Structure-function analyses reveal that a glucuronoyl esterase from
CE15
biotechnology
carbohydrate
carbohydrate esterase
carbohydrate-active enzymes
enzyme kinetics
enzyme mechanism
enzyme mutation
enzyme structure
glucuronoyl esterase
lignin-carbohydrate complexes
plant cell wall
protein structure
uronic acid
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
19 04 2019
19 04 2019
Historique:
received:
30
01
2019
revised:
20
02
2019
pubmed:
1
3
2019
medline:
17
10
2019
entrez:
1
3
2019
Statut:
ppublish
Résumé
Glucuronoyl esterases (GEs) catalyze the cleavage of ester linkages found between lignin and glucuronic acid moieties on glucuronoxylan in plant biomass. As such, GEs represent promising biochemical tools in industrial processing of these recalcitrant resources. However, details on how GEs interact with their natural substrates are sparse, calling for thorough structure-function studies. Presented here is the structure and biochemical characterization of a GE,
Identifiants
pubmed: 30814248
pii: S0021-9258(20)36316-X
doi: 10.1074/jbc.RA119.007831
pmc: PMC6484129
doi:
Substances chimiques
Bacterial Proteins
0
Carbohydrates
0
Hydrocarbons, Aromatic
0
Uronic Acids
0
Esterases
EC 3.1.-
Banques de données
PDB
['6hsw', '4g4j', '6ehn', '6gs0', '4g4g']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
6635-6644Informations de copyright
© 2019 Arnling Bååth et al.
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