MG_239_HEXAMER – ATP-dependent protease La
Name | ||
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WID | MG_239_HEXAMER |
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Name | ATP-dependent protease La |
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Cross references | PDB: 2ANE | |
Structure | ||
Biosynthesis | [c]: (6) MG_239_MONOMER ⇒ MG_239_HEXAMER |
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No. subunits | 6 | |
Empirical formula (pH 7.5) | H39306C24126N6468O7296S102 | |
Molecular weight (pH 7.5; Da) | 539984.25 |
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Extinction coefficient (260 nm, 25C, pH 7.0) |
-291750.00 | |
Half life (OD (600 nm) = 0.3, M9 media, 36C; min) |
1200.00 |
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Synthesis | ||
Formation process | Process_MacromolecularComplexation |
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Localization | c | |
Function | ||
Enzyme |
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Complex subunit | ATP-dependent protease La [c]: (6) MG_239_MONOMER ⇒ MG_239_HEXAMER |
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Parameters | ||
Parameters |
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Comments | ||
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]. | |
References |
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Metadata | ||
Created | 2012-10-01 15:07:39 | |
Last updated | 2012-10-01 15:14:10 |