title: In silico studies on the substrate specificity of an l-arabinose isomerase from Bacillus licheniformis.
abstract: l-Arabinose isomerase (BLAI) from Bacillus licheniformis was found to be active only with l-arabinose, unlike other l-arabinose isomerases (l-AIs) active with a variety of aldoses. Therefore, the differences in molecular interactions and substrate orientation in the active site of l-AIs have been examined and the residue at position 346 is proposed to be responsible for the unique substrate specificity of BLAI.
authors.affiliation: Department of Bioscience and Biotechnology, Konkuk University, Gwangjin-Gu, Seoul 143-701, Republic of Korea.
authors.forename: Ponnandy
authors.initials: P
authors.lastname: Prabhu
authors.forename: Marimuthu
authors.initials: M
authors.lastname: Jeya
authors.forename: Jung-Kul
authors.initials: JK
authors.lastname: Lee
mesh_terms: D019747:Aldose-Ketose Isomerases / Q000378:metabolism*; D001407:Bacillus / Q000201:enzymology*; D001665:Binding Sites; D020134:Catalytic Domain; D003198:Computer Simulation; D007700:Kinetics; D013379:Substrate Specificity
chemical_list: D019747:Aldose-Ketose Isomerases; C019715:L-arabinose isomerase