Characterization of xanthine oxidase from Cellulosimicrobium funkei possessing hypoxanthine-metabolizing activity.
Actinobacteria
/ enzymology
Amino Acid Sequence
Bacterial Proteins
DNA, Bacterial
Hypoxanthine
/ metabolism
Oxidation-Reduction
Purines
/ metabolism
Recombinant Proteins
/ metabolism
Rhodococcus
/ genetics
Uric Acid
/ metabolism
Whole Genome Sequencing
Xanthine
/ metabolism
Xanthine Dehydrogenase
/ metabolism
Xanthine Oxidase
/ chemistry
Journal
Journal of applied microbiology
ISSN: 1365-2672
Titre abrégé: J Appl Microbiol
Pays: England
ID NLM: 9706280
Informations de publication
Date de publication:
Jun 2021
Jun 2021
Historique:
revised:
19
09
2020
received:
15
06
2020
accepted:
02
10
2020
pubmed:
23
10
2020
medline:
8
6
2021
entrez:
22
10
2020
Statut:
ppublish
Résumé
Purine-degrading enzymes are favourable as medications and diagnostic tools for hyperuricemia. This study aimed to characterize enzymes isolated from micro-organisms, which may be useful for developing a new prophylaxis for hyperuricemia. Cellulosimicrobium funkei A153 was found to be a good catalyst for hypoxanthine degradation and could oxidize hypoxanthine to xanthine and further to uric acid. The enzyme catalysing this oxidation was purified, and its partial amino acid sequences were examined. Based on this information and genome sequencing results, this xanthine dehydrogenase family protein was cloned and expressed in Rhodococcus erythropolis L88. The recombinant enzyme with a His-tag was characterized. The enzyme was a xanthine oxidase as it could utilize molecular oxygen as an electron acceptor. It was stable under 50°C and exhibited maximum activity at pH 7·0. The k Xanthine oxidase is favourable for hyperuricemia medication because it oxidizes hypoxanthine, an easily adsorbed purine, to xanthine and further to uric acid, which are hardly adsorbed purines. The enzyme is useful for decreasing serum uric acid levels via conversion of easily absorbed purines to hardly absorbed purines in the intestine. Enzymes from micro-organisms may be used as a novel prophylaxis for hyperuricemia.
Substances chimiques
Bacterial Proteins
0
DNA, Bacterial
0
Purines
0
Recombinant Proteins
0
Xanthine
1AVZ07U9S7
Uric Acid
268B43MJ25
Hypoxanthine
2TN51YD919
Xanthine Dehydrogenase
EC 1.17.1.4
Xanthine Oxidase
EC 1.17.3.2
purine
W60KTZ3IZY
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
2132-2140Subventions
Organisme : JSPS KAKENHI
ID : 20K15432
Informations de copyright
© 2020 The Society for Applied Microbiology.
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