3.4.21.107: peptidase Do
This is an abbreviated version!
For detailed information about peptidase Do, go to the full flat file.
Word Map on EC 3.4.21.107
-
3.4.21.107
-
degeneration
-
macular
-
cerebral
-
retinal
-
infarct
-
neovascularization
-
vessel
-
parkinsonism
-
leukoencephalopathy
-
arteriopathy
-
subcortical
-
carasil
-
xiap
-
misfolded
-
choroid
-
osteoarthritis
-
maculopathy
-
preeclampsia
-
polypoidal
-
pink1
-
acuity
-
alopecia
-
drusen
-
medicine
-
small-vessel
-
extracytoplasmic
-
amd-associated
-
notch3
-
spondylosis
-
transmigration
-
ranibizumab
-
biotechnology
-
molecular biology
- 3.4.21.107
- degeneration
-
macular
- cerebral
- retinal
- infarct
- neovascularization
- vessel
- parkinsonism
- leukoencephalopathy
-
arteriopathy
-
subcortical
-
carasil
- xiap
-
misfolded
- choroid
- osteoarthritis
- maculopathy
- preeclampsia
-
polypoidal
- pink1
-
acuity
- alopecia
-
drusen
- medicine
-
small-vessel
-
extracytoplasmic
-
amd-associated
-
notch3
- spondylosis
-
transmigration
-
ranibizumab
- biotechnology
- molecular biology
Reaction
acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-/-Val =
Synonyms
bacterial PQC factor, BB_0104, BCAL2829, CD630_32840, Deg1, DEG2, DEG5, DEG7, DEG8, Deg9, DegP, DegP protease, DegP/HtrA, DegQ, DegS, DepP9, Do, Do protease, HhoA, HhoB, high temperature requirement A, high temperature requirement A protease, high temperature requirement A1, high temperature requirement factor A, high-temperature requirement A, high-temperature requirement A protease, high-temperature requirement A-1, high-temperature requirement A1, high-temperature requirement A1 protease, high-temperature requirement factor A, HtrA, HtrA (DegP) protease, HtrA heat shock protease, HtrA protease, HTRA serine peptidase 1, HtrA-like protease, HtrA/DegP, HtrA1, HtrA2, HtrA3, HTRA4, MAL8P1.126, More, MucD, Nma111p, Omi/HtrA protease orthologue Ynm3p, protease do, protease Do-like 5, protease Do-like 8, PRSS11, S01.273, serine protease, serine protease HtrA, serine protease HtrA1, YNL123w
ECTree
3.4.21.107 peptidase DoAdvanced search results
results (
results (Subunits
Subunits on EC 3.4.21.107 - peptidase Do
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
decamer
-
10 * 54000, SDS-PAGE, enzyme exists in 3 different forms: pentamer, hexamer and decamer
dodecamer
hexamer
homooligomer
DegP of Escherichia coli assembles into large homooligomers with an internal cavity combining both chaperone and protease activity
multimer
oligomer
pentamer
-
5 * 54000, SDS-PAGE, enzyme exists in 3 different forms: pentamer, hexamer and decamer
tetracosamer
trimer
additional information
?
-
x * 104000, calculated from sequence for full-length protein, x * 60000, mature C-terminal fragment, * 40000, mature N-terminal fragment, SDS-PAGE
dodecamer
-
12 * 50000, SDS-PAGE, enzyme can exist in two oligomeric forms which are interconvertible
dodecamer
-
consists of two stacks of hexameric rings, SDS-PAGE, cross-linking experiments
hexamer
-
6 * 50000, SDS-PAGE, enzyme can exist in two oligomeric forms which are interconvertible
hexamer
-
6 * 54000, SDS-PAGE, enzyme exists in 3 different forms: pentamer, hexamer and decamer
hexamer
two trimers for a hexameric structure by staggered association
hexamer
crystal structures suggest that HtrA proteins differ in their molecular architecture, ranging from trimers with surface-accessible active sites to hexamers
hexamer
purified wild type DegP exists mainly as hexamers (dimers of trimers) in solution
hexamer
DegP, dimer of two trimers
multimer
-
DegP activates its chaperone and protease functions via formation of large cage-like 12- and 24-mers after binding to substrate proteins. Cryo-electron microscopic and biochemical studies reveal that both oligomers are consistently assembled by blocks of DegP trimers, via pairwise PDZ1-PDZ2 interactions between neighboring trimers. Such interactions simultaneously eliminate the inhibitory effects of the PDZ2 domain. Additionally, both DegP oligomers are also observed in extracts of Escherichia. coli cells, strongly implicating their physiological importance
multimer
gel filtration shows three DegP oligomers, namely the 6-mer (DegP6), the 12-mer (DegP12) and the 24-mer (DegP24), of which the two larger particles had additional proteins bound. Binding of misfolded proteins transforms hexameric DegP into large, catalytically active 12-meric and 24-meric multimers. A structural analysis of these particles reveal that DegP represents a protein packaging device whose central compartment is adaptable to the size and concentration of substrate. Moreover, the inner cavity serves antagonistic functions
oligomer
-
largest complexes are dodecamers, probably formed by dimerization of trimers, gel filtration experiments
oligomer
-
DegP protease chaperone system is regulated by oligomer conversion from the resting hexamer into the catalytically active 12mer and 24mer that capture and digest misfolded proteins
oligomer
-
x * about 50000, SDS-PAGE. In the absence of substrate, DegP oligomerizes as a hexameric cage but in its presence DegP reorganizes into active 12- and 24-mer cages. The size of the substrate molecule is the main factor conditioning the oligomeric state adopted by the enzyme, while ther factors such as temperature, do not influence the oligomeric state
trimer
crystal structures suggest that HtrA proteins differ in their molecular architecture, ranging from trimers with surface-accessible active sites to hexamers
additional information
-
secondary structures for activated protease at different temperatures
additional information
DegQ changes its oligomeric state from hexamers to either 12 or 24mers depending on the concentration of unfolded substrate, DegQ forms 12mers in the absence of substrate at acidic pH, enzyme structure analysis of the 12 and 24mer states in complex with model substrates, overview. The polypeptides are probably cooperatively bound by PDZ1 and protease domains
additional information
the Deg protein contain a catalytic domain with the serine protease catalytic triad, and C-terminal PDZ domains, two in DegP and DegQ, one in DegS
additional information
-
HtrA contains a putative N-terminal membrane anchor domain, Ile13 to Ile26, a trypsin-like serine protease catalytic triad formed by His129, Asp158, and Ser240, and a single C-terminal PDZ domain, Gly296 to Arg385
