MG_457_HEXAMER – ATP-dependent metalloprotease FtsH

Name
WID MG_457_HEXAMER View in model
Name ATP-dependent metalloprotease FtsH View in model
 
Structure
Biosynthesis [m]: (6) MG_457_MONOMERMG_457_HEXAMER View in model
No. subunits 6
Empirical formula (pH 7.5) H33258C20472N5664O6216S72
Molecular weight (pH 7.5; Da) 460498.69 View in model
Extinction coefficient 
(260 nm, 25C, pH 7.0)
-281970.00
Half life (OD (600 nm) = 0.3, 
M9 media, 36C; min)
1200.00 View in model
 
Synthesis
Formation process Process_MacromolecularComplexation View in model
Localization m
 
Function
Enzyme View in model
Complex subunit ATP-dependent metalloprotease FtsH
[m]: (6) MG_457_MONOMERMG_457_HEXAMER
View in model
 
Parameters
Parameters View in model
 
Comments
Comments FtsH is a processive protease which can dislocate membrane proteins, degrades peptides in both directions, preferentially cleaves hydrophobic and basic residues, and produces fragments of length 10-20 amino acids [PUB_0030]. FtsH uses 8.3 ATP / cleavage at a rate 1.8 cleavage/min [PUB_0031]. Composition Functions as a homohexamer with Zn2+ cofactor [PUB_0030].
References
  1. Bruckner RC, Gunyuzlu PL, Stein RL. Coupled kinetics of ATP and peptide hydrolysis by Escherichia coli FtsH protease. Biochemistry 42, 10843-52 (2003). WholeCell: PUB_0031, PubMed: 12962509

  2. Ito K, Akiyama Y. Cellular functions, mechanism of action, and regulation of FtsH protease. Annu Rev Microbiol 59, 211-31 (2005). WholeCell: PUB_0030, PubMed: 15910274

 
Metadata
Created 2012-10-01 15:07:42
Last updated 2012-10-01 15:14:17