메뉴 건너뛰기




Volumn 581, Issue 29, 2007, Pages 5597-5600

Glucose-6-phosphate as a probe for the glucosamine-6-phosphate N-acetyltransferase Michaelis complex

Author keywords

Acetyltransferase; Crystal structure; Inhibitor; Kinetics; Michaelis complex; UDP GlcNAc

Indexed keywords

ACETYL COENZYME A; ANTIFUNGAL AGENT; GLUCOSAMINE PHOSPHATE ACETYLTRANSFERASE; GLUCOSE 6 PHOSPHATE; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE;

EID: 36549056086     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.10.065     Document Type: Article
Times cited : (12)

References (18)
  • 1
    • 0014806761 scopus 로고
    • A mutation in aspergillus nidulans producing hyphal walls which lack chitin
    • Katz D., and Rosenberger R.F. A mutation in aspergillus nidulans producing hyphal walls which lack chitin. Biochim. Biophys. Acta 208 (1970) 452-460
    • (1970) Biochim. Biophys. Acta , vol.208 , pp. 452-460
    • Katz, D.1    Rosenberger, R.F.2
  • 3
    • 0017173199 scopus 로고
    • The last two pathway-specific enzyme activities of hexosamine biosynthesis are present in blastocladiella emersonii zoospores prior to germination
    • Selitrennikoff C.P., and Sonneborn D.R. The last two pathway-specific enzyme activities of hexosamine biosynthesis are present in blastocladiella emersonii zoospores prior to germination. Biochim. Biophys. Acta 451 (1976) 408-416
    • (1976) Biochim. Biophys. Acta , vol.451 , pp. 408-416
    • Selitrennikoff, C.P.1    Sonneborn, D.R.2
  • 4
    • 0028271352 scopus 로고
    • Characterization of the essential yeast gene encoding N-acetylglucosamine-phosphate mutase
    • Hofmann M., Boles E., and Zimmermann F.K. Characterization of the essential yeast gene encoding N-acetylglucosamine-phosphate mutase. Eur. J. Biochem. 221 (1994) 741-747
    • (1994) Eur. J. Biochem. , vol.221 , pp. 741-747
    • Hofmann, M.1    Boles, E.2    Zimmermann, F.K.3
  • 5
    • 0027179961 scopus 로고
    • Developmental regulation of hexosamine biosynthesis by protein phosphatases 2a and 2c in blastocladiella emersonii
    • Etchebehere L.C., Simon M.N., Campanhã R.B., Zapella P.D., Véron M., and Maia J.C. Developmental regulation of hexosamine biosynthesis by protein phosphatases 2a and 2c in blastocladiella emersonii. J. Bacteriol. 175 (1993) 5022-5027
    • (1993) J. Bacteriol. , vol.175 , pp. 5022-5027
    • Etchebehere, L.C.1    Simon, M.N.2    Campanhã, R.B.3    Zapella, P.D.4    Véron, M.5    Maia, J.C.6
  • 7
    • 0035844169 scopus 로고    scopus 로고
    • The crystal structures of apo and complexed saccharomyces cerevisiae gna1 shed light on the catalytic mechanism of an amino-sugar n-acetyltransferase
    • Peneff C., Mengin-Lecreulx D., and Bourne Y. The crystal structures of apo and complexed saccharomyces cerevisiae gna1 shed light on the catalytic mechanism of an amino-sugar n-acetyltransferase. J. Biol. Chem. 276 (2001) 16328-16334
    • (2001) J. Biol. Chem. , vol.276 , pp. 16328-16334
    • Peneff, C.1    Mengin-Lecreulx, D.2    Bourne, Y.3
  • 8
    • 36549018818 scopus 로고    scopus 로고
    • Hurtado, R., Plotnikov, A.N. and van Aalten, D.M.F. (in preparation) Structural and kinetic analysis of human and Aspergillus fumigatus glucosamine n-acetyl transferase reveals exploitable active site differences.
  • 9
    • 0018416496 scopus 로고
    • Ellman's reagent: 5,5′-dithiobis(2-nitrobenzoic acid) - a reexamination
    • Riddles P., Blakeley R., and Zerner B. Ellman's reagent: 5,5′-dithiobis(2-nitrobenzoic acid) - a reexamination. Anal. Biochem. 97 (1979) 75-81
    • (1979) Anal. Biochem. , vol.97 , pp. 75-81
    • Riddles, P.1    Blakeley, R.2    Zerner, B.3
  • 10
    • 0030051742 scopus 로고    scopus 로고
    • Acetyltransfer precedes uridylyltransfer in the formation of udp-n-acetylglucosamine in separable active sites of the bifunctional glmu protein of Escherichia coli
    • Gehring A.M., Lees W.J., Mindiola D.J., Walsh C.T., and Brown E.D. Acetyltransfer precedes uridylyltransfer in the formation of udp-n-acetylglucosamine in separable active sites of the bifunctional glmu protein of Escherichia coli. Biochemistry 35 (1996) 579-585
    • (1996) Biochemistry , vol.35 , pp. 579-585
    • Gehring, A.M.1    Lees, W.J.2    Mindiola, D.J.3    Walsh, C.T.4    Brown, E.D.5
  • 12
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Cryst. D 53 (1997) 240-255
    • (1997) Acta Cryst. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 13
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Cryst. D 60 (2004) 2126-2132
    • (2004) Acta Cryst. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 14
    • 7544226311 scopus 로고    scopus 로고
    • Prodrg: a tool for high-throughput crystallography of protein-ligand complexes
    • Schuettelkopf A.W., and van Aalten D.M.F. Prodrg: a tool for high-throughput crystallography of protein-ligand complexes. Acta Cryst. D 60 (2004) 1355-1363
    • (2004) Acta Cryst. D , vol.60 , pp. 1355-1363
    • Schuettelkopf, A.W.1    van Aalten, D.M.F.2
  • 15
    • 0025398721 scopus 로고
    • WHAT IF: a molecular modeling and drug design program
    • Vriend G. WHAT IF: a molecular modeling and drug design program. J. Mol. Graph. 8 (1990) 52-56
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 16
    • 36549044164 scopus 로고    scopus 로고
    • DeLano, W.L. (2004). Use of pymol as a communications tool for molecular science. Abstr. Pap. Am. Chem. Soc. 228, 030-CHED.
  • 17
    • 0001109389 scopus 로고
    • Stereochemistry of reaction. paths at carbonyl centers
    • Buergi H.B., Dunitz J.D., Lehn J.M., and Wipff G. Stereochemistry of reaction. paths at carbonyl centers. Tetrahedron 30 (1974) 1563-1572
    • (1974) Tetrahedron , vol.30 , pp. 1563-1572
    • Buergi, H.B.1    Dunitz, J.D.2    Lehn, J.M.3    Wipff, G.4
  • 18
    • 0032898932 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae gna1, an essential gene encoding a novel acetyltransferase involved in udp-n-acetylglucosamine synthesis
    • Mio T., Yamada-Okabe T., Arisawa M., and Yamada-Okabe H. Saccharomyces cerevisiae gna1, an essential gene encoding a novel acetyltransferase involved in udp-n-acetylglucosamine synthesis. J. Biol. Chem. 274 (1999) 424-429
    • (1999) J. Biol. Chem. , vol.274 , pp. 424-429
    • Mio, T.1    Yamada-Okabe, T.2    Arisawa, M.3    Yamada-Okabe, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.