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Volumn 320, Issue 2, 2002, Pages 237-247

Structure of porphobilinogen synthase from pseudomonas aeruginosa in complex with 5-fluorolevulinic acid suggests a double schiff base mechanism

Author keywords

5 fluorolevulinic acid; Crystal structure; Enzyme inhibitor complex; Porphobilinogen synthase; Pseudomonas aeruginosa

Indexed keywords

5 FLUOROLEVULINIC ACID; LEVULINIC ACID; PORPHOBILINOGEN SYNTHASE; SCHIFF BASE; UNCLASSIFIED DRUG;

EID: 0036299038     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00472-2     Document Type: Article
Times cited : (44)

References (31)
  • 11
    • 0014429273 scopus 로고
    • Delta-aminolevulinic acid dehydratase of Rhodospeudomonas spheroides II. Association to polymers and dissociation to subunits
    • (1968) J. Biol. Chem. , vol.243 , pp. 1231-1235
    • Nandi, D.L.1    Shemin, D.2
  • 18
    • 0023035981 scopus 로고
    • Dissection of the early steps in the porphobilinogen synthase catalyzed reaction. Requirements for Schiff's base formation
    • (1986) J. Biol. Chem. , vol.261 , pp. 9348-9353
    • Jaffe, E.K.1    Hanes, D.2
  • 19
    • 0028830064 scopus 로고
    • Characterization of the two 5-aminolevulinic acid binding sites, the A-and P-sites, of 5-aminolaevulinic acid dehydratase from Escherichia coli
    • (1995) Biochem. J. , vol.305 , pp. 151-158
    • Spencer, P.1    Jordan, P.M.2
  • 31
    • 0026597444 scopus 로고
    • Free R-value: A novel statistical quantity for assessing the accuracy of crystal structures
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.