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Literature summary for 2.5.1.58 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

Protein Variants Comment Organism
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
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
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
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
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
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

Organism UniProt Comment Textmining
Rattus norvegicus
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recombinant enzyme
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Substrates and Products (Substrate)

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