A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Phosphoserine aminotransferase from Bacillus circulans subsp alkalophilus: Purification, gene cloning and sequencing
Tekijät: Battchikova N, Himanen JP, Ahjolahti M, Korpela T
Kustantaja: ELSEVIER SCIENCE BV
Julkaisuvuosi: 1996
Lehti: Biochimica et Biophysica Acta: Protein Structure and Molecular Enzymology
Tietokannassa oleva lehden nimi: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
Lehden akronyymi: BBA-PROTEIN STRUCT M
Vuosikerta: 1295
Numero: 2
Aloitussivu: 187
Lopetussivu: 194
Sivujen määrä: 8
ISSN: 0167-4838
DOI: https://doi.org/10.1016/0167-4838(96)00039-8
Tiivistelmä
Two peaks of aspartate aminotransferase (AspAT) catalytic activity were observed during DEAE chromatography of a protein extract from alkalophilic B. circulans. The enzyme purified from the major peak appeared to be not aspartate but phosphoserine aminotransferase (PSAT) with a considerably high AspAT side activity. The sequence of the enzyme N-terminus was determined, and the PSAT gene was cloned as two separate fragments. DNA sequencing revealed the open reading frame for the PSAT starting from TTG, putative ribosomal binding site and terminator of transcription. The PSAT gene encodes a protein of 361 amino acids (M(r) 39 793) which shows moderate homology to other known phosphoserine aminotransferases (36-46% of identity, 60-64% of similarity). The PSAT from the alkalophile shares with all of them the consensus sequence pattern around the pyridoxal S-phosphate attachment site.
Two peaks of aspartate aminotransferase (AspAT) catalytic activity were observed during DEAE chromatography of a protein extract from alkalophilic B. circulans. The enzyme purified from the major peak appeared to be not aspartate but phosphoserine aminotransferase (PSAT) with a considerably high AspAT side activity. The sequence of the enzyme N-terminus was determined, and the PSAT gene was cloned as two separate fragments. DNA sequencing revealed the open reading frame for the PSAT starting from TTG, putative ribosomal binding site and terminator of transcription. The PSAT gene encodes a protein of 361 amino acids (M(r) 39 793) which shows moderate homology to other known phosphoserine aminotransferases (36-46% of identity, 60-64% of similarity). The PSAT from the alkalophile shares with all of them the consensus sequence pattern around the pyridoxal S-phosphate attachment site.
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