Structure and polymorphism of the Chironomus thummi gene encoding special lobe-specific silk protein, ssp1601Published in conjunction with A Wisconsin Gathering Honoring Waclaw Szybalski on the occasion of his 75th year and 20 years of Editorship-in-Chief of Gene, 10–11 August 1997, University of Wisconsin, Madison, WI, USA.1

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.

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

Jiao

Wang

et al. 2012

J. Basic Microbiol

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Molecular phylogeny of theChironomus genus deduced from nucleotide sequences of two nuclear genes,ssp 160 and the globin 2b gene

et al. 2000

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Cited by 2 publications

References 26 publications

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

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

Molecular phylogeny of theChironomus genus deduced from nucleotide sequences of two nuclear genes,ssp 160 and the globin 2b gene

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