ATPHs_ProteinTranslocation_SecA – Protein translocation (SecA)

Name
WID ATPHs_ProteinTranslocation_SecA View in model
Name Protein translocation (SecA) View in model
 
Reaction
Stoichiometry [c]: ATP + H2OADP + H + PI View in model
 
Catalysis
Enzyme MG_072_DIMER [c] View in model
 
Energetics
Is spontaneous (pH 7.5, 25C, I = 0) False View in model
 
Kinetics
Forward kinetics Vmax = 1.626e+14 1/min View in model
 
Associations
Pathways ALA_ASP_METABOLISM
Process Process_ProteinTranslocation View in model
 
Comments
Comments Translocation catalyzed at rate 2.710e12 amino acids 1/s [PUB_0001] and requiring 1 ATP per 35 amino acids [PUB_0001, PUB_0002, PUB_0003]. Forms a dimer [PUB_0004].
References
  1. Eds Dalbey RE, von Heijne G. Protein Targeting, Transport, and Translocation. Academic Press, San Diego (2002). WholeCell: PUB_0003, ISBN: 9780122007316

  2. Doyle SM, Bilsel O, Teschke CM. SecA folding kinetics: a large dimeric protein rapidly forms multiple native states. J Mol Biol 341, 199-214 (2004). WholeCell: PUB_0002, PubMed: 15312773

  3. Tomkiewicz D, Nouwen N, van Leeuwen R, Tans S, Driessen AJ. SecA supports a constant rate of preprotein translocation. J Biol Chem 281, 15709-13 (2006). WholeCell: PUB_0001, PubMed: 16601117

  4. van Wely KH, Swaving J, Freudl R, Driessen AJ. Translocation of proteins across the cell envelope of Gram-positive bacteria. FEMS Microbiol Rev 25, 437-54 (2001). WholeCell: PUB_0004, PubMed: 11524133

 
Metadata
Created 2012-10-01 15:08:06
Last updated 2012-10-01 15:15:00