Enhancement of L-ribulose Production from L-ribose Through Modification of Ochrobactrum sp. CSL1 Ribose-5-phosphate Isomerase A.
L-ribose
L-ribulose
Ochrobactrum sp. CSL1
Ribose-5-phosphate isomerase A
Journal
Applied biochemistry and biotechnology
ISSN: 1559-0291
Titre abrégé: Appl Biochem Biotechnol
Pays: United States
ID NLM: 8208561
Informations de publication
Date de publication:
Oct 2022
Oct 2022
Historique:
accepted:
27
05
2022
pubmed:
8
6
2022
medline:
24
9
2022
entrez:
7
6
2022
Statut:
ppublish
Résumé
L-ribulose, a kind of high-value rare sugar, could be utilized to manufacture L-form sugars and antiviral drugs, generally produced from L-arabinose as a substrate. However, the production of L-ribulose from L-arabinose is limited by the equilibrium ratio of the catalytic reaction, hence, it is necessary to explore a new biological enzymatic method to produce L-ribulose. Ribose-5-phosphate isomerase (Rpi) is an enzyme that can catalyze the reversible isomerization between L-ribose and L-ribulose, which is of great significance for the preparation of L-ribulose. In order to obtain highly active ribose-5-phosphate isomerase to manufacture L-ribulose, ribose-5-phosphate isomerase A (OsRpiA) from Ochrobactrum sp. CSL1 was engineered based on structural and sequence analyses. Through a rational design strategy, a triple-mutant strain A10T/T32S/G101N with 160% activity was acquired. The enzymatic properties of the mutant were systematically investigated, and the optimum conditions were characterized to achieve the maximum yield of L-ribulose. Kinetic analysis clarified that the A10T/T32S/G101N mutant had a stronger affinity for the substrate and increased catalytic efficiency. Furthermore, molecular dynamics simulations indicated that the binding of the substrate to A10T/T32S/G101N was more stable than that of wild type. The shorter distance between the catalytic residues of A10T/T32S/G101N and L-ribose illuminated the increased activity. Overall, the present study provided a solid basis for demonstrating the complex functions of crucial residues in RpiAs as well as in rare sugar preparation.
Identifiants
pubmed: 35670905
doi: 10.1007/s12010-022-04015-2
pii: 10.1007/s12010-022-04015-2
doi:
Substances chimiques
Antiviral Agents
0
Pentoses
0
ribulose
5556-48-9
Ribose
681HV46001
Arabinose
B40ROO395Z
Aldose-Ketose Isomerases
EC 5.3.1.-
ribosephosphate isomerase
EC 5.3.1.6
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
4852-4866Subventions
Organisme : National Natural Science Foundation of China
ID : 21676173
Organisme : National Natural Science Foundation of China
ID : 32001634
Informations de copyright
© 2022. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.
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