Aspergillus nidulans thermostable arginine deiminase-Dextran conjugates with enhanced molecular stability, proteolytic resistance, pharmacokinetic properties and anticancer activity.
Animals
Antineoplastic Agents
/ chemistry
Arginine
/ metabolism
Aspergillus nidulans
/ enzymology
Cell Line, Tumor
Cell Proliferation
Citrulline
/ metabolism
Dextrans
/ metabolism
Enzyme Stability
Humans
Hydrogen-Ion Concentration
Hydrolases
/ chemistry
Kinetics
Mice
Molecular Weight
Protein Multimerization
Proteolysis
Temperature
Anticancer activity
Aspergillus nidulans
Dextran conjugation
Pharmacokinetics
Thermostable arginine deiminase
Journal
Enzyme and microbial technology
ISSN: 1879-0909
Titre abrégé: Enzyme Microb Technol
Pays: United States
ID NLM: 8003761
Informations de publication
Date de publication:
Dec 2019
Dec 2019
Historique:
received:
17
03
2019
revised:
11
09
2019
accepted:
17
09
2019
entrez:
17
10
2019
pubmed:
17
10
2019
medline:
6
2
2020
Statut:
ppublish
Résumé
The potential anticancer activity of arginine deiminase (ADI) via deimination of l-arginine into citrulline has been extensively verified against various arginine-auxotrophic tumors, however, the higher antigenicity, structural instability and in vivo proteolysis are the major challenges that limit this enzyme from further clinical implementation. Since, this clinically applied enzyme was derived from Mycobacterium spp, thus, searching for ADI from eukaryotic microbes "especially thermophilic fungi" could have a novel biochemical, conformational and catalytic properties. Aspergillus nidulans ADI was purified with 5.3 folds, with molecular subunit structure 48 kDa and entire molecular mass 120 kDa, ensuring its homotrimeric identity. The peptide fingerprinting analysis revealing the domain Glu
Identifiants
pubmed: 31615671
pii: S0141-0229(19)30170-X
doi: 10.1016/j.enzmictec.2019.109432
pii:
doi:
Substances chimiques
Antineoplastic Agents
0
Dextrans
0
Citrulline
29VT07BGDA
Arginine
94ZLA3W45F
Hydrolases
EC 3.-
arginine deiminase
EC 3.5.3.6
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
109432Informations de copyright
Copyright © 2019 Elsevier Inc. All rights reserved.