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 (M(r) 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.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Battchikova N,Koivulehto M,Denesyuk A,Ptitsyn L,Boretsky Y,Hellman J,Korpela Tdoi
10.1093/oxfordjournals.jbchem.a021429subject
Has Abstractpub_date
1996-08-01 00:00:00pages
425-32issue
2eissn
0021-924Xissn
1756-2651journal_volume
120pub_type
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