title: Putative exposed aromatic and hydroxyl residues on the surface of the N-terminal domains of Chi1 from Aeromonas caviae CB101 are essential for chitin binding and hydrolysis.
abstract: Chitinase Chi1 of Aeromonas caviae CB101 possesses chitin binding sites at both its N and C termini. Four putative exposed residues aligned in a line on the surface of the N-terminal domains of Chi1 were found to contribute to the enzyme-chitin binding and hydrolysis via site-directed mutagenesis. Also, it was found that Chi1 requires the cooperation of the N- and C-terminal domains to bind fully with crystalline and colloidal chitin.
authors.affiliation: School of Life Science, Xiamen University, People's Republic of China.
authors.forename: Qiang
authors.initials: Q
authors.lastname: Li
authors.forename: Fengping
authors.initials: F
authors.lastname: Wang
authors.forename: Ying
authors.initials: Y
authors.lastname: Zhou
authors.forename: Xiang
authors.initials: X
authors.lastname: Xiao
mesh_terms: D000333:Aeromonas / Q000201:enzymology* / Q000235:genetics; D002686:Chitin / Q000378:metabolism*; D002688:Chitinases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006868:Hydrolysis; D017665:Hydroxyl Radical; D016297:Mutagenesis, Site-Directed; D013329:Structure-Activity Relationship
chemical_list: D002686:Chitin; D017665:Hydroxyl Radical; D002688:Chitinases