Characterization of Two Glycoside Hydrolases of Family GH13 and GH57, Present in a Polysaccharide Utilization Locus (PUL) of
alpha-1,4-transglycosylation
glycogen branching enzyme
glycogen branching enzymes (EC 2.4.1.18)
glycogen synthesis
maltooctadecaose
polysaccharide utilization loci
Journal
Molecules (Basel, Switzerland)
ISSN: 1420-3049
Titre abrégé: Molecules
Pays: Switzerland
ID NLM: 100964009
Informations de publication
Date de publication:
12 Jun 2024
12 Jun 2024
Historique:
received:
23
05
2024
revised:
07
06
2024
accepted:
09
06
2024
medline:
27
6
2024
pubmed:
27
6
2024
entrez:
27
6
2024
Statut:
epublish
Résumé
Glycogen, an α-glucan polymer serving as an energy storage compound in microorganisms, is synthesized through distinct pathways (GlgC-GlgA or GlgE pathway). Both pathways involve multiple enzymes, with a shared glycogen branching enzyme (GBE). GBEs play a pivotal role in establishing α-1,6-linkages within the glycogen structure. GBEs are also used for starch modification. Understanding how these enzymes work is interesting for both glycogen synthesis in microorganisms, as well as novel applications for starch modification. This study focuses on a putative enzyme GH13_9 GBE (PoGBE13), present in a polysaccharide utilization locus (PUL) of
Identifiants
pubmed: 38930854
pii: molecules29122788
doi: 10.3390/molecules29122788
pii:
doi:
Substances chimiques
Glycoside Hydrolases
EC 3.2.1.-
Glycogen
9005-79-2
Polysaccharides
0
1,4-alpha-Glucan Branching Enzyme
EC 2.4.1.18
Starch
9005-25-8
Bacterial Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Dutch Research Council
ID : This research was performed in the public private partnership CarboBased, coordinated by the Carbohydrate Competence Center (CCC) and cofinanced by AVEBE and the "Samenwerkingsverband Noord-Nederland (SNN), Ruimtelijk Economisch Programma".
Pays : Netherlands