Premium
An evolutionary analysis of the GH57 amylopullulanases based on the DOMON_glucodextranase_like domains
Author(s) -
Jiao YuLiang,
Wang ShuJun,
Lv MingSheng,
Fang YaoWei,
Liu Shu
Publication year - 2013
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.201100530
Subject(s) - phylogenetic tree , pullulanase , glycoside hydrolase , hydrolysis , starch , gene duplication , biology , phylogenetic relationship , genetics , biochemistry , gene , chemistry
Thermostable amylopullulanase (TAPU) is valuable in starch saccharification industry for its capability to catalyze both α‐1,4 and α‐1,6 glucosidic bonds under the industrial starch liquefication condition. The majority of TAPUs belong to glycoside hydrolase family 57 (GH57). In this study, we performed a phylogenetic analysis of GH57 amylopullulanase (APU) based on the highly conserved DOMON_glucodextranase_like (DDL) domain and classified APUs according to their multidomain architectures, phylogenetic analysis and enzymatic characters. This study revealed that amylopullulanase, pullulanase, andα‐amylase had passed through a long joint evolution process, in which DDL played an important role. The phylogenetic analysis of DDL domain showed that the GH57 APU is directly sharing a common ancestor with pullulanase, and the DDL domains in some species undergo evolution scenarios such as domain duplication and recombination.