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Volumn 357, Issue 2, 2001, Pages 399-405

Characterization of active-site residues in diadenosine tetraphosphate hydrolase from Lupinus angustifolius

Author keywords

Ap4A; Catalytic site; Kinetics; Mutagenesis; Nudix

Indexed keywords

CATALYST ACTIVITY; ESCHERICHIA COLI; HYDROLYSIS; LIVING SYSTEMS STUDIES; MUTAGENESIS;

EID: 0035878923     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3570399     Document Type: Article
Times cited : (32)

References (28)
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    • The gene, ialA, associated with the invasion of human erythrocytes by Bartonella bacilliformis, designates a nudix hydrolase active on dinucleoside 5′-polyphosphates
    • (1999) J. Biol. Chem. , vol.274 , pp. 1203-1206
    • Conyers, G.B.1    Bessman, M.J.2
  • 4
  • 17
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    • Enzymes hydrolyzing ApppA and/or AppppA in higher plants. Purification and some properties of diadenosine triphosphatase, diadenosine tetraphosphatase, and phosphodiesterase from yellow lupin (Lupinus luteus) seeds
    • (1983) J. Biol. Chem. , vol.258 , pp. 9982-9989
    • Jakubowski, H.1    Guranowski, A.2
  • 19
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    • The DCP2 protein is required for mRNA decapping in Saccharomyces cerevisiae and contains a functional MutT motif
    • (1999) EMBO J. , vol.18 , pp. 5411-5422
    • Dunckley, T.1    Parker, R.2
  • 20
    • 0033544954 scopus 로고    scopus 로고
    • Site-directed mutagenesis of diphosphoinositol polyphosphate phosphohydrolase, a dual specificity NUDT enzyme that attacks diadenosine polyphosphates and diphosphoinositol polyphosphates
    • (1999) J. Biol. Chem. , vol.274 , pp. 35434-35440
    • Yang, X.1    Safrany, S.T.2    Shears, S.B.3
  • 25
    • 0025256426 scopus 로고
    • Fluoride is a strong and specific inhibitor of (asymmetrical) Ap4A hydrolases
    • (1990) FEBS Lett. , vol.262 , pp. 205-208
    • Guranowski, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.