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Title: Aspartate aminotransferase from an alkalophilic Bacillus contains an additional 20 - amino acid extension at its fu nctionally i mportant N - terminus
Authors: Battchikova, Natalia
Koivulehto, Marianne
Denesyuk, Alexander
Ptitsyn, Leonid
Boretsky, Yuriy
Hellman, Jukka
Korpela, Timo
Борецький, Юрій
Keywords: Aspartate aminotransferase
Bacillus circulans
Issue Date: 1996
Citation: Aspartate aminotransferase from an alkalophilic Bacillus contains an additional 20 - amino acid extension at its functionally i mportant N - terminus / Battchikova N ., Koivulehto M ., Denesyuk A., Ptitsyn L ., Boretsky Y ., Hellman J ., Korpela T. // J Biochem. – 1996. – Vol. 120(2) . – P. 425 – 432. (Scopus)
Abstract: Aspartate aminotransferase (AspAT), responsible for a minor part of the total AspAT enzymic activity in alkalophilic Bacillus circulans, was purified, its N-terminal amino acid sequence was determined, and its gene was cloned as two separate fragments. DNA sequencing showed an open reading frame of 432 amino acids (Mr 47,439) exhibiting moderately low homology with AspATs from other sources. Sequence alignment of the enzyme with chicken mitochondrial, chicken cytoplasmic and Escherichia coli AspATs was performed with the MULTALIN program and further optimized assuming that the three-dimensional structures of the proteins were conserved. The primary structure of the studied AspAT diverged markedly from the others in the catalytically important small domain and in a segment of 31 amino acids in the large domain. The functional N-terminal arm was about two times longer than those of AspATs from other sources. According to the molecular model, the unique regions of B. circulans AspAT are all located together, forming a continuous network of contacts. Additional contacts formed by the elongated N-terminal arm may result in some limitation of domain movements in the alkalophilic enzyme in comparison to in other known AspATs.
Appears in Collections:Наукові праці професорсько-викладацького складу ЛДУФК в базах даних Scopus, WoS, Tomson Reuters

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