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.
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.
Li
Qiang
Q
School of Life Science, Xiamen University, People's Republic of China.
Wang
Fengping
F
Zhou
Ying
Y
Xiao
Xiang
X
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
D002686:Chitin; D017665:Hydroxyl Radical; D002688:Chitinases