| Literature DB >> 24613924 |
Hui Peng1, Yunyun Zheng2, Maojiao Chen2, Ying Wang2, Yazhong Xiao2, Yi Gao2.
Abstract
A novel starch-binding domain (SBD) that represents a new carbohydrate-binding module family (CBM69) was identified in the α-amylase (AmyP) of the recently established alpha-amylase subfamily GH13_37. The SBD and its homologues come mostly from marine bacteria, and phylogenetic analysis indicates that they are closely related to the CBM20 and CBM48 families. The SBD exhibited a binding preference toward raw rice starch, but the truncated mutant (AmyPΔSBD) still retained similar substrate preference. Kinetic analyses revealed that the SBD plays an important role in soluble starch hydrolysis because different catalytic efficiencies have been observed in AmyP and the AmyPΔSBD.Entities:
Keywords: Binding preference; Carbohydrate-binding module; Soluble starch hydrolysis; Starch-binding domain; α-Amylase
Mesh:
Substances:
Year: 2014 PMID: 24613924 DOI: 10.1016/j.febslet.2014.02.050
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124