An evolutionary analysis of the GH57 amylopullulanases based on the DOMON_glucodextranase_like domains.
J Basic Microbiol
; 53(3): 231-9, 2013 Mar.
Article
em En
| MEDLINE
| ID: mdl-22733591
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.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Filogenia
/
Proteínas de Bactérias
/
Estrutura Terciária de Proteína
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Evolução Molecular
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Pyrococcus
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Thermococcus
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Glucosidases
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Glicosídeo Hidrolases
Idioma:
En
Revista:
J Basic Microbiol
Assunto da revista:
MICROBIOLOGIA
Ano de publicação:
2013
Tipo de documento:
Article