New Insights into the Determinants of Specificity in Human Type I Arginase: Generation of a Mutant That Is Only Active with Agmatine as Substrate.
agmatine
arginase
arginine
determinants of specificity
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
09 Jun 2022
09 Jun 2022
Historique:
received:
28
04
2022
revised:
25
05
2022
accepted:
04
06
2022
entrez:
24
6
2022
pubmed:
25
6
2022
medline:
28
6
2022
Statut:
epublish
Résumé
Arginase catalyzes the hydrolysis of L-arginine into L-ornithine and urea. This enzyme has several analogies with agmatinase, which catalyzes the hydrolysis of agmatine into putrescine and urea. However, this contrasts with the highlighted specificity that each one presents for their respective substrate. A comparison of available crystal structures for arginases reveals an important difference in the extension of two loops located in the entrance of the active site. The first, denominated
Identifiants
pubmed: 35742891
pii: ijms23126438
doi: 10.3390/ijms23126438
pmc: PMC9224512
pii:
doi:
Substances chimiques
Agmatine
70J407ZL5Q
Urea
8W8T17847W
Arginine
94ZLA3W45F
Ornithine
E524N2IXA3
Arginase
EC 3.5.3.1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : University of Concepción
ID : VRID-Enlace 217.037.022-1
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