An evolutionary analysis of the GH57 amylopullulanases based on the DOMON_glucodextranase_like domains.
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.
College of Marine Sciences, HuaiHai Institute of Technology, Lianyungang, People's Republic of China.
Yu-Liang
YL
Jiao
Shu-Jun
SJ
Wang
Ming-Sheng
MS
Lv
Yao-Wei
YW
Fang
Shu
S
Liu
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics*; D019143:Evolution, Molecular; D005959:Glucosidases / Q000737:chemistry* / Q000235:genetics; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D007218:Industrial Microbiology; D010802:Phylogeny; D017434:Protein Structure, Tertiary / Q000235:genetics*; D019711:Pyrococcus / Q000201:enzymology* / Q000235:genetics; D011995:Recombination, Genetic; D013213:Starch / Q000378:metabolism; D019712:Thermococcus / Q000201:enzymology* / Q000235:genetics
D001426:Bacterial Proteins; D013213:Starch; D005959:Glucosidases; D006026:Glycoside Hydrolases; C082507:amylopullulanase; C100181:pullulanase; C023149:exo-1,6-alpha-glucosidase