메뉴 건너뛰기




Volumn 11, Issue 6, 2004, Pages 539-543

A unique catalytic mechanism for UDP-galactopyranose mutase

Author keywords

[No Author keywords available]

Indexed keywords

ANTIMYCOBACTERIAL AGENT; ARABINOGALACTAN; CYANOBOROHYDRIDE SODIUM; FLAVINE NUCLEOTIDE; GALACTOSE; MUTASE; SODIUM BOROHYDRIDE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE GALACTOFURANOSE; URIDINE DIPHOSPHATE GALACTOPYRANOSE; URIDINE DIPHOSPHATE GALACTOPYRANOSE MUTASE;

EID: 2542428317     PISSN: 15459993     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsmb772     Document Type: Article
Times cited : (129)

References (37)
  • 1
    • 0026686943 scopus 로고
    • Tuberculosis: Commentary on a reemergent killer
    • Bloom, B.R. & Murray, C.J. Tuberculosis: commentary on a reemergent killer. Science 257, 1055-1064 (1992).
    • (1992) Science , vol.257 , pp. 1055-1064
    • Bloom, B.R.1    Murray, C.J.2
  • 2
    • 33845677589 scopus 로고    scopus 로고
    • World Health Organization, Geneva
    • World Health Organization. Fact Sheet No. 104 (World Health Organization, Geneva, 2002).
    • (2002) Fact Sheet No. 104
  • 4
    • 0035628608 scopus 로고    scopus 로고
    • Chemistry and biology of arabinofuranosyl- and galactofuranosyl-containing polysaccharides
    • Houseknecht, J.B. & Lowary, T.L. Chemistry and biology of arabinofuranosyl- and galactofuranosyl-containing polysaccharides. Curr. Opin. Chem. Biol. 5, 677-682 (2001).
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 677-682
    • Houseknecht, J.B.1    Lowary, T.L.2
  • 5
    • 0038247827 scopus 로고    scopus 로고
    • D-arabinofuranosides from Mycobacteria: Synthesis and conformation
    • Lowary, T.L. D-arabinofuranosides from Mycobacteria: synthesis and conformation (reprinted from Glycochemistry: Principles, Synthesis, and Applications (eds. Wang, P.G. & Bertozzi, C.R., Marcel Dekker, New York) 133-162, 2001), J. Carbohydr. Chem. 21, 691-722 (2002).
    • (2002) J. Carbohydr. Chem. , vol.21 , pp. 691-722
    • Lowary, T.L.1
  • 6
    • 0009696995 scopus 로고    scopus 로고
    • reprinted (eds. Wang, P.G. & Bertozzi, C.R., Marcel Dekker, New York)
    • Lowary, T.L. D-arabinofuranosides from Mycobacteria: synthesis and conformation (reprinted from Glycochemistry: Principles, Synthesis, and Applications (eds. Wang, P.G. & Bertozzi, C.R., Marcel Dekker, New York) 133-162, 2001), J. Carbohydr. Chem. 21, 691-722 (2002).
    • (2001) Glycochemistry: Principles, Synthesis, and Applications , pp. 133-162
  • 7
    • 0031417910 scopus 로고    scopus 로고
    • Biosynthetic origin of mycobacterial cell wall galactofuranosyl residues
    • Weston, A. et al. Biosynthetic origin of mycobacterial cell wall galactofuranosyl residues. Tuber. Lung Dis. 78, 123-131 (1997).
    • (1997) Tuber. Lung Dis. , vol.78 , pp. 123-131
    • Weston, A.1
  • 8
    • 0034971311 scopus 로고    scopus 로고
    • Cell wall core galactofuran synthesis is essential for growth of Mycobacteria
    • Pan, F., Jackson, M., Ma, Y.F. & McNeil, M. Cell wall core galactofuran synthesis is essential for growth of Mycobacteria. J. Bacteriol. 183, 3991-3998 (2001).
    • (2001) J. Bacteriol. , vol.183 , pp. 3991-3998
    • Pan, F.1    Jackson, M.2    Ma, Y.F.3    McNeil, M.4
  • 9
    • 0037301077 scopus 로고    scopus 로고
    • Galactofuranose metabolism: A potential target for antimicrobial chemotherapy
    • Pedersen, L.L. & Turco, S.J. Galactofuranose metabolism: a potential target for antimicrobial chemotherapy. Cell. Mol. Life Sci., 60, 259-266 (2003).
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 259-266
    • Pedersen, L.L.1    Turco, S.J.2
  • 10
    • 0033612742 scopus 로고    scopus 로고
    • Positional isotope exchange catalyzed by UDP-galactopyranose mutase
    • Barlow, J.N., Girvin, M.E. & Blanchard, J.S. Positional isotope exchange catalyzed by UDP-galactopyranose mutase. J. Am. Chem. Soc. 121, 6968-6969 (1999).
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 6968-6969
    • Barlow, J.N.1    Girvin, M.E.2    Blanchard, J.S.3
  • 11
    • 0034721448 scopus 로고    scopus 로고
    • Studies of UDP-galactopyranose mutase from Escherichia coli: An unusual role for reduced FAD in its catalysis
    • Zhang, Q. & Liu, H. Studies of UDP-galactopyranose mutase from Escherichia coli: an unusual role for reduced FAD in its catalysis. J. Am. Chem. Soc. 122, 9065-9070 (2000).
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 9065-9070
    • Zhang, Q.1    Liu, H.2
  • 12
    • 0028355860 scopus 로고
    • Structure of the O antigen of Escherichia coli K-12 and the sequence of its rfb gene cluster
    • Stevenson, G. et al. Structure of the O antigen of Escherichia coli K-12 and the sequence of its rfb gene cluster. J. Bacteriol. 176, 4144-4156 (1994).
    • (1994) J. Bacteriol. , vol.176 , pp. 4144-4156
    • Stevenson, G.1
  • 13
    • 0033851115 scopus 로고    scopus 로고
    • The chemical and biological versatility of riboflavin
    • Massey, V. The chemical and biological versatility of riboflavin. Biochem. Soc. Trans. 28, 283-296 (2000).
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 283-296
    • Massey, V.1
  • 14
    • 0024601564 scopus 로고
    • Mechanisms of flavoprotein-catalyzed reactions
    • Ghisla, S. & Massey, V. Mechanisms of flavoprotein-catalyzed reactions. Eur. J. Biochem. 181, 1-17 (1989).
    • (1989) Eur. J. Biochem. , vol.181 , pp. 1-17
    • Ghisla, S.1    Massey, V.2
  • 15
    • 0034815662 scopus 로고    scopus 로고
    • UDP-galactopyranose mutase has a novel structure and mechanism
    • Sanders, D.A.R. et al. UDP-galactopyranose mutase has a novel structure and mechanism. Nat. Struct. Biol. 8, 858-863 (2001).
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 858-863
    • Sanders, D.A.R.1
  • 16
    • 0032898919 scopus 로고    scopus 로고
    • NifL of Klebsiella pneumoniae: Redox characterization in relation to the nitrogen source
    • Klopprogge, K. & Schmitz, R.A. NifL of Klebsiella pneumoniae: redox characterization in relation to the nitrogen source. Biochim. Biophys. Acta. 1431, 462-470 (1999).
    • (1999) Biochim. Biophys. Acta , vol.1431 , pp. 462-470
    • Klopprogge, K.1    Schmitz, R.A.2
  • 17
    • 0024076739 scopus 로고
    • Common ancestry of Escherichia coli pyruvate oxidase and the acetohydroxy acid synthases of the branched-chain amino acid biosynthetic pathway
    • Chang, Y.Y. & Cronan, J.E. Common ancestry of Escherichia coli pyruvate oxidase and the acetohydroxy acid synthases of the branched-chain amino acid biosynthetic pathway. J. Bacteriol. 170, 3937-3945 (1988).
    • (1988) J. Bacteriol. , vol.170 , pp. 3937-3945
    • Chang, Y.Y.1    Cronan, J.E.2
  • 18
    • 0032537483 scopus 로고    scopus 로고
    • Biosynthesis of 2-aceto-2-hydroxy acids: Acetolactate synthases and acetohydroxyacid synthases
    • Chipman, D., Barak, Z. & Schloss, J.V. Biosynthesis of 2-aceto-2-hydroxy acids: acetolactate synthases and acetohydroxyacid synthases. Biochim. Biophys. Acta 1385, 401-419 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1385 , pp. 401-419
    • Chipman, D.1    Barak, Z.2    Schloss, J.V.3
  • 19
    • 0242468752 scopus 로고    scopus 로고
    • Reconstitution of UDP-galactopyranose mutase with 1-deaza-FAD and 5-deaza-FAD: Analysis and mechanistic implications
    • Huang, Z., Zhang, Q. & Liu, H. Reconstitution of UDP-galactopyranose mutase with 1-deaza-FAD and 5-deaza-FAD: analysis and mechanistic implications. Bioorg. Chem. 31, 494-502 (2003).
    • (2003) Bioorg. Chem. , vol.31 , pp. 494-502
    • Huang, Z.1    Zhang, Q.2    Liu, H.3
  • 20
    • 0034612999 scopus 로고    scopus 로고
    • Enzymatic synthesis of UDP-(3-deoxy-3-fluoro)-D-galactose and UDP-(2-deoxy-2-fluoro)-D-galactose and substrate activity with UDP-galactopyranose mutase
    • Barlow, J.N. & Blanchard, J.S. Enzymatic synthesis of UDP-(3-deoxy-3-fluoro)-D-galactose and UDP-(2-deoxy-2-fluoro)-D-galactose and substrate activity with UDP-galactopyranose mutase. Carbohydr. Res. 328, 473-480 (2000).
    • (2000) Carbohydr. Res. , vol.328 , pp. 473-480
    • Barlow, J.N.1    Blanchard, J.S.2
  • 21
    • 0344407501 scopus 로고    scopus 로고
    • Potentiometric analysis of UDP-galactopyranose mutase: Stabilization of the flavosemiquinone by substrate
    • Fullerton, S.W.B et al. Potentiometric analysis of UDP-galactopyranose mutase: stabilization of the flavosemiquinone by substrate. Biochemistry 42, 2104-2109 (2003).
    • (2003) Biochemistry , vol.42 , pp. 2104-2109
    • Fullerton, S.W.B.1
  • 23
    • 0037133184 scopus 로고    scopus 로고
    • Structure of adenylylsulfate reductase from the hyperthermophilic Archaeoglobus fulgidus at 1.6-Å resolution
    • Fritz, G. et al. Structure of adenylylsulfate reductase from the hyperthermophilic Archaeoglobus fulgidus at 1.6-Å resolution. Proc. Natl. Acad. Sci. USA 99, 1836-1841 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1836-1841
    • Fritz, G.1
  • 24
    • 0022800854 scopus 로고
    • New flavins for old: Artificial flavins as active site probes of flavoproteins
    • Ghisla, S. & Massey, V. New flavins for old: artificial flavins as active site probes of flavoproteins. Biochem. J. 239, 1-12 (1986).
    • (1986) Biochem. J. , vol.239 , pp. 1-12
    • Ghisla, S.1    Massey, V.2
  • 25
    • 0008181750 scopus 로고
    • The kinetics and mechanism of 1,5-dihydroflavin reduction of carbonyl compounds and flavin oxidation of alcohols
    • Williams, R.F. & Bruice, T.C. The kinetics and mechanism of 1,5-dihydroflavin reduction of carbonyl compounds and flavin oxidation of alcohols. J. Am. Chem. Soc. 98, 7752-7768 (1976).
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 7752-7768
    • Williams, R.F.1    Bruice, T.C.2
  • 26
    • 0017313963 scopus 로고
    • The chemistry of an N5-methyl-1,5-dihydroflavin and its aminium cation radical
    • Kemal, C. & Bruice, T.C. The chemistry of an N5-methyl-1,5-dihydroflavin and its aminium cation radical. J. Am. Chem. Soc. 98, 3955-3964 (1976).
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 3955-3964
    • Kemal, C.1    Bruice, T.C.2
  • 28
    • 0015785951 scopus 로고
    • Direct evidence for carbanions and covalent N5-flavine-carbanion adducts as catalytic intermediates in the oxidation of nitroethane by D-amino acid oxidase
    • Porter, D.J.T., Voet, J.G., & Bright, H.J. Direct evidence for carbanions and covalent N5-flavine-carbanion adducts as catalytic intermediates in the oxidation of nitroethane by D-amino acid oxidase. J. Biol. Chem. 248, 4400-4416 (1973).
    • (1973) J. Biol. Chem. , vol.248 , pp. 4400-4416
    • Porter, D.J.T.1    Voet, J.G.2    Bright, H.J.3
  • 29
    • 0017764982 scopus 로고
    • Kinetics and mechanisms of the 1,5-dihydroflavin reduction of carbonyl compounds and the flavin oxidation of alcohols
    • Williams, R.F., Shinkai, S.S. & Bruice, T.C. Kinetics and mechanisms of the 1,5-dihydroflavin reduction of carbonyl compounds and the flavin oxidation of alcohols. J. Am. Chem. Soc. 99, 921-931 (1977).
    • (1977) J. Am. Chem. Soc. , vol.99 , pp. 921-931
    • Williams, R.F.1    Shinkai, S.S.2    Bruice, T.C.3
  • 30
    • 33947471043 scopus 로고
    • The factors determining nucleophilic reactivities
    • Edwards, J.O. & Pearson, R.G. The factors determining nucleophilic reactivities. J. Am. Chem. Soc. 84, 16-24 (1962).
    • (1962) J. Am. Chem. Soc. , vol.84 , pp. 16-24
    • Edwards, J.O.1    Pearson, R.G.2
  • 31
    • 84985083786 scopus 로고
    • The α-effect - A critical examination of the phenomenon and its origin
    • Hoz, S. & Buncel, E. The α-effect - a critical examination of the phenomenon and its origin. Israel J. Chem. 26, 313-319 (1985).
    • (1985) Israel J. Chem. , vol.26 , pp. 313-319
    • Hoz, S.1    Buncel, E.2
  • 32
    • 0033842423 scopus 로고    scopus 로고
    • A mechanistic study of the dihydroflavin reductive cleavage of the dihydroflavin-tetrahydronaphthalene epoxide adducts
    • Lee, Y.T. & Fisher, J.F. A mechanistic study of the dihydroflavin reductive cleavage of the dihydroflavin-tetrahydronaphthalene epoxide adducts. Bioorg. Chem. 28, 163-175 (2000).
    • (2000) Bioorg. Chem. , vol.28 , pp. 163-175
    • Lee, Y.T.1    Fisher, J.F.2
  • 33
    • 0014028239 scopus 로고
    • The mechanism of the condensation of formaldehyde with tetrahydrofolic acid
    • Kallen, R.G. & Jencks, W.P. The mechanism of the condensation of formaldehyde with tetrahydrofolic acid. J. Biol. Chem. 241, 5851-5863 (1966).
    • (1966) J. Biol. Chem. , vol.241 , pp. 5851-5863
    • Kallen, R.G.1    Jencks, W.P.2
  • 34
    • 0019980204 scopus 로고
    • Are the redox properties of tetrahydrofolate cofactors utilized in folate-dependent reactions?
    • Matthews, R.G. Are the redox properties of tetrahydrofolate cofactors utilized in folate-dependent reactions? Fed. Proc. 41, 2600-2604 (1982).
    • (1982) Fed. Proc. , vol.41 , pp. 2600-2604
    • Matthews, R.G.1
  • 35
    • 0001209090 scopus 로고
    • Flavin coenzymes: At the crossroads of biological redox chemistry
    • Walsh, C. Flavin coenzymes: at the crossroads of biological redox chemistry. Acc. Chem. Res. 13, 148-155 (1980).
    • (1980) Acc. Chem. Res. , vol.13 , pp. 148-155
    • Walsh, C.1
  • 36
    • 0034860788 scopus 로고    scopus 로고
    • Substrate dehydrogenation by flavoproteins
    • Fitzpatrick, P.F. Substrate dehydrogenation by flavoproteins. Acc. Chem. Res. 34, 299-307 (2001).
    • (2001) Acc. Chem. Res. , vol.34 , pp. 299-307
    • Fitzpatrick, P.F.1
  • 37
    • 0035833723 scopus 로고    scopus 로고
    • Improved chemical synthesis of UDP-galactofuranose
    • Marlow, A.L. & Kiessling, L.L. Improved chemical synthesis of UDP-galactofuranose. Org. Lett. 3, 2517-2519 (2001).
    • (2001) Org. Lett. , vol.3 , pp. 2517-2519
    • Marlow, A.L.1    Kiessling, L.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.