Application | Comment | Organism |
---|---|---|
molecular biology | the GGTase-I variants with altered substrate specificity can serve as tools for studying GGTase-I substrate selectivity and the effects of prenylation pathway modifications on specific proteins | Rattus norvegicus |
Protein Variants | Comment | Organism |
---|---|---|
additional information | development of GGTase-I variants with expanded/altered substrate selectivity by site-directed mutagenesis | Rattus norvegicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
geranylgeranyl diphosphate + protein-cysteine | Rattus norvegicus | - |
S-geranylgeranyl-protein + diphosphate | - |
? | |
additional information | Rattus norvegicus | the enzyme modifies proteins by attaching a 20-carbon isoprenoid group to a cysteine residue near the C-terminus of a target protein. The enzyme requires a C-terminal Ca1a2X sequence on its substrates, with the a1, a2, and X residues serving as substrate-recognition elements for GGTase-I. Crystallographic structures of rat GGTase-I show a tightly packed and hydrophobic a2 residue binding pocket, consistent with a preference for moderately sized a2 residues in GGTase-I substrates, peptide substrate structure-activity relationship, overview. Identification of specific active-site residues within rat GGTase-I involved in substrate recognition | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | P53610 | subunit beta | - |
Rattus norvegicus | Q04631 | subunit alpha | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
geranylgeranyl diphosphate + protein-cysteine | - |
Rattus norvegicus | S-geranylgeranyl-protein + diphosphate | - |
? | |
additional information | the enzyme modifies proteins by attaching a 20-carbon isoprenoid group to a cysteine residue near the C-terminus of a target protein. The enzyme requires a C-terminal Ca1a2X sequence on its substrates, with the a1, a2, and X residues serving as substrate-recognition elements for GGTase-I. Crystallographic structures of rat GGTase-I show a tightly packed and hydrophobic a2 residue binding pocket, consistent with a preference for moderately sized a2 residues in GGTase-I substrates, peptide substrate structure-activity relationship, overview. Identification of specific active-site residues within rat GGTase-I involved in substrate recognition | Rattus norvegicus | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
GGTase-I | - |
Rattus norvegicus |
General Information | Comment | Organism |
---|---|---|
evolution | tunable selectivity may be a general phenomenon among multispecific enzymes involved in posttranslational modification and raises the possibility of variable substrate selectivity among GGTase-I orthologues from different organisms | Rattus norvegicus |