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Literature summary for 2.5.1.59 extracted from

  • Gangopadhyay, S.A.; Losito, E.L.; Hougland, J.L.
    Targeted reengineering of protein geranylgeranyltransferase type I selectivity functionally implicates active-site residues in protein-substrate recognition (2014), Biochemistry, 53, 434-446.
    View publication on PubMed
Search for more literature for 2.5.1.59

Application

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

Protein Variants Comment Organism
additional information development of GGTase-I variants with expanded/altered substrate selectivity by site-directed mutagenesis Rattus norvegicus

Natural Substrates/ Products (Substrates)

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 ?
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 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus P53610 subunit beta
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Rattus norvegicus Q04631 subunit alpha
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Substrates and Products (Substrate)

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

Synonyms Comment Organism
GGTase-I
-
 Rattus norvegicus

General Information

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