title: Homologous Alkalophilic and Acidophilic L-Arabinose isomerases reveal region-specific contributions to the pH dependence of activity and stability.
abstract: To study the pH dependence of l-arabinose isomerase (AI) activity and stability, we compared homologous AIs with their chimeras. This study demonstrated that an ionizable amino acid near the catalytic site determines the optimal pH (pH(opt)) for activity, whereas the N-terminal surface R residues play an important role in determining the pH(opt) for stability.
authors.affiliation: Division of Applied Biology and Chemistry, Kyungpook National University, Daegu, South Korea. leehicam@knu.ac.kr
authors.forename: Sang-Jae
authors.initials: SJ
authors.lastname: Lee
authors.forename: Sang Jun
authors.initials: SJ
authors.lastname: Lee
authors.forename: Yong-Jik
authors.initials: YJ
authors.lastname: Lee
authors.forename: Seong-Bo
authors.initials: SB
authors.lastname: Kim
authors.forename: Sung-Kun
authors.initials: SK
authors.lastname: Kim
authors.forename: Dong-Woo
authors.initials: DW
authors.lastname: Lee
mesh_terms: D019747:Aldose-Ketose Isomerases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D056450:Alicyclobacillus / Q000201:enzymology / Q000235:genetics; D000596:Amino Acids / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D020134:Catalytic Domain; D004269:DNA, Bacterial / Q000737:chemistry / Q000235:genetics; D004275:DNA, Ribosomal / Q000737:chemistry / Q000235:genetics; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D055550:Protein Stability; D012336:RNA, Ribosomal, 16S / Q000235:genetics; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid
chemical_list: D000596:Amino Acids; D004269:DNA, Bacterial; D004275:DNA, Ribosomal; D012336:RNA, Ribosomal, 16S; D019747:Aldose-Ketose Isomerases; C019715:L-arabinose isomerase