Protein prenyltransferases.
Three different protein prenyltransferases (farnesyltransferase and geranylgeranyltransferases I and II) catalyze the attachment of prenyl lipid anchors 15 or 20 carbons long to the carboxyl termini of a variety of eukaryotic proteins. Farnesyltransferase and geranylgeranyltransferase I both recognize a 'Ca1a2X' motif on their protein substrates; geranylgeranyltransferase II recognizes a different, non-CaaX motif. Each enzyme has two subunits. The genes encoding CaaX protein prenyltransferases are considerably longer than those encoding non-CaaX subunits, as a result of longer introns. Alternative splice forms are predicted to occur, but the extent to which each splice form is translated and the functions of the different resulting isoforms remain to be established. Farnesyltransferase-inhibitor drugs have been developed as anti-cancer agents and may also be able to treat several other diseases. The effects of these inhibitors are complicated, however, by the overlapping substrate specificities of geranylgeranyltransferase I and farnesyltransferase.
Maurer-Stroh
Sebastian
S
Research Institute of Molecular Pathology, Dr Bohr-Gasse 7, A-1030 Vienna, Austria. stroh@imp.univie.ac.at
Washietl
Stefan
S
Eisenhaber
Frank
F
D019883:Alkyl and Aryl Transferases / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D002384:Catalysis; D019143:Evolution, Molecular; D051231:Farnesyltranstransferase; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017368:Protein Prenylation; D051381:Rats; D016415:Sequence Alignment; D013379:Substrate Specificity
D019883:Alkyl and Aryl Transferases; C075607:Rab geranylgeranyltransferase; C083291:geranylgeranyltransferase type-I; D051231:Farnesyltranstransferase