Cloning, expression, and characterization of aminopeptidase P from the hyperthermophilic archaeon Thermococcus sp. strain NA1.
作者： Hyun Sook Lee , Yun Jae Kim , Seung Seob Bae , Jeong Ho Jeon , Jae Kyu Lim
DOI: 10.1128/AEM.72.3.1886-1890.2006
关键词:
摘要: Genomic analysis of a hyperthermophilic archaeon, Thermococcus sp. strain NA1, revealed the presence 1,068-bp open reading frame encoding protein consisting 356 amino acids with calculated molecular mass 39,714 Da (GenBank accession no. DQ144132). Sequence showed that it was similar to putative aminopeptidase P (APP) kodakaraensis KOD1. Amino acid residues important for catalytic activity and metal binding ligands conserved in bacterial, nematode, insect, mammalian APPs were also NA1 APP. The archaeal APP, designated TNA1_APP (Thermococcus APP), cloned expressed Escherichia coli. recombinant enzyme hydrolyzed amino-terminal Xaa-Pro bond Lys(Nepsilon-Abz)-Pro-Pro-pNA dipeptide Met-Pro (Km, 0.96 mM), revealing its functional identity. Further characterization be Co2+-, Mn2+-, or Zn2+-dependent metallopeptidase. Optimal APP as substrate occurred at pH 5 temperature 100 degrees C. thermostable, half-life >100 min 80 This study represents first archaeon
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