; EDETIC ACID; FLAVINE ADENINE NUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXIDOREDUCTASE; PYRIDINE NUCLEOTIDE; PYRUVIC ACID; UREA; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE;

EID: 0031054864     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi962260s     Document Type: Article
Times cited : (15)

References (20)
  • 1
    • 0024281299 scopus 로고
    • Evaluation of 5-Enolpyruvoylshikimate-3-phosphate Synthase Substrate and Inhibitor Binding by Stopped-Flow and Equilibrium Fluorescence Measurements
    • Anderson, K. S., Sikorski, J. A., & Johnson, K. A. (1988) Evaluation of 5-Enolpyruvoylshikimate-3-phosphate Synthase Substrate and Inhibitor Binding by Stopped-Flow and Equilibrium Fluorescence Measurements, Biochemistry 27, 1604-1610.
    • (1988) Biochemistry , vol.27 , pp. 1604-1610
    • Anderson, K.S.1    Sikorski, J.A.2    Johnson, K.A.3
  • 2
    • 0027512265 scopus 로고
    • Overexpression, Purification, and Mechanistic Study of UDP-N-Acetylenolpyruvylglucosamine Reductase
    • Benson, T. E., Marquardt, J. L., Marquardt, A. C., Etzkorn, F. A., & Walsh, C. T. (1993) Overexpression, Purification, and Mechanistic Study of UDP-N-Acetylenolpyruvylglucosamine Reductase, Biochemistry 32, 2024-2030.
    • (1993) Biochemistry , vol.32 , pp. 2024-2030
    • Benson, T.E.1    Marquardt, J.L.2    Marquardt, A.C.3    Etzkorn, F.A.4    Walsh, C.T.5
  • 3
    • 0028245192 scopus 로고
    • Crystallization and Preliminary X-ray Crystallographic Studies of UDP-N-Acetylenolpyruvylglucosamine Reductase
    • Benson, T. E., Walsh, C. T., & Hogle, J. M. (1994) Crystallization and Preliminary X-ray Crystallographic Studies of UDP-N-Acetylenolpyruvylglucosamine Reductase, Protein Sci. 3, 1125-1127.
    • (1994) Protein Sci. , vol.3 , pp. 1125-1127
    • Benson, T.E.1    Walsh, C.T.2    Hogle, J.M.3
  • 4
    • 0029056202 scopus 로고
    • An Enzyme-Substrate Complex Involved in Bacterial Cell Wall Biosynthesis
    • Benson, T. E., Filman, D. J., Walsh, C. T., & Hogle, J. M. (1995) An Enzyme-Substrate Complex Involved in Bacterial Cell Wall Biosynthesis, Nature Struct. Biol. 2, 644-653.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 644-653
    • Benson, T.E.1    Filman, D.J.2    Walsh, C.T.3    Hogle, J.M.4
  • 5
    • 0029643799 scopus 로고    scopus 로고
    • The Structure of the Substrate-Free Form of MurB, An Essential Enzyme for the Synthesis of Bacterial Cell Walls
    • Benson, T. E., Walsh, C. T., & Hogle, J. M. (1996) The Structure of the Substrate-Free Form of MurB, An Essential Enzyme for the Synthesis of Bacterial Cell Walls, Structure, 4, 47-54.
    • (1996) Structure , vol.4 , pp. 47-54
    • Benson, T.E.1    Walsh, C.T.2    Hogle, J.M.3
  • 6
    • 0026880575 scopus 로고
    • Intracellular Steps of Bacterial Cell Wall Peptidoglycan Biosynthesis: Enzymology, Antibiotics, and Antibiotic Resistance
    • Bugg, T. D. H., & Walsh, C. T. (1992) Intracellular Steps of Bacterial Cell Wall Peptidoglycan Biosynthesis: Enzymology, Antibiotics, and Antibiotic Resistance, Nat. Prod. Rep. 9, 199-215.
    • (1992) Nat. Prod. Rep. , vol.9 , pp. 199-215
    • Bugg, T.D.H.1    Walsh, C.T.2
  • 8
    • 0029007512 scopus 로고
    • Steady-State Kinetic Mechanism of Escherichia coli UDP-N-Acetylenolpyruvylglucosamine Reductase
    • Dhalla, A. M., Yanchunas, J., Jr., Ho, H.-T., Falk, P., Villafranca, J. J., & Robertson, J. G. (1995) Steady-State Kinetic Mechanism of Escherichia coli UDP-N-Acetylenolpyruvylglucosamine Reductase, Biochemistry 34, 5390-5402.
    • (1995) Biochemistry , vol.34 , pp. 5390-5402
    • Dhalla, A.M.1    Yanchunas J., Jr.2    Ho, H.-T.3    Falk, P.4    Villafranca, J.J.5    Robertson, J.G.6
  • 9
    • 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
  • 10
    • 0015210971 scopus 로고
    • Circular Dichroism Studies of the Flavin Chromophore and of the Relation between Redox Properties and Flavin Environment in Oxidases and Dehydrogenases
    • Edmondson, D. E., & Tollin, G. (1971) Circular Dichroism Studies of the Flavin Chromophore and of the Relation Between Redox Properties and Flavin Environment in Oxidases and Dehydrogenases, Biochemistry 10, 113-123.
    • (1971) Biochemistry , vol.10 , pp. 113-123
    • Edmondson, D.E.1    Tollin, G.2
  • 11
    • 0000991825 scopus 로고
    • Some Problems in Interval Estimation
    • Fieller, E. C. (1954) Some Problems in Interval Estimation, J. R. Statist. Soc. B16, 175-185.
    • (1954) J. R. Statist. Soc. , vol.B16 , pp. 175-185
    • Fieller, E.C.1
  • 12
    • 0020997912 scopus 로고
    • Dictionary of Protein Secondary Structure: Pattern Recognition of Hydrogen-Bonded and Geometrical Features
    • Kabsch, W., & Sander, C. (1983) Dictionary of Protein Secondary Structure: Pattern Recognition of Hydrogen-Bonded and Geometrical Features, Biopolymers 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 13
    • 0028300515 scopus 로고
    • Modulation of the Oxidation-Reduction Potential of the Flavin in Lipoamide Dehydrogenase from Escherichia coli by Alteration of a Nearby Charged Residue, K53R
    • Maeda-Yorita, K., Russell, G. C., Guest, J. R., Massey, V., & Williams, C. H., Jr. (1994) Modulation of the Oxidation-Reduction Potential of the Flavin in Lipoamide Dehydrogenase from Escherichia coli by Alteration of a Nearby Charged Residue, K53R, Biochemistry 33, 6213-6220.
    • (1994) Biochemistry , vol.33 , pp. 6213-6220
    • Maeda-Yorita, K.1    Russell, G.C.2    Guest, J.R.3    Massey, V.4    Williams C.H., Jr.5
  • 14
    • 0023656828 scopus 로고
    • Variable Selection Method Improves the Prediction of Protein Secondary Structure from Circular Dichroism Spectra
    • Manavalan, P., & Johnson, W. C., Jr. (1987) Variable Selection Method Improves the Prediction of Protein Secondary Structure from Circular Dichroism Spectra, Anal. Biochem. 167, 76-85.
    • (1987) Anal. Biochem. , vol.167 , pp. 76-85
    • Manavalan, P.1    Johnson W.C., Jr.2
  • 15
    • 0019023686 scopus 로고
    • Active-Site Probes of Flavoproteins
    • Massey, V., & Hemmerich, P. (1980) Active-Site Probes of Flavoproteins, Biochem. Soc. Trans. 8, 246-257.
    • (1980) Biochem. Soc. Trans. , vol.8 , pp. 246-257
    • Massey, V.1    Hemmerich, P.2
  • 16
    • 0026823076 scopus 로고
    • Cloning and Identification of the Escherichia coli murB DNA Sequence, Which Encodes UDP-N-Acetylenolpyruvoylglucosamine Reductase
    • Pucci, M. J., Discotto, L. F., & Dougherty, T. J. (1992) Cloning and Identification of the Escherichia coli murB DNA Sequence, Which Encodes UDP-N-Acetylenolpyruvoylglucosamine Reductase, J. Bacteriol. 174, 1690-1693.
    • (1992) J. Bacteriol. , vol.174 , pp. 1690-1693
    • Pucci, M.J.1    Discotto, L.F.2    Dougherty, T.J.3
  • 17
    • 0027291015 scopus 로고
    • Prediction of Protein Structure at Better than 70% Accuracy
    • Rost, B., & Sander, C. (1993) Prediction of Protein Structure at Better than 70% Accuracy, J. Mol. Biol. 232, 584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 18
    • 0028300741 scopus 로고
    • Combining Evolutionary Information and Neural Networks to Predict Protein Secondary Structure
    • Rost, B., & Sander, C. (1994) Combining Evolutionary Information and Neural Networks to Predict Protein Secondary Structure, Proteins: Struct., Funct., Genet. 19, 55-72.
    • (1994) Proteins: Struct., Funct., Genet. , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 19
    • 0026457258 scopus 로고
    • Substitution of Arg214 at the Substrate-Binding Site of p-Hydroxybenzoate Hydroxylase from Pseudomonas fluorescens
    • van Berkel, W., Westphal, A., Eschrich, K., Eppink, M., & DeKok, A. (1992) Substitution of Arg214 at the Substrate-Binding Site of p-Hydroxybenzoate Hydroxylase from Pseudomonas fluorescens, Eur. J. Biochem. 210, 411-419.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 411-419
    • Van Berkel, W.1    Westphal, A.2    Eschrich, K.3    Eppink, M.4    DeKok, A.5
  • 20
    • 0015236836 scopus 로고
    • Pyridine-Nucleotide Transhydrogenase 4. Studies on the Reductive Mechanism of Transhydrogenase from Azotobacter vinelandii
    • van den Broek, H. W. J., & Veeger, C. (1971) Pyridine-Nucleotide Transhydrogenase 4. Studies on the Reductive Mechanism of Transhydrogenase from Azotobacter vinelandii, Eur. J. Biochem. 24, 63-71.
    • (1971) Eur. J. Biochem. , vol.24 , pp. 63-71
    • Van Den Broek, H.W.J.1    Veeger, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.