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Literature summary for 5.4.99.2 extracted from

  • Padovani, D.; Labunska, T.; Banerjee, R.
    Energetics of interaction between the G-protein chaperone, MeaB, and B12-dependent methylmalonyl-CoA mutase (2006), J. Biol. Chem., 281, 17838-17844.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Methylorubrum extorquens
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Subunits

Subunits Comment Organism
More holomutase enzyme binds G-protein chaperone MeaB 15fold more tightly in presence of guanosine 5’-(beta-gamma-imino)triphosphate than of GDP, the apomutase binds MeaB with similar affinity in presence of either nucleotide. a large structural rearrangement accompanies interaction between the proteins and buries between 4000 and 8600 A2 of surface area. The intrinsic low GTPase activity of MeaB is stimulated 100fold by binding to the mutase Methylorubrum extorquens