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Volumn , Issue 11, 1999, Pages 2853-2857

Origin of the slow-binding inhibition of aldolase by D-glycero-tetrulose 1-phosphate (D-erythrulose 1-phosphate) from the comparison with the isosteric phosphonate analog

Author keywords

Aldolase; Bioorganic chemistry; Enzyme inhibitors; Enzyme mechanism; Structure activity relationship

Indexed keywords

ENZYME INHIBITOR; FRUCTOSE BISPHOSPHATE ALDOLASE; PHOSPHONIC ACID DERIVATIVE;

EID: 0032720421     PISSN: 1434193X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1099-0690(199911)1999:11<2853::aid-ejoc2853>3.0.co;2-0     Document Type: Article
Times cited : (6)

References (44)
  • 23
    • 0023464501 scopus 로고
    • Aldolases are considered as targets for the development of new antiparasitic drugs since glycolysis is the only source of energy for parasites, such as trypanosome: [8a] F. R. Opperdoes, Ann. Rev. Microbiol. 1987, 41, 127-151.
    • (1987) Ann. Rev. Microbiol. , vol.41 , pp. 127-151
    • Opperdoes, F.R.1
  • 27
    • 85088883200 scopus 로고    scopus 로고
    • note
    • -1) and E the amount of enzyme subunit (μmol) used in the assay.
  • 32
    • 0344787722 scopus 로고    scopus 로고
    • note
    • Concentrations of 4 and aldolase were 1 mM and 5 μM repectively, the resulting loss of enzyme activity was 34%. In controls performed with DHAP (1 mM), or L-erythrulose 1-phosphate (1 mM) used instead of compound 4, the resulting losses of enzyme activity were 45% and 34%, respectively. In other controls where 4 or sodium tetrahydroborate were omitted, no significant loss of enzyme activity was detected (< 5%). For the assay performed with D-erythrulose 1-phosphate (1 mM), the sample was dialyzed for 18 h against an inhibitor-free solution prior to the measurement of the enzyme activity. The resulting irreversible loss of enzyme activity was 53%. In controls where D-erythrulose 1-phosphate or sodium tetrahydroborate were omitted, the loss of enzyme activity was 10%.
  • 33
  • 35
    • 85088883135 scopus 로고    scopus 로고
    • note
    • 1H-NMR spectroscopy, or by oxidation by hexacyanoferrate(III), failed due possibly to the enzyme inhibition.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.