An evolutionary analysis of the GH57 amylopullulanases based on the DOMON_glucodextranase_like domains. (26th June 2012)

• Record Type: Journal Article
• Authors: Jiao, Yu‐Liang; Wang, Shu‐Jun; Lv, Ming‐Sheng; Fang, Yao‐Wei; Liu, Shu
• Is Part Of: Journal of basic microbiology. Volume 53:issue 3(2013:Mar.)
• Page Start: 231
• Page End: 239
• Publication Date: 2012-06-26
• Subjects: Microbiology -- Periodicals; 579
• DOI: 10.1002/jobm.201100530
• Languages: English
• ISSNs: 0233-111X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <sec id="jobm201100530-sec-0001" sec-type="section"> <p>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.</p> </sec> </abstract>