Sequence-structural features and evolutionary relationships of family GH57 α-amylases and their putative α-amylase-like homologues
about
Structural features underlying the selective cleavage of a novel exo-type maltose-forming amylase from Pyrococcus sp. ST04Aspergillus Oryzae S2 α-Amylase Domain C Involvement in Activity and Specificity: In Vivo Proteolysis, Molecular and Docking StudiesAnalysis on evolutionary relationship of amylases from archaea, bacteria and eukaryotaGlobal analysis of viral infection in an archaeal model systemUnique carbohydrate binding platforms employed by the glucan phosphatases.α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.Glycosynthesis in a waterworld: new insight into the molecular basis of transglycosylation in retaining glycoside hydrolases.Structure and function of α-glucan debranching enzymes.Remarkable evolutionary relatedness among the enzymes and proteins from the α-amylase family.Close relationship of a novel Flavobacteriaceae α-amylase with archaeal α-amylases and good potentials for industrial applications.In silico identification of catalytic residues and domain fold of the family GH119 sharing the catalytic machinery with the α-amylase family GH57.Evolutionary history of eukaryotic α-glucosidases from the α-amylase family.Sequence fingerprints of enzyme specificities from the glycoside hydrolase family GH57.An extremely thermostable amylopullulanase from Staphylothermus marinus displays both pullulan- and cyclodextrin-degrading activities.An evolutionary analysis of the GH57 amylopullulanases based on the DOMON_glucodextranase_like domains.Maltose-forming α-amylase from the hyperthermophilic archaeon Pyrococcus sp. ST04.In silico analysis of the α-amylase family GH57: eventual subfamilies reflecting enzyme specificities.
P2860
Q27690698-70A14C50-5684-4E38-A968-12F3EE9F9EC6Q35996113-B82C17D6-E103-46A2-ABF8-CDC0A2774B87Q36445939-AC95C1FE-308A-44A3-A0A2-F45CB069BCA2Q36456100-BC4DD510-56C4-4592-9485-D4121CEE7211Q37037323-5F3DB636-51B3-4053-964D-F4C0568751F2Q38117539-430AEB5C-ACC4-43D6-8D40-06D608EA2D9DQ38385154-7B376C83-C6A7-43AE-AAC4-1F84996D6CBEQ38823309-B4A03CCE-43B0-4B36-8669-881918A95672Q38827804-46C5A225-1640-4B00-A343-71ED45A7A7A9Q41949796-CFAD34B2-6407-43D1-A292-AD8ECB0155FCQ42660043-F3B8B996-B59E-4935-AA8F-E4F0EE0809FFQ42989083-48A328D7-984D-42E4-924C-A673517B3A88Q43015165-45937FFF-67DD-4313-A19E-B0BE2CA8658EQ44345445-F23B9CDA-D86D-4D96-8F34-BE3771916B42Q45025044-9F8FB962-5F94-4B88-899C-8A9F03675C0FQ46874853-F8023F25-3BBD-4F20-BD6C-D1B190DA2033Q55717987-E9757AE0-571C-4B1D-91FF-E63418A4EF5B
P2860
Sequence-structural features and evolutionary relationships of family GH57 α-amylases and their putative α-amylase-like homologues
description
wetenschappelijk artikel (gepubliceerd in 2011-08)
@nl
наукова стаття, опублікована в серпні 2011
@uk
name
Sequence-structural features a ...... tive α-amylase-like homologues
@en
Sequence-structural features a ...... tive α-amylase-like homologues
@nl
type
label
Sequence-structural features a ...... tive α-amylase-like homologues
@en
Sequence-structural features a ...... tive α-amylase-like homologues
@nl
prefLabel
Sequence-structural features a ...... tive α-amylase-like homologues
@en
Sequence-structural features a ...... tive α-amylase-like homologues
@nl
P2860
P1433
P1476
Sequence-structural features a ...... tive α-amylase-like homologues
@en
P2093
Karol Blesák
Stefan Janeček
P2860
P2888
P304
P356
10.1007/S10930-011-9348-7
P407
P577
2011-08-01T00:00:00Z