Assessment of structural behaviour of a new L-asparaginase and SAXS data-based evidence for catalytic activity in its monomeric form.
L-Asparaginase
Molecular docking
Monomer
Pseudomonas resinovorans
SAXS
Journal
International journal of biological macromolecules
ISSN: 1879-0003
Titre abrégé: Int J Biol Macromol
Pays: Netherlands
ID NLM: 7909578
Informations de publication
Date de publication:
31 Dec 2023
31 Dec 2023
Historique:
received:
12
05
2023
revised:
30
08
2023
accepted:
06
09
2023
medline:
27
11
2023
pubmed:
10
9
2023
entrez:
9
9
2023
Statut:
ppublish
Résumé
The present study reports the structural and functional characterization of a new glutaminase-free recombinant L-asparaginase (PrASNase) from Pseudomonas resinovorans IGS-131. PrASNase showed substrate specificity to L-asparagine, and its kinetic parameters, K
Identifiants
pubmed: 37689286
pii: S0141-8130(23)03700-5
doi: 10.1016/j.ijbiomac.2023.126803
pii:
doi:
Substances chimiques
Asparaginase
EC 3.5.1.1
Asparagine
7006-34-0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
126803Informations de copyright
Copyright © 2023. Published by Elsevier B.V.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors have declared that they have no conflict of interest related to this work.