Enzymatic characterization of agmatinase (AGM-1) from the filamentous fungus Neurospora crassa.
Agmatinase
Agmatine
Arginase
Fungi
Polyamines
Journal
Fungal genetics and biology : FG & B
ISSN: 1096-0937
Titre abrégé: Fungal Genet Biol
Pays: United States
ID NLM: 9607601
Informations de publication
Date de publication:
12 2021
12 2021
Historique:
received:
30
07
2021
revised:
03
10
2021
accepted:
05
10
2021
pubmed:
12
10
2021
medline:
27
1
2022
entrez:
11
10
2021
Statut:
ppublish
Résumé
Agmatinase is a metallohydrolase involved in the hydrolysis of agmatine to produce urea and putrescine. Although its role in organisms is still under study, there are no reports of this family of enzymes in filamentous fungi. Recently, a protein showing agmatinase activity was reported in Neurospora crassa. Therefore, the aim of this work is to determine if the protein (AGM-1) found in the filamentous fungus N. crassa is a true agmatinase. The protein AGM-1was purified directly from N. crassa cultures, and its enzymatic characterization was carried out. The catalytic parameters such as optimum pH, thermostability, transformation kinetics, and activity in the presence of a cofactor were determined. The results show that AGM-1 can use manganese as a cofactor for its enzymatic activity, showing a transformation rate constant (k
Identifiants
pubmed: 34634482
pii: S1087-1845(21)00118-3
doi: 10.1016/j.fgb.2021.103634
pii:
doi:
Substances chimiques
Agmatine
70J407ZL5Q
Ureohydrolases
EC 3.5.3.-
agmatinase
EC 3.5.3.11
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
103634Informations de copyright
Copyright © 2021 Elsevier Inc. All rights reserved.