Title : Functional mapping and implications of substrate specificity of the yeast high-affinity leucine permease Bap2.

Pub. Date : 2014 Jul

PMID : 24699373






4 Functional Relationships(s)
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1 In Saccharomyces cerevisiae, leucine uptake is mediated by multiple amino acid permeases, including the high-affinity leucine permease Bap2. Leucine branched-chain amino acid permease BAP2 Saccharomyces cerevisiae S288C
2 Upon leucine binding, these alpha-helix breaks were assumed to mediate a conformational transition in Bap2 from an outward-open to a substrate-binding occluded state. Leucine branched-chain amino acid permease BAP2 Saccharomyces cerevisiae S288C
3 Bap2-mediated leucine import was inhibited by some amino acids according to the following order of severity: phenylalanine, leucine>isoleucine>methionine, tyrosine>valine>tryptophan; histidine and asparagine had no effect. Leucine branched-chain amino acid permease BAP2 Saccharomyces cerevisiae S288C
4 Bap2-mediated leucine import was inhibited by some amino acids according to the following order of severity: phenylalanine, leucine>isoleucine>methionine, tyrosine>valine>tryptophan; histidine and asparagine had no effect. Leucine branched-chain amino acid permease BAP2 Saccharomyces cerevisiae S288C