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Information on EC 3.4.24.B20 - FtsH protease and Organism(s) Aquifex aeolicus and UniProt Accession O67077

for references in articles please use BRENDA:EC3.4.24.B20
preliminary BRENDA-supplied EC number
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.B20 FtsH protease
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Aquifex aeolicus
UNIPROT: O67077
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Word Map
The taxonomic range for the selected organisms is: Aquifex aeolicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
degradative cleavage of proteins
Synonyms
ftsh protease, ftsh2, ftsh1, ftsh11, ftsh5, ftsh3, ftsh6, ftsh12, atp-dependent zinc metalloprotease, atftsh2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CAS REGISTRY NUMBER
COMMENTARY hide
253850-13-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
casein + H2O
?
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
contains zinc
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
x-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structures of a transmembrane helix-lacking FtsH construct from Aquifex aeolicus, at 2.9 A and 3.3 A resolution in space groups R32 and P312, respectively. In both structures, the FtsH hexamer is created from two different subunits of the asymmetric unit by the threefold symmetry of the crystals. All subunits are loaded with ADP. Within the ATPase cycle while the whole subunit switches from the opened to the closed state, pore loop-1 interacts with the substrate and translocates it into the proteolytic chamber
vapor diffusion method, using either 2 M ammonium sulfate, 0.1 M Tris-HCl pH 8.5, 10 mM EDTA or, as another condition, 60% tacsimate pH 7.0, 10 mM adenylyl imidodiphosphate lithium salt hydrate
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography, Resource Q anion-exchange chromatography, and Superdex 16/6000 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) CodonPlus cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vostrukhina, M.; Popov, A.; Brunstein, E.; Lanz, M.A.; Baumgartner, R.; Bieniossek, C.; Schacherl, M.; Baumann, U.
The structure of Aquifex aeolicus FtsH in the ADP-bound state reveals a C2-symmetric hexamer
Acta Crystallogr. Sect. D
71
1307-1318
2015
Aquifex aeolicus (O67077)
Manually annotated by BRENDA team
Uthoff, M.; Baumann, U.
Conformational flexibility of pore loop-1 gives insights into substrate translocation by the AAA+ protease FtsH
J. Struct. Biol.
204
199-206
2018
Aquifex aeolicus (O67077)
Manually annotated by BRENDA team