Disease relevance of AK3

• The AK3 cDNA was expressed in Escherichia coli, which resulted in complementation of an adenylate kinase mutation of E. coli [1].

High impact information on AK3

• Three different types of cDNA clones for mitochondrial GTP:AMP phosphotransferase (AK3) were isolated from a cDNA library of bovine liver poly(A)+ RNA [1].
• From comparison of the size of the product synthesized in vitro from the message directed by the isolated cDNA with that of the purified AK3 protein, AK3 appeared to have no cleavable NH2-terminal sequence as found in other mitochondrial proteins [1].
• By Northern blot analysis, three species of AK3 mRNA apparently corresponding to the isolated cDNA clones were detected, which would be a result of varying terminations and polyadenylations of the primary transcript [1].
• Furthermore the diastereomers of guanosine 5'-O-[1-thio]diphosphate (GDP-[alpha S]) have been used to assign Mg2+ coordination to GDP when bound to AK3 [2].
• The amino acid sequence of GTP:AMP phosphotransferase (AK3) from beef-heart mitochondria has been determined, except for one segment of about 33 residues in the middle of the polypeptide chain [3].

Anatomical context of AK3

• Similarly, the diastereomers of guanosine 5'-O-[thio]triphosphate (GTP[alpha S]) and guanosine 5'-O-[2-thio]triphosphate (GTP[beta S]) were utilized to seek unambiguous assignment of Mg2+ coordination to GTP when bound to GTP-AMP phosphotransferase from beef heart mitochondria (AK3) [2].

Other interactions of AK3

• With 30% of all aligned residues being identical, the homology between AK3 and AK1 is well established [3].

References