Functional Enhancement by Single-residue Substitution of Streptomyces coelicolor A3(2) H+-translocating Pyrophosphatase
Author:
Publisher
Oxford University Press (OUP)
Subject
Molecular Biology,Biochemistry,General Medicine
Link
http://academic.oup.com/jb/article-pdf/146/5/617/14113812/mvp114.pdf
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2. Vacuolar H+-pyrophosphatases: from the evolutionary backwaters into the mainstream;Drozdowicz;Trends Plant Sci.,2001
3. Site-directed mutagenesis of vacuolar H+-pyrophosphatase: necessity of Cys634 for inhibition by maleimides but not catalysis;Kim;J. Biol. Chem.,1995
4. Acidic residues necessary for pyrophosphate-energized pumping and inhibition of the vacuolar H+-pyrophosphatase by N,N′-dicyclohexylcarbodiimide;Zhen;J. Biol. Chem.,1997
5. Mutagenesis analysis of functional residues in putative substrate-binding site and acidic domains of vacuolar H+-pyrophosphatase;Nakanishi;J. Biol. Chem.,2001
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1. A Simple Strategy to Determine the Dependence of Membrane-Bound Pyrophosphatases on K+ as a Cofactor;Methods in Enzymology;2018
2. Membrane pyrophosphatases from Thermotoga maritima and Vigna radiata suggest a conserved coupling mechanism;Nature Communications;2016-12
3. Identification of the critical residues for the function of vacuolar H+-pyrophosphatase by mutational analysis based on the 3D structure;The Journal of Biochemistry;2014-07-28
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