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Literature summary extracted from

  • Bowers, K.E.; Fierke, C.A.
    Positively charged side chains in protein farnesyltransferase enhance catalysis by stabilizing the formation of the diphosphate leaving group (2004), Biochemistry, 43, 5256-5265.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.58 K294A slightly higher peptide affinity than wild-type enzyme, 7fold decrease in affinity for farnesyl diphosphate, mutation decreases the positive charge in the diphosphate binding pocket and also decrease the value of Km(Mg2+), compared to wild-type, decrease in rate constant for farnesylation in absence of Mg2+ Rattus norvegicus
2.5.1.58 K294Q little alteration in peptide affinity, 2fold decrease in affinity for farnesyl diphosphate, mutation decreases the positive charge in the diphosphate binding pocket and also decrease the value of Km(Mg2+), compared to wild-type, decrease in rate constant for farnesylation in absence of Mg2+ Rattus norvegicus
2.5.1.58 R291A 2fold lower peptide affinity than wild-type enzyme, 3-4fold decrease in affinity for farnesyl diphosphate, mutation decreases the positive charge in the diphosphate binding pocket and also decrease the value of Km(Mg2+), compared to wild-type, decrease in rate constant for farnesylation in absence of Mg2+ Rattus norvegicus
2.5.1.58 R291G little alteration in peptide affinity, 3-4fold decrease in affinity for farnesyl diphosphate, mutation decreases the positive charge in the diphosphate binding pocket and also decrease the value of Km(Mg2+), compared to wild-type,decrease in rate constant for farnesylation in absence of Mg2+ Rattus norvegicus
2.5.1.58 R291K slightly higher peptide affinity than wild-type enzyme, mutation decreases the positive charge in the diphosphate binding pocket and also decrease the value of Km(Mg2+), compared to wild-type, decrease in rate constant for farnesylation in absence of Mg2+ Rattus norvegicus
2.5.1.58 R291Q little alteration in peptide affinity, mutation decreases the positive charge in the diphosphate binding pocket and also decrease the value of Km(Mg2+), compared to wild-type, decrease in rate constant for farnesylation in absence of Mg2+ Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.58 Rattus norvegicus
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recombinant enzyme
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.58 farnesyl diphosphate + protein-cysteine
-
Rattus norvegicus S-farnesyl protein + diphosphate
-
?