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Literature summary for 2.5.1.59 extracted from

  • Hartman, H.L.; Bowers, K.E.; Fierke, C.A.
    Lysine beta311 of protein geranylgeranyltransferase type I partially replaces magnesium (2004), J. Biol. Chem., 279, 30546-30553.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
Kbeta311A mutation decreases prenylation rate constant in absence of Mg2+. Addition of Mg2+ increases geranylgeranylation rate constant Rattus norvegicus
Kbeta311D mutation decreases prenylation rate constant in absence of Mg2+. Addition of Mg2+ increases geranylgeranylation rate constant Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ prenylation rate constant of wild type enzyme is not dependent on Mg2+ and is about 20fold slower than the maximal rate constant catalyzed by protein farnesyltransferase. Prenylation rate constant in mutant Kbeta311A or Kbeta311D decreases in absence of magnesium 9–41fold without significantly affecting the binding affinityof either substrate. Furthermore, the geranylgeranylation rate constant is enhanced by the addition of Mg2+ for Kbeta311A and Kbeta311D GGTase I 2–5-fold compared with wild type GGTase I. These results demonstrate that lysine beta311 of GGTase I partially replaces the catalytic function of Mg2+ observed in protein farnesyltransferase Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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Synonyms

Synonyms Comment Organism
geranylgeranyltransferase type I
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 Rattus norvegicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
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 additional information
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 Rattus norvegicus