Carboxy-terminal CFFL-sequence-specific monomeric protein geranylgeranyltransferase I from the eyes of the shrimpPenaeus japonicus

✍ Scribed by Lin, Ruei-Shiuan; Chuang, Nin-Nin

• Publisher: John Wiley and Sons
• Year: 1998
• Tongue: English
• Weight: 343 KB
• Volume: 281
• Category: Article
• ISSN: 0022-104X
• DOI: 10.1002/(sici)1097-010x(19980815)281:6<565::aid-jez4>3.0.co;2-l

✦ Synopsis

Protein geranylgeranyltransferase I from the eyes of Penaeus japonicus geranylgeranylates predominantly the sequence CFFL and Drosophila-specific Ras1 carboxyl termini, with the sequence CKML, as well as mammalian-specific Gγ carboxyl termini, with the sequence CAIL, but not the protein farnesyltransferase-specific sequence CVLS. The purified protein geranylgeranyltransferase I from shrimp was evidenced by immunoblotting and polyacrylamide gel electrophoresis under denaturing conditions to consist of single subunit of Mr 66,000 ± 500. Since the active protein geranylgeranyltransferase I was found to have a relative mass of 67,000 ± 1,000, the purified enzyme was deduced to be a monomer. The enzyme had an optimal pH of 8.0 with 100 mM Tris as the buffer and a K m of 7 ± 2 µM with the synthetic peptide KCFFL as the substrate. The enzyme was inhibited by Zn ++ and Mg ++ ions at micromolar concentrations.