Functional role of aspartyl and glutamyl residues in the membrane segments of the yeast PMA1 ATPase: interaction with DCCD.
Padmanabha
K P
KP
Department of Genetics, Yale University School of Medicine, New Haven, CT 06510, USA.
Pardo
J P
JP
Petrov
V V
VV
Sen Gupta
S
S
Slayman
C W
CW
D001224:Aspartic Acid / Q000235:genetics / Q000378:metabolism*; D002462:Cell Membrane / Q000201:enzymology; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology*; D005656:Fungal Proteins / Q000187:drug effects / Q000235:genetics / Q000378:metabolism; D018698:Glutamic Acid / Q000235:genetics / Q000378:metabolism*; D016297:Mutagenesis, Site-Directed; D006180:Proton-Translocating ATPases / Q000187:drug effects / Q000235:genetics / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D029701:Saccharomyces cerevisiae Proteins; D013329:Structure-Activity Relationship; D014475:Uncoupling Agents / Q000494:pharmacology*
D005656:Fungal Proteins; C434364:PMA2 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D014475:Uncoupling Agents; D001224:Aspartic Acid; D018698:Glutamic Acid; D004024:Dicyclohexylcarbodiimide; C092477:PMA1 protein, S cerevisiae; D006180:Proton-Translocating ATPases