Arginine 383 is a crucial residue in ABCG2 biogenesis
نویسندگان
چکیده
منابع مشابه
Arginine 383 is a crucial residue in ABCG2 biogenesis.
ABCG2 is an ATP-binding cassette half-transporter initially identified in multidrug-resistant cancer cell lines and recently suggested to play an important role in pharmacokinetics. Here we report studies of a conserved arginine predicted to localize near the cytoplasmic side of TM1. First, we determined the effect of losing charge and bulk at this position via substitutions with glycine and al...
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The 76-kDa NtpI subunit constitutes the membrane-embedded V(0) moiety of Enterococcus hirae vacuolar type Na+-ATPase with a 16-kDa NtpK hexamer containing Na+ binding sites. In this study, we investigated the role of an arginine residue, which is highly conserved among the corresponding subunits of bacterial vacuolar-type ATPases, at position 573 of NtpI. Substitution of Glu, Leu, or Gln for Ar...
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Reaction of phenylglyoxal, a reagent specific for arginine residues, with porcine phospholipase Az results in complete elimination of catalytic activity. The modification reaction is markedly dependent on pH. Other dicarbonyl compounds such as 2,3-butanedione and 1,2cyclohexanedione also react with the enzyme to cause loss of activity but at significantly slower rates. At pH 7.0, the inactivati...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Biomembranes
سال: 2009
ISSN: 0005-2736
DOI: 10.1016/j.bbamem.2009.04.016