In silico studies on the substrate specificity of an l-arabinose isomerase from Bacillus licheniformis.
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.
Prabhu
Ponnandy
P
Department of Bioscience and Biotechnology, Konkuk University, Gwangjin-Gu, Seoul 143-701, Republic of Korea.
Jeya
Marimuthu
M
Lee
Jung-Kul
JK
D019747:Aldose-Ketose Isomerases / Q000378:metabolism*; D001407:Bacillus / Q000201:enzymology*; D001665:Binding Sites; D020134:Catalytic Domain; D003198:Computer Simulation; D007700:Kinetics; D013379:Substrate Specificity
D019747:Aldose-Ketose Isomerases; C019715:L-arabinose isomerase