Please use this identifier to cite or link to this item: https://repository.ldufk.edu.ua/handle/34606048/10380
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dc.contributor.authorBattchikova, Natalia
dc.contributor.authorKoivulehto, Marianne
dc.contributor.authorDenesyuk, Alexander
dc.contributor.authorPtitsyn, Leonid
dc.contributor.authorBoretsky, Yuriy
dc.contributor.authorHellman, Jukka
dc.contributor.authorKorpela, Timo
dc.contributor.authorБорецький, Юрій
dc.date.accessioned2018-05-10T19:30:27Z-
dc.date.available2018-05-10T19:30:27Z-
dc.date.issued1996
dc.identifier.citationAspartate 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)uk_UA
dc.identifier.urihttp://repository.ldufk.edu.ua/handle/34606048/10380-
dc.description.abstractAspartate 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.uk_UA
dc.language.isoenuk_UA
dc.subjectAspartate aminotransferaseuk_UA
dc.subjectalkalophileuk_UA
dc.subjectBacillus circulansuk_UA
dc.subjectcloninguk_UA
dc.titleAspartate aminotransferase from an alkalophilic Bacillus contains an additional 20 - amino acid extension at its fu nctionally i mportant N - terminusuk_UA
dc.typeArticleuk_UA
Appears in Collections:Наукові праці професорсько-викладацького складу ЛДУФК в базах даних Scopus, WoS, Tomson Reuters

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