New PDF release: Molecular and Cellular Mechanisms of H+ Transport

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Additional info for Molecular and Cellular Mechanisms of H+ Transport

Example text

Molecular modeling studies suggest that binding is to phe124 and asp136 (12). This region of the H/K ATPase is homologous to the region responsible for high afimity ouabain binding to the Na,K ATPase (13). These data substantiate the presence of the iIrSt two segments spanning the membrane in the a subunit of the HlK ATPase, as deduced from the trypsinolysis data. Further, a fluorescent K+ competitive arylquinoline, MDPQ, shows enhanced hydrophobicity of its environment with formation of the E2-P·I conformer of the enzyme, suggesting that the MlIloop/M2 segment moves cytoplasmically as the enzyme assumes the E2 conformation(14).

229-254. The Topology of the 0: , ft Subunits of the Gastric HIK ATPase Jai Moo Shin, Krister Bamberg, Marie Besancon, Keith Munson, Frederic Mercier, Dennis Bayle, Steve Hersey* and George Sachs UCLA and Wadsworth VAMC, Los Angeles and * Emory University, Atlanta Supported by USV A SMI and NIH grant #'s 40615, 41301 and 14752. INTRODUCTION Knowledge of the secondary structure of the gastric H/K ATPase,a P type transport ATPase, allows deductions as to the ion transport pathway across the membrane spanning domain of the large, 1033 amino acid catalytic 0: subunit and as to the site of interaction between the smaller, glycosylated, 6 subunit and the 0: subunit.

The protonated form does not bind in the region of cys 892 or cys 321. Omeprazole is less stabilised and converts rapidly to the sulfenamide after 44 binding to the enzyme in its protonated form close to cys 813. Omeprazole reacts irrst: with cys 813, thus preventing reaction with cys 822 by steric hindrance of access of the sulfenamide to this second cysteine in the M6 segment. Omeprazole also reacts with cys 892 which is probably in the vicinity of the omeprazole-H + binding site. Lansoprazole is the least stabilised by protein binding, and reacts with aU the cysteines available from the extracytoplasmic surface, namely cys 321, 813 and 892.

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