Key amino acid residues govern the substrate selectivity of the transporter Xltr1p from Trichoderma reesei for glucose, mannose, and galactose.

ABSTRACT: This research identified four amino acid residues (Leu174, Asn297, Tyr301, and Gln291) that contribute to substrate recognition by the high-affinity glucose transporter Xltr1p from Trichoderma reesei. Potential hotspots affecting substrate specificity were selected through homology modeling, evolutionary conservation analyses, and substrate-docking modeling of Xltr1p. Variants carrying mutations at these hotspots were subsequently obtained via in silico screening. Replacement of Leu174 or Asn297 in Xltr1p with alanine resulted in loss of hexose transport activity, indicating that Leu174 and Asn297 play essential roles in hexose transport. The Y301W variant exhibited accelerated mannose transport, but lost galactose transport capacity, and mutation of Gln291 to alanine greatly accele

SUBMITTER: Ma W 

PROVIDER: S-EPMC11611029 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature