MG_239_HEXAMER – ATP-dependent protease La

WID MG_239_HEXAMER View in model
Name ATP-dependent protease La View in model
Cross references PDB: 2ANE
Biosynthesis [c]: (6) MG_239_MONOMERMG_239_HEXAMER View in model
No. subunits 6
Empirical formula (pH 7.5) H39306C24126N6468O7296S102
Molecular weight (pH 7.5; Da) 539984.25 View in model
Extinction coefficient 
(260 nm, 25C, pH 7.0)
Half life (OD (600 nm) = 0.3, 
M9 media, 36C; min)
1200.00 View in model
Formation process Process_MacromolecularComplexation View in model
Localization c
Enzyme View in model
Complex subunit ATP-dependent protease La
[c]: (6) MG_239_MONOMERMG_239_HEXAMER
View in model
Parameters View in model
Comments Very processive protease; processes entire peptides without falling off. Can catalyze 10,000 cleavages per min. Degrades peptides in both directions [PUB_0029]. Cleavage site is 2-4 hydrophobic residues preceded by a charged or hydrophilic residue. Produces amino acid fragments of length 5-30 amino acids at a cost of 4 ATP due to stochastic distribution of cleavage sites [PUB_0029]. Degrades ssrA-tagged polypeptides [PUB_0821]. Also has chaperone-like activity for macromolecular complexes [PUB_0029]. Composition Function as a hexamer with Mg2+ cofactor [PUB_0029].
  1. Gur E, Sauer RT. Evolution of the ssrA degradation tag in Mycoplasma: specificity switch to a different protease. Proc Natl Acad Sci U S A 105, 16113-8 (2008). WholeCell: PUB_0821, PubMed: 18852454

  2. Lee I, Suzuki CK. Functional mechanics of the ATP-dependent Lon protease- lessons from endogenous protein and synthetic peptide substrates. Biochim Biophys Acta 1784, 727-35 (2008). WholeCell: PUB_0029, PubMed: 18359303

Created 2012-10-01 15:07:39
Last updated 2012-10-01 15:14:10