Cloning, Expression, and Characterization of Aminopeptidase P from the Hyperthermophilic Archaeon Thermococcus sp. Strain NA1

Genomic analysis of a hyperthermophilic archaeon, Thermococcus sp. strain NA1, revealed the presence of a 1,068-bp open reading frame encoding a protein consisting of 356 amino acids with a calculated molecular mass of 39,714 Da (GenBank accession no. DQ144132). Sequence analysis showed that it was...

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Hlavní autoři: Lee, Hyun Sook, Kim, Yun Jae, Bae, Seung Seob, Jeon, Jeong Ho, Lim, Jae Kyu, Jeong, Byeong Chul, Kang, Sung Gyun, Lee, Jung-Hyun
Médium: Artigo
Jazyk:Inglês
Vydáno: American Society for Microbiology 2006
Témata:
Enzymology and Protein Engineering
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC1393192/
https://ncbi.nlm.nih.gov/pubmed/16517635
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/AEM.72.3.1886-1890.2006
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