An evolutionary analysis of the GH57 amylopullulanases based on the DOMON_glucodextranase_like domains.

Yu-Liang Jiao, Shu-Jun Wang, Ming-Sheng Lv, Yao-Wei Fang, Shu Liu

Index: J. Basic Microbiol. 53(3) , 231-9, (2013)

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Abstract

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.© 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.