caa a22 4500 397556667 CHVBK 20180308164804.0 cr unu---uuuuu 161202e199608 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021429 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021429 Aspartate Aminotransferase from an Alkalophilic Bacilus Contains an Additional 20-Amino Acid Extension at Its Functionally Important N-Terminus [Elektronische Daten] [Natalia Battchikova, Marianne Koivulehto, Alexander Denesyuk, Leonid Ptitsyn, Yuri Boretsky, Jukka Hellman, Timo Korpela] 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. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence aspartate aminotransferase nationallicence alkalophile nationallicence Bacillus circulans nationallicence cloning nationallicence protein sequence analysis nationallicence Battchikova Natalia Finnish-Russian Joint Biotechnology Laboratory, University of Turku BioCity 6A, FIN-20620 Turku, Finland aut Koivulehto Marianne Finnish-Russian Joint Biotechnology Laboratory, University of Turku BioCity 6A, FIN-20620 Turku, Finland aut Denesyuk Alexander Finnish-Russian Joint Biotechnology Laboratory, University of Turku BioCity 6A, FIN-20620 Turku, Finland aut Ptitsyn Leonid Institute of Biotechnology Nauchny pr. 8, Moscow 117246, Russia aut Boretsky Yuri Institute of Biotechnology Nauchny pr. 8, Moscow 117246, Russia aut Hellman Jukka Centre for Biotechology, University of Turku BioCity 5B, FIN-20520 Turku, Finland aut Korpela Timo Finnish-Russian Joint Biotechnology Laboratory, University of Turku BioCity 6A, FIN-20620 Turku, Finland aut The Journal of Biochemistry Oxford University Press 120/2(1996-08), 425-432 0021-924X 120:2<425 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021429 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021429 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Battchikova Natalia Finnish-Russian Joint Biotechnology Laboratory, University of Turku BioCity 6A, FIN-20620 Turku, Finland aut NATIONALLICENCE 700 1- Koivulehto Marianne Finnish-Russian Joint Biotechnology Laboratory, University of Turku BioCity 6A, FIN-20620 Turku, Finland aut NATIONALLICENCE 700 1- Denesyuk Alexander Finnish-Russian Joint Biotechnology Laboratory, University of Turku BioCity 6A, FIN-20620 Turku, Finland aut NATIONALLICENCE 700 1- Ptitsyn Leonid Institute of Biotechnology Nauchny pr. 8, Moscow 117246, Russia aut NATIONALLICENCE 700 1- Boretsky Yuri Institute of Biotechnology Nauchny pr. 8, Moscow 117246, Russia aut NATIONALLICENCE 700 1- Hellman Jukka Centre for Biotechology, University of Turku BioCity 5B, FIN-20520 Turku, Finland aut NATIONALLICENCE 700 1- Korpela Timo Finnish-Russian Joint Biotechnology Laboratory, University of Turku BioCity 6A, FIN-20620 Turku, Finland aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/2(1996-08), 425-432 0021-924X 120:2<425 1996 120 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford