Autor: |
Ganesh Bhat B; Departments of Nutrition, Pediatrics, and Medicine, The University of North Carolina, Chapel Hill NC 27599-7400, USA., Wang P, Kim JH, Black TM, Lewin TM, Fiedorek FT Jr, Coleman RA |
Jazyk: |
angličtina |
Zdroj: |
Biochimica et biophysica acta [Biochim Biophys Acta] 1999 Aug 18; Vol. 1439 (3), pp. 415-23. |
DOI: |
10.1016/s1388-1981(99)00103-1 |
Abstrakt: |
Rat mitochondrial glycerol-3-phosphate acyltransferase (GPAT) cDNA was cloned and characterized. We identified a cDNA containing an open reading frame of 828 amino acids that had an 89% homology with the coding region of the previously characterized mouse mitochondrial GPAT and a predicted amino acid sequence that was 96% identical. The rat 5' UTR was only 159 nucleotides, in contrast to the 926 nucleotide 5' UTR of the mouse cDNA and had an internal deletion of 167 nucleotides. GPAT was expressed in Sf21 insect cells, and specific inhibitors strongly suggest that, like the Escherichia coli GPAT, the recombinant mitochondrial GPAT and the mitochondrial GPAT isoform in rat liver contain critical serine, histidine, and arginine residues. |
Databáze: |
MEDLINE |
Externí odkaz: |
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