A newly cloned alginate lyase from Sphingomonas sp. MJ-3 showed exo-type and edo-type alginate degrading activity. Homology-modelled structure of MJ-3 aginate lyase shared low relationship with reported crystal structures. When the multiple sequence and conserved domains were analyzed, interestingly, the cloned gene product was predicted to consist of AlgL (alginate lyase L)-like protein domain and heparinase-like protein domain. AlgL domain in N-terminal and heparinase domain in C-terminal were homology-modeled on 3AFL.pdb and 2FUQ.pdb as templates, respectively. The amino acid residues in proposed active site were mutated and characterized. Acknowledgement : This work was supported by New &Renewable Energy R&D program(20093020090020) and Korea Institute for Advancement in Technology (KIAT) through the Workforce Development Program in Strategic Technology under the Korea Ministry of Knowledge Economy(MKE).
한국생물공학회 [The Korean Society for Biotechnology and Bioengineering]
설립연도
1984
분야
공학>생물공학
소개
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