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Volumn 56, Issue 3, 2004, Pages 625-628

Crystal structures of Staphylococcus aureus type I dehydroquinase from enzyme turnover experiments

Author keywords

[No Author keywords available]

Indexed keywords

3 DEHYDROQUINATE DEHYDRATASE;

EID: 3142688132     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20165     Document Type: Article
Times cited : (18)

References (16)
  • 3
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    • Hawkins AR, Lamb HK, Moore JD, Charles IG, Roberts CF. The pre-chorismate (shikimate) and quinate pathways in filamentous fungi: theoretical and practical aspects. J Gen Microbiol 1993;139: 2891-2899.
    • (1993) J Gen Microbiol , vol.139 , pp. 2891-2899
    • Hawkins, A.R.1    Lamb, H.K.2    Moore, J.D.3    Charles, I.G.4    Roberts, C.F.5
  • 5
    • 0022432581 scopus 로고
    • Nucleotide sequence encoding the biosynthetic dehydroquinase function of the penta-functional arom locus of Aspergillus nidulans
    • Charles IG, Keyte JW, Brammar WJ, Hawkins AR. Nucleotide sequence encoding the biosynthetic dehydroquinase function of the penta-functional arom locus of Aspergillus nidulans. Nucleic Acids Res 1985;13:8119-8128.
    • (1985) Nucleic Acids Res , vol.13 , pp. 8119-8128
    • Charles, I.G.1    Keyte, J.W.2    Brammar, W.J.3    Hawkins, A.R.4
  • 6
    • 0025877807 scopus 로고
    • Identification of the active-site lysine residues of two biosynthetic 3-dehydroquinases
    • Chaudhuri S, Duncan K, Graham LD, Coggins JR. Identification of the active-site lysine residues of two biosynthetic 3-dehydroquinases. Biochem J 1991;275:1-6.
    • (1991) Biochem J , vol.275 , pp. 1-6
    • Chaudhuri, S.1    Duncan, K.2    Graham, L.D.3    Coggins, J.R.4
  • 7
    • 0029824788 scopus 로고    scopus 로고
    • Evidence from kinetic isotope studies for an enolate intermediate in the mechanism of type II dehydroquinases
    • Harris JM, Gonzalez-Bello C, Kleanthous C, Hawkins AR, Coggins JR, Abell C. Evidence from kinetic isotope studies for an enolate intermediate in the mechanism of type II dehydroquinases. Biochem J 1996;319:333-336.
    • (1996) Biochem J , vol.319 , pp. 333-336
    • Harris, J.M.1    Gonzalez-Bello, C.2    Kleanthous, C.3    Hawkins, A.R.4    Coggins, J.R.5    Abell, C.6
  • 10
    • 0037603068 scopus 로고    scopus 로고
    • Crystal structure of the type II 3-dehydroquinase from Helicobacter pylori
    • Lee BI, Kwak JE, Suh SW. Crystal structure of the type II 3-dehydroquinase from Helicobacter pylori. Proteins 2003;51:616-617.
    • (2003) Proteins , vol.51 , pp. 616-617
    • Lee, B.I.1    Kwak, J.E.2    Suh, S.W.3
  • 11
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 1997;276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otinowski, Z.1    Minor, W.2
  • 13
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 1991; 47:110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 14
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    • The CCP4 suite: Programs for protein crystallography
    • Collaborative-Computational-Project-4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994;50:760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.