Probing Energy Coupling in the Yeast Plasma Membrane H+-ATPase with Acetyl Phosphate
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference39 articles.
1. Structure and function of proton translocating ATPase in plasma membranes of plants and fungi
2. Relationships of molecular structure and function in Ca2(+)-transport ATPase
3. Structure and Function of Plasma Membrane ATPase
4. The predicted secondary structures of the nucleotide-binding sites of six cation-transporting ATPases lead to a probable tertiary fold
5. The energy transduction mechanism is different among P-type ion-transporting ATPases. Acetyl phosphate causes uncoupling between hydrolysis and ion transport in H+,K(+)-ATPase.
Cited by 7 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Metabolic Engineering of a Phosphoketolase Pathway for Pentose Catabolism in Saccharomyces cerevisiae;Applied and Environmental Microbiology;2004-05
2. Molecular Architecture of the Phosphorylation Region of the Yeast Plasma Membrane H+-ATPase;Journal of Biological Chemistry;2003-02
3. Dissecting the Hydrolytic Activities of Sarcoplasmic Reticulum ATPase in the Presence of Acetyl Phosphate;Journal of Biological Chemistry;2002-10
4. Slippage and uncoupling in P-type cation pumps; implications for energy transduction mechanisms and regulation of metabolism;Biochimica et Biophysica Acta (BBA) - Biomembranes;2001-08
5. Stability and Structure of Metal Ion Complexes Formed in Solution with Acetyl Phosphate and Acetonylphosphonate: Quantification of Isomeric Equilibria;Journal of the American Chemical Society;1999-06-19
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