Molecular Cloning, Sequencing, and Expression in Escherichia coli of the Gene Encoding a Novel 5-Oxoprolinase without ATP-Hydrolyzing Activity from Alcaligenes faecalis N-38A

The gene encoding a novel 5-oxoprolinase without ATP-hydrolyzing activity from Alcaligenes faecalis N-38A was cloned and characterized. The coding region of this gene is 1,299 bp long. The predicted primary protein is composed of 433 amino acid residues, with a 31-amino-acid signal peptide. The matu...

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Hlavní autoři: Nishimura, Atsuhisa, Oyama, Hiroshi, Hamada, Takatoshi, Nobuoka, Katsunori, Shin, Takashi, Murao, Sawao, Oda, Kohei
Médium: Artigo
Jazyk:Inglês
Vydáno: American Society for Microbiology 2000
Témata:
Enzymology and Protein Engineering
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC92134/
https://ncbi.nlm.nih.gov/pubmed/10919770
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