Mechanistic characterization of UDP-glucuronic acid 4-epimerase.
Bacillus cereus
/ enzymology
Bacterial Proteins
/ genetics
Biocatalysis
Carbohydrate Sequence
Catalytic Domain
Chromatography, High Pressure Liquid
Escherichia coli
/ genetics
Hydrogen-Ion Concentration
Kinetics
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Mutant Proteins
/ metabolism
Mutation
Racemases and Epimerases
/ genetics
Recombinant Proteins
/ genetics
Uridine Diphosphate Sugars
/ chemistry
UDP-glucuronic acid
decarboxylase
epimerase
kinetic isotope effect
short-chain dehydrogenase/reductase
Journal
The FEBS journal
ISSN: 1742-4658
Titre abrégé: FEBS J
Pays: England
ID NLM: 101229646
Informations de publication
Date de publication:
02 2021
02 2021
Historique:
received:
06
03
2020
revised:
22
06
2020
accepted:
06
07
2020
pubmed:
10
7
2020
medline:
27
7
2021
entrez:
10
7
2020
Statut:
ppublish
Résumé
UDP-glucuronic acid (UDP-GlcA) is a central precursor in sugar nucleotide biosynthesis and common substrate for C4-epimerases and decarboxylases releasing UDP-galacturonic acid (UDP-GalA) and UDP-pentose products, respectively. Despite the different reactions catalyzed, the enzymes are believed to share mechanistic analogy rooted in their joint membership to the short-chain dehydrogenase/reductase (SDR) protein superfamily: Oxidation at the substrate C4 by enzyme-bound NAD
Identifiants
pubmed: 32645249
doi: 10.1111/febs.15478
pmc: PMC7984243
doi:
Substances chimiques
Bacterial Proteins
0
Mutant Proteins
0
Recombinant Proteins
0
Uridine Diphosphate Sugars
0
UDP-galacturonic acid
50722-58-2
Racemases and Epimerases
EC 5.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1163-1178Informations de copyright
© 2020 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
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