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X‐ray structure of Arthrobacter globiformis M30 ketose 3‐epimerase for the production of d ‐allulose from d ‐fructose
Author(s) -
Yoshida Hiromi,
Yoshihara Akihide,
Gullapalli Pushpa Kiran,
Ohtani Kouhei,
Akimitsu Kazuya,
Izumori Ken,
Kamitori Shigehiro
Publication year - 2018
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x18011706
Subject(s) - ketose , chemistry , fructose , biochemistry , stereochemistry , aldose , glycoside
The X‐ray structure of ketose 3‐epimerase from Arthrobacter globiformis M30, which was previously reported to be a d ‐allulose 3‐epimerase (AgD‐AE), was determined at 1.96 Å resolution. The crystal belonged to the hexagonal space group P 6 5 22, with unit‐cell parameters a = b = 103.98, c = 256.53 Å. The structure was solved by molecular replacement using the structure of Mesorhizobium loti l ‐ribulose 3‐epimerase (MlL‐RE), which has 41% sequence identity, as a search model. A hexagonal crystal contained two molecules in the asymmetric unit, and AgD‐AE formed a homotetramer with twofold symmetry. The overall structure of AgD‐AE was more similar to that of MlL‐RE than to the known structures of d ‐psicose (alternative name d ‐allulose) 3‐epimerases ( d ‐PEs or d ‐AEs), although AgD‐AE and MlL‐RE have different substrate specificities. Both AgD‐AE and MlL‐RE have long helices in the C‐terminal region that would contribute to the stability of the homotetramer. AgD‐AE showed higher enzymatic activity for l ‐ribulose than d ‐allulose; however, AgD‐AE is stable and is a unique useful enzyme for the production of d ‐allulose from d ‐fructose.