Tryptophan production by catalysis of a putative tryptophan synthase protein.
Tryptophan Synthase
/ metabolism
Tryptophan
/ metabolism
Escherichia coli
/ genetics
Mutagenesis, Site-Directed
Bacterial Proteins
/ genetics
Sphingomonadaceae
/ enzymology
Recombinant Proteins
/ metabolism
Catalytic Domain
Cloning, Molecular
Hydrogen-Ion Concentration
Indoles
/ metabolism
Catalysis
Serine
/ metabolism
Sphingobacterium
Consensus pattern
Enzyme activity
Essential amino acid
Tryptophan
Tryptophan synthase
Journal
Archives of microbiology
ISSN: 1432-072X
Titre abrégé: Arch Microbiol
Pays: Germany
ID NLM: 0410427
Informations de publication
Date de publication:
02 Sep 2024
02 Sep 2024
Historique:
received:
31
07
2024
accepted:
28
08
2024
revised:
26
08
2024
medline:
2
9
2024
pubmed:
2
9
2024
entrez:
2
9
2024
Statut:
epublish
Résumé
Essential amino acid, tryptophan which intake from food plays a critical role in numerous metabolic functions, exhibiting extensive biological functions and applications. Tryptophan is beneficial for the food sector by enhancing nutritional content and promoting the development of functional foods. A putative gene encoding tryptophan synthase was the first identified in Sphingobacterium soilsilvae Em02, a cellulosic bacterium making it inherently more environmentally friendly. The gene was cloned and expressed in exogenous host Escherichia coli, to elucidate its function. The recombinant tryptophan synthase with a molecular weight 42 KDa was expressed in soluble component. The enzymatic activity to tryptophan synthase in vivo was assessed using indole and L-serine and purified tryptophan synthase. The optimum enzymatic activity for tryptophan synthase was recorded at 50 ºC and pH 7.0, which was improved in the presence of metal ions Mg
Identifiants
pubmed: 39222088
doi: 10.1007/s00203-024-04123-z
pii: 10.1007/s00203-024-04123-z
doi:
Substances chimiques
Tryptophan Synthase
EC 4.2.1.20
Tryptophan
8DUH1N11BX
Bacterial Proteins
0
Recombinant Proteins
0
Indoles
0
indole
8724FJW4M5
Serine
452VLY9402
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
390Subventions
Organisme : National Natural Science Foundation of China
ID : 32070107
Informations de copyright
© 2024. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.
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