Studies on the active site of the Neurospora crassa plasma membrane H+-ATPase with periodate-oxidized nucleotides.
作者： A P Bidwai , N A Morjana , G A Scarborough
DOI: 10.1016/S0021-9258(18)80135-1
关键词: Biology 、 Vanadate 、 Stereochemistry 、 Binding site 、 Active site 、 Nucleotide 、 ATPase 、 Divalent 、 Neurospora crassa 、 Dephosphorylation 、 Biochemistry
摘要: Abstract The Neurospora crassa plasma membrane H+-ATPase is inactivated by the periodate-oxidized nucleotides, oATP, oADP, and oAMP, with oAMP most effective. Inhibition of ATPase essentially irreversible, because Sephadex G-50 column chromatography oAMP-treated does not result in a reversal inhibition. protected against substrate ATP, product ADP, competitive inhibitors TNP (2',3'-O-(2,4,6-trinitrocyclohexadienylidine)-ATP TNP-ADP, suggesting that inhibition occurs at nucleotide binding site enzyme. rate inactivation only slightly affected EDTA, indicating interaction absence divalent cation. protection ADP likewise unaffected EDTA. absolutely dependent on presence acidic phospholipids or lysophospholipids known to be required for activity, these lipids either aid formation render it accessible. Incubation Mg2+ plus vanadate, which locks enzyme conformation resembling transition state dephosphorylation reaction, completely protects this exist, inaccessible oAMP. Labeling studies [14C] indicate incorporation 1 mol sufficient cause complete ATPase.
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