Characterization of the First Bacterial and Thermostable GDP-Mannose 3,5-Epimerase.
Amino Acid Sequence
Bacterial Proteins
Carbohydrate Epimerases
/ chemistry
Catalysis
Enzyme Activation
Enzyme Stability
Guanosine Diphosphate Mannose
/ chemistry
Hydrogen-Ion Concentration
Models, Molecular
Molecular Structure
Protein Conformation
Recombinant Proteins
Structure-Activity Relationship
Thermodynamics
GDP-mannose 3,5-epimerase
Methylacidiphilum fumariolicum
biocatalysis
l-sugars
recombinant expression
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
19 Jul 2019
19 Jul 2019
Historique:
received:
27
06
2019
revised:
16
07
2019
accepted:
18
07
2019
entrez:
24
7
2019
pubmed:
25
7
2019
medline:
28
12
2019
Statut:
epublish
Résumé
GDP-mannose 3,5-epimerase (GM35E) catalyzes the conversion of GDP-mannose towards GDP-l-galactose and GDP-l-gulose. Although this reaction represents one of the few enzymatic routes towards the production of l-sugars and derivatives, it has not yet been exploited for that purpose. One of the reasons is that so far only GM35Es from plants have been characterized, yielding biocatalysts that are relatively unstable and difficult to express heterologously. Through the mining of sequence databases, we succeeded in identifying a promising bacterial homologue. The gene from the thermophilic organism
Identifiants
pubmed: 31330931
pii: ijms20143530
doi: 10.3390/ijms20143530
pmc: PMC6678494
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Recombinant Proteins
0
Guanosine Diphosphate Mannose
3123-67-9
Carbohydrate Epimerases
EC 5.1.3.-
GDPmannose 3,5-epimerase
EC 5.1.3.18
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Fonds Wetenschappelijk Onderzoek
ID : 1S16817N
Organisme : Fonds Wetenschappelijk Onderzoek
ID : G0F3417N
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