In vitro association with peroxisomes and conformational change of peroxisomal serine:pyruvate/alanine:glyoxylate aminotransferase in rat and human livers.
To understand the targeting mechanisms of peroxisomal serine:pyruvate aminotransferase, in vitro import experiments were carried out using this 43 kDa peroxisomal enzyme, which was synthesized in a coupled transcription/translation system. Being different from other peroxisomal enzymes, such as acyl-CoA oxidase and urate oxidase used in previous in vitro import experiment, the soluble form of peroxisomal serine:pyruvate aminotransferase was fairly resistant to proteinase K digestion. However, the enzyme recovered in the peroxisomal fraction was proteinase K sensitive. This indicates that the association of peroxisomal serine:pyruvate aminotransferase with the peroxisomal membrane causes a marked conformational change in the structure of this protein.
Oda
T
T
Department of Biochemistry, Hamamatsu University School of Medicine, Shizuoka, Japan. odat129@hama-med.ac.jp
Funai
T
T
Miura
S
S
D000410:Alanine Transaminase / Q000737:chemistry* / Q000378:metabolism*; D000818:Animals; D002458:Cell Fractionation; D006801:Humans; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008830:Microbodies / Q000201:enzymology*; D014176:Protein Biosynthesis; D011487:Protein Conformation; D051381:Rats; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D000637:Transaminases; D014158:Transcription, Genetic
D011994:Recombinant Proteins; D000637:Transaminases; D000410:Alanine Transaminase; C019635:Alanine-glyoxylate transaminase