Substrate binding modes and anomer selectivity of chitinase A from Vibrio harveyi.

ABSTRACT: High-performance liquid chromatography mass spectrometry (HPLC MS) was employed to assess the binding behaviors of various substrates to Vibrio harveyi chitinase A. Quantitative analysis revealed that hexaNAG preferred subsites -2 to +2 over subsites -3 to +2 and pentaNAG only required subsites -2 to +2, while subsites -4 to +2 were not used at all by both substrates. The results suggested that binding of the chitooligosaccharides to the enzyme essentially occurred in compulsory fashion. The symmetrical binding mode (-2 to +2) was favored presumably to allow the natural form of sugars to be utilized effectively. Crystalline alpha chitin was initially hydrolyzed into a diverse ensemble of chitin oligomers, providing a clear sign of random attacks that took place within chitin chains. Howeve

SUBMITTER: Suginta W 

PROVIDER: S-EPMC2763143 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature