A Thermostable Aspartate Aminotransferase from Aeropyrum pernix K1
نویسندگان
چکیده
منابع مشابه
Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1.
An O-acetylserine sulfhydrylase (OASS) from the hyperthermophilic archaeon Aeropyrum pernix K1, which shares the pyridoxal 5'-phosphate binding motif with both OASS and cystathionine beta-synthase (CBS), was cloned and expressed by using Escherichia coli Rosetta(DE3). The purified protein was a dimer and contained pyridoxal 5'-phosphate. It was shown to be an enzyme with CBS activity as well as...
متن کاملCharacterization of novel hexadecameric thioredoxin peroxidase from Aeropyrum pernix K1.
A gene (APE2278) encoding the peroxiredoxin (Prx) homologous protein of yeast and human was identified in the genome data base of the aerobic hyperthermophilic archaeon Aeropyrum pernix. We cloned the gene and produced the encoded protein in Escherichia coli cells. The isolated recombinant protein showed peroxidase activity in vitro and used the thioredoxin system of A. pernix as an electron do...
متن کاملI-ApeI, a novel intron-encoded LAGLIDADG homing endonuclease from the archaeon, Aeropyrum pernix K1
Over 50 introns have been reported in archaeal rRNA genes (rDNAs), a subset of which nests putative homing endonuclease (HEase) genes. Here, we report the identification and characterization of a novel archaeal LAGLIDADG-type HEase, I-ApeKI [corrected], encoded by the ApeK1.S908 intron within the 16S rDNA of Aeropyrum pernix K1. I-ApeKI [corrected] consists of 222 amino acids and harbors two LA...
متن کاملExpression, purification and crystal structure of a truncated acylpeptide hydrolase from Aeropyrum pernix K1.
Acylpeptide hydrolase (APH) catalyzes the N-terminal hydrolysis of Nalpha-acylpeptides to release Nalpha-acylated amino acids. The crystal structure of recombinant APH from the thermophilic archaeon Aeropyrum pernix K1 (apAPH) was reported recently to be at a resolution of 2.1 Angstrom; using X-ray diffraction. A truncated mutant of apAPH that lacks the first short alpha-helix at the N-terminal...
متن کاملEnzymatic Degradation of PrPSc by a Protease Secreted from Aeropyrum pernix K1
BACKGROUND An R30 fraction from the growth medium of Aeropyrum pernix was analyzed for the protease that can digest the pathological prion protein isoform (PrP(Sc)) from different species (human, bovine, deer and mouse). METHODOLOGY/PRINCIPAL FINDINGS Degradation of the PrP(Sc) isoform by the R30 fraction and the purified protease was evaluated using the 6H4 anti-PrP monoclonal antibody. Frag...
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ژورنال
عنوان ژورنال: Bulletin of the Korean Chemical Society
سال: 2009
ISSN: 0253-2964
DOI: 10.5012/bkcs.2009.30.12.3143