3.4.24.B17: FtsH endopeptidase

This is an abbreviated version!
For detailed information about FtsH endopeptidase, go to the full flat file.

Reaction

proteolytic degradation of proteins =

Synonyms

cell division protein ftsH, FtsH, FtsH protease, FTSH_ECOLI, HflB, HlB, M41.001, MtFtsH, T.ftsH

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.24 Metalloendopeptidases

                3.4.24.B17 FtsH endopeptidase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
7	Activating Compound
5	AA Sequence
1	CAS Registry Number
19	Cloned(Commentary)
57	Cofactor
5	Crystallization (Commentary)
2	Expression
18	General Information
18	Inhibitors
6	KM Value [mM]
49	Localization
26	Metals/Ions
3	Molecular Weight [Da]
63	Natural Substrates/ Products (Substrates)
308	Organism
7	pH Optimum
3	Posttranslational Modification
39	Protein Variants
13	Purification (Commentary)
13	Reaction
24	Reaction Type
77	Reference
2	Renatured (Commentary)
12	Specific Activity [micromol/min/mg]
263	Substrates and Products (Substrate)
22	Subunits
100	Synonyms
12	Temperature Optimum [°C]
2	Temperature Range [°C]
8	Turnover Number [1/s]

Crystallization

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Crystallization on EC 3.4.24.B17 - FtsH endopeptidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide Go to Crystallization (commentary) Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

crystallization of a fragment, covering the entire protease domain (residues 405-634), crystals are grown in a buffer solution containing 0.1 M MES (pH 6.0) and 5% PEG8K, at 20°C, using vapor-diffusion technique. 2.79 resolution

Aquifex aeolicus

O67077

670228

crystallization of the soluble cytosolic region of FtsH (residues 126-624), crystals are grown in a buffer solution containing 0.1 M Tris-HCl (pH 7.2) and 1% PEG8K, 0.2 mM Zn acetate, 5 mM MgCl2 and 2.5 mM ADP at 20°C, using vapor-diffusion technique. 2.79 A resolution

Aquifex aeolicus

O67077

670228

hanging-drop vapour-diffusion method, AAA domain solution: 10 mg/ml protein, 20 mM Tris-HCl, pH 8.5, 50 mM NaCl, 1 mM DTT, precipitant is 1.5 M ammonium sulfate, 2 to 3 days, X-ray structure determination and analysis at about 1.5 A

Escherichia coli

-

649174

X-ray structure determination and analysis at about 1.5 A, molecular modeling

Escherichia coli

-

653896

microbatch methodFtsH is expressed in Escherichia coli as a construct (residues 146-610) lacking the two transmembrane helices and purified

Thermotoga maritima

Q9WZ49

670698