Acetylornithine aminotransferase TM1785 performs multiple functions in the hyperthermophile Thermotoga maritima.
Thermotoga maritima
acetylornithine aminotransferase
amino acid racemase
cysteine lyase
d-amino acid metabolism
multifunctional enzyme
Journal
FEBS letters
ISSN: 1873-3468
Titre abrégé: FEBS Lett
Pays: England
ID NLM: 0155157
Informations de publication
Date de publication:
12 2021
12 2021
Historique:
revised:
29
10
2021
received:
25
09
2021
accepted:
31
10
2021
pubmed:
9
11
2021
medline:
1
1
2022
entrez:
8
11
2021
Statut:
ppublish
Résumé
The hyperthermophilic bacterium Thermotoga maritima peptidoglycan contains unusual d-lysine alongside typical d-alanine and d-glutamate. We previously identified lysine racemase and threonine dehydratase, but knowledge of d-amino acid metabolism remains limited. Herein, we identified and characterized T. maritima acetylornithine aminotransferase TM1785. The enzyme was most active towards acetyl-l-ornithine, but also utilized l-glutamate, l-ornithine and acetyl-l-lysine as amino donors, and 2-oxoglutarate was the preferred amino acceptor. TM1785 also displayed racemase activity towards four amino acids and lyase activity towards l-cysteine, but no dehydratase activity towards l-serine, l-threonine or corresponding d-amino acids. Catalytic efficiency (k
Identifiants
pubmed: 34747014
doi: 10.1002/1873-3468.14222
doi:
Substances chimiques
Bacterial Proteins
0
Glutamic Acid
3KX376GY7L
Serine
452VLY9402
Ornithine
E524N2IXA3
Transaminases
EC 2.6.1.-
acetylornithine transaminase
EC 2.6.1.11
Cysteine
K848JZ4886
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2931-2941Informations de copyright
© 2021 Federation of European Biochemical Societies.
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