Abstract:
:A conformational transition between E2 and E1 forms of Na, K-ATPase induced by different nucleotides has been studied under steady state conditions using the enzyme labelled with 5-iodoacetamidofluorescein. In the presence of K+ the plot of fluorescence as a function of [ATP], [ADP] or [CTP] (in a range of 5 microM-12 mM) is a biphasic one. A similar dependence for AMP, ITP, GTP and UTP demonstrates a hyperbolic behaviour. The data suggest that the shift in the equilibrium between E2 and E1 forms of Na,K-ATPase towards the E1 conformation is induced by ATP binding both with high and low affinity sites. Two structural features of ATP are apparently important for its interaction with more than one type of ATP binding sites or for providing for E2-E1 transition induced by this interaction: (i) beta-phosphate group in the terminal part of the molecule, (ii) unprotonated N1 and/or NH2-group in the 6th position of the purine base.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Lopina OD,Pindel EV,Boldyrev AAdoi
10.1016/0014-5793(90)81510-usubject
Has Abstractpub_date
1990-06-18 00:00:00pages
75-7issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(90)81510-Ujournal_volume
266pub_type
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