The joining of the 15-carbon farnesyl group ðC15H25Þ and the 20-carbon geranylgeranyl group ðC20H33Þ to protein–cysteines at or near their carboxy-termini is catalyzed by protein farnesyltransferase (FTase) and protein geranylgeranyltransferase-I and II (GGTase-I and GGTase-II) [1]. The prenyltransferases are hetero-dimers consisting of a- and b-subunits with combined molecular masses ranging from 91 to 98 kDa. The a-subunits of FTase and GGTase-I are the same, and the b-subunits differ. The b-subunits of the three enzymes are homologous to the a-subunits and to each other. The overall reactions are shown by the following chemical equations: FPPþHS-peptide! farnesyl-S-peptideþ PP GGPP þHS-peptide! geranylgeranyl-S-accepto
ABSTRACT: Protein prenylation is a ubiquitous covalent post-translational modification found in all ...
Prenylation is a lipidation post-translational modification wherein a hydrophobic isoprenoid group i...
Three different prenyltransferases attach isoprenyl anchors to C-terminal motifs in substrate protei...
Prenylation is essential for the function of many cellular signaling proteins, including Ras, which ...
Prenylation is essential for the function of many cellular signaling proteins, including Ras, which ...
Prenylation is a universal covalent post-translational modification found in all eukaryotic cells, c...
Prenylation is an important post-translational modification that targets proteins to the cellular me...
Protein farnesyltransferase (FTase) is a member of the prenyltransferase family, which also includes...
Protein farnesyltransferase (FTase) is a member of the prenyltransferase family, which also includes...
Post‐translational modifications (PTMs) expand the number of protein isoforms in eukaryotic proteome...
Up to 2% of the mammalian proteome is post-translationally modified with isoprenes (Gelb 1997). The ...
Post-translational modifications (PTMs) expand the number of protein isoforms in eukaryotic proteome...
Many G-proteins, like Ras, require prenylation for membrane localization and function. Protein farn...
Many G-proteins, like Ras, require prenylation for membrane localization and function. Protein farn...
Free to read at publisher's site. Post‐translational isoprenylation of proteins is carried out by th...
ABSTRACT: Protein prenylation is a ubiquitous covalent post-translational modification found in all ...
Prenylation is a lipidation post-translational modification wherein a hydrophobic isoprenoid group i...
Three different prenyltransferases attach isoprenyl anchors to C-terminal motifs in substrate protei...
Prenylation is essential for the function of many cellular signaling proteins, including Ras, which ...
Prenylation is essential for the function of many cellular signaling proteins, including Ras, which ...
Prenylation is a universal covalent post-translational modification found in all eukaryotic cells, c...
Prenylation is an important post-translational modification that targets proteins to the cellular me...
Protein farnesyltransferase (FTase) is a member of the prenyltransferase family, which also includes...
Protein farnesyltransferase (FTase) is a member of the prenyltransferase family, which also includes...
Post‐translational modifications (PTMs) expand the number of protein isoforms in eukaryotic proteome...
Up to 2% of the mammalian proteome is post-translationally modified with isoprenes (Gelb 1997). The ...
Post-translational modifications (PTMs) expand the number of protein isoforms in eukaryotic proteome...
Many G-proteins, like Ras, require prenylation for membrane localization and function. Protein farn...
Many G-proteins, like Ras, require prenylation for membrane localization and function. Protein farn...
Free to read at publisher's site. Post‐translational isoprenylation of proteins is carried out by th...
ABSTRACT: Protein prenylation is a ubiquitous covalent post-translational modification found in all ...
Prenylation is a lipidation post-translational modification wherein a hydrophobic isoprenoid group i...
Three different prenyltransferases attach isoprenyl anchors to C-terminal motifs in substrate protei...