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• W1986784642 abstract "Abstract 1. Soluble beef-heart mitochondrial ATPase (F 1 ) was incubated with [ 3 H]pyridoxal 5′-phosphate and the Schiffbase complex formed was reduced with sodium borohydride. Spectral measurements indicate that lysine residues are modified and gel electrophoresis in the presence of detergent shows the tritium label to be associated with the two largest subunits, α and β. 2. In the absence of protecting ligands, the loss of ATP hydrolysis activity is linearly dependent on the level of pyridoxylation with complete inactivation correlating to 10 mol pyridoxamine phosphate incorporated per mol enzyme. Partial inactivation of F 1 with pyridoxal phosphate has no effect on either the K m for ATP or the ability of bicarbonate to stimulate residual hydrolysis activity, suggesting a mixed population of fully active and fully inactive enzyme. 3. In the presence of excess magnesium, the addition of ADP or ATP, but not AMP, decreases the rate and extent of modification of F 1 by pyridoxal phosphate. The non-hydrolyzable ATP analog, 5′-adenylyl-β, γ-imidodiphosphate, is particularly effective in protecting F 1 against both modification and inactivation. Efrapeptin and P i have no effect on the modification reaction. 4. Prior modification of F 1 with pyridoxal phosphate decreases the number of exchangeable nucleotide binding sites by one. However, pyridoxylation of F 1 is ineffective in displacing endogenous nucleotides bound at non-catalytic sites and does not affect the stoichiometry of P i binding. 5. The ability of nucleotides to protect against modification and inactivation by pyridoxal phosphate and the loss of one exchangeable nucleotide site with the pyridoxylation of F 1 suggest the presence of a positively charged lysine residue at the catalytic site of an enzyme that binds two negatively charged substrates." @default.
• W1986784642 created "2016-06-24" @default.
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• W1986784642 date "1982-02-01" @default.
• W1986784642 modified "2023-09-26" @default.
• W1986784642 title "Pyridoxylation of essential lysine residues of mitochondrial adenosine triphosphatase" @default.
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• W1986784642 doi "https://doi.org/10.1016/0005-2728(82)90297-3" @default.
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