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Plant H^+-PPases: Reversible Enzymes with Contrasting Functions Dependent on Membrane Environment 被引量:1

Plant H^+-PPases: Reversible Enzymes with Contrasting Functions Dependent on Membrane Environment
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摘要 Plant proton-translocating pyrophosphatases (H^+-PPases) are generally thought of as tonoplast-localized proton pumps that utilize the energy released by hydrolysis of the phosphoanhydride bond of pyrophosphate (PPi) to assist in the acidification of the vacuole.It has been suggested that H^+-PPases function as an additional acidification mechanism to complement the ubiquitous V-ATPase,especially in young,growing tissues where PPi is abundant and ATP is depleted (Shiratake et al.,1997). Plant proton-translocating pyrophosphatases (H^+-PPases) are generally thought of as tonoplast-localized proton pumps that utilize the energy released by hydrolysis of the phosphoanhydride bond of pyrophosphate (PPi) to assist in the acidification of the vacuole.It has been suggested that H^+-PPases function as an additional acidification mechanism to complement the ubiquitous V-ATPase,especially in young,growing tissues where PPi is abundant and ATP is depleted (Shiratake et al.,1997).
出处 《Molecular Plant》 SCIE CAS CSCD 2016年第3期317-319,共3页 分子植物(英文版)
基金 This work was supported by the National Science Foundation (IOS-1122148 to G.A.P., J.P.-V., K.R., and R.A.G.).ACKNOWLEDGMENTS We thank E.G. Baxter (Arizona State University School of Life Sciences Visualization laboratory) for help with the model figure. We apologize to authors of several excellent papers who were not directly cited due to reference number restrictions. No conflict of interest declared.
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