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Parallel β/α‐barrels of α‐amylase, cyclodextrin glycosyltransferase and oligo‐1,6‐glucosidase versus the barrel of β‐amylase: Evolutionary distance is a reflection of unrelated sequences
Author(s) -
Janeček Štefan
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01019-6
Subject(s) - amylase , barrel (horology) , enzyme , starch , cyclodextrin , biochemistry , glycosyltransferase , chemistry , monomer , materials science , organic chemistry , polymer , composite material
The structures of functionally related β/α‐barrel starch hydrolases, α‐amylase, β‐amylase, cyclodextrin glycosyltransferase and oligo‐1,6‐glucosidase, are discussed, their mutual sequence similarities being emphasized. Since these enzymes (except for β‐amylase) along with the predicted set of more than ten β/α‐barrels from the α‐amylase enzyme superfamily fulfil the criteria characteristic of the products of divergent evolution, their unrooted distance tree is presented.