Identification of a novel d-amino acid aminotransferase involved in d-glutamate biosynthetic pathways in the hyperthermophile Thermotoga maritima

Autor:	Tetsuya Miyamoto, Toshiyuki Moriya, Masumi Katane, Yasuaki Saitoh, Masae Sekine, Kumiko Sakai‐Kato, Tairo Oshima, Hiroshi Homma
Rok vydání:	2022
Předmět:	Aspartic Acid Alanine Glutamine Lysine Alanine Racemase Glutamic Acid Glyoxylates Cell Biology Peptidoglycan Biochemistry Biosynthetic Pathways Homoserine Ketoglutaric Acids Thermotoga maritima Amino Acids Molecular Biology Transaminases
Zdroj:	The FEBS journalReferences. 289(19)
ISSN:	1742-4658
Popis:	The hyperthermophilic bacterium Thermotoga maritima has an atypical peptidoglycan that contains d-lysine alongside the usual d-alanine and d-glutamate. We previously identified a lysine racemase involved in d-lysine biosynthesis, and this enzyme also possesses alanine racemase activity. However, T. maritima has neither alanine racemase nor glutamate racemase enzymes; hence, the precise biosynthetic pathways of d-alanine and d-glutamate remain unclear in T. maritima. In the present study, we identified and characterized a novel d-amino acid aminotransferase (TM0831) in T. maritima. TM0831 exhibited aminotransferase activity towards 23 d-amino acids, but did not display activity towards l-amino acids. It displayed high specific activities towards d-homoserine and d-glutamine as amino donors. The most preferred acceptor was 2-oxoglutarate, followed by glyoxylate. Additionally, TM0831 displayed racemase activity towards four amino acids including aspartate and glutamate. Catalytic efficiency (k
Databáze:	OpenAIRE
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