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
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macular
-
cerebral
-
retinal
-
infarct
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neovascularization
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vessel
-
parkinsonism
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leukoencephalopathy
-
arteriopathy
-
subcortical
-
carasil
-
xiap
-
misfolded
-
choroid
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osteoarthritis
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maculopathy
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preeclampsia
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polypoidal
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pink1
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acuity
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alopecia
-
drusen
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medicine
-
small-vessel
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extracytoplasmic
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amd-associated
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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 (Substrates Products
Substrates Products on EC 3.4.21.107 - peptidase Do
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
aggrecan + H2O
aggrecan fragments
-
the HtrA1-specific cleavage site is VQTV3562357TWPD within the interglobular domain of aggrecan
-
-
?
citrate synthase + H2O
?
-
acts on the thermally unfolded synthase but not on the native form
-
?
colicin A lysis protein + H2O
?
-
i.e. pCal, hydrolyses the acylated precursor form, cleaves at two sites near the C-terminal end to give two truncated proteins which are matured into two truncated Cals
-
?
competence-stimulating peptide CSP-1 + H2O
?
-
enzyme HtrA constitutes the primary extracytoplasmic competence-stimulating peptide-degrading activity in cultures of Streptococcus pneumoniae. Both substrate isoforms CSP-1 and CSP-2 interact with HtrA with similar efficiencies
cleavage predominantly follows residue Phe8 of the CSP-1 isoform of the peptide within its central hydrophobic patch
-
?
competence-stimulating peptide CSP-2 + H2O
?
-
enzyme HtrA constitutes the primary extracytoplasmic competence-stimulating peptide-degrading activity in cultures of Streptococcus pneumoniae. Both substrate isoforms CSP-1 and CSP-2 interact with HtrA with similar efficiencies
-
-
?
CSP-1 FRET peptide + H2O
?
-
reporter peptide with incorporation of a QSY-7 quencher and a Cys(Alexa488) fluorophore at theN-erminus andC-terminus of CSP-1, respectively
-
-
?
D1 protein + H2O
?
-
degrades photodamaged D1 protein of photosystem II
-
?
E-cadherin + H2O
85 kDa N-terminal fragment + 40 kDa C-terminal fragment
-
selective substrate
-
-
?
Faa1p + H2O
?
-
direct interaction of Faa1p with the Omi/HtrA protease orthologue Ynm3p alters lipid homeostasis, Ynm3p modulates fatty acid metabolism and gene regulation through negative regulation of ACSL activity, overview
-
-
?
filamentous haemagglutinin precursor + H2O
?
-
DegP contributes to degrading the filamentous haemagglutinin precursor when it is blocked intracellularly
-
-
?
insulin growth factor-binding protein 5 + H2O
?
-
substrate of isoform HTRA1
-
-
?
outer membrane protein A + H2O
?
in contrast to misfolded model substrates, which are degraded within a few min, the co-purified outer-membrane proteins are stable. Even in the presence of externally applied proteases, the bound outer-membrane proteins are almost entirely resistant to proteolytic degradation. DegP functions as a geniune chaperone
-
-
?
outer membrane protein C + H2O
?
in contrast to misfolded model substrates, which are degraded within a few min, the co-purified outer-membrane proteins are stable. Even in the presence of externally applied proteases, the bound outer-membrane proteins are almost entirely resistant to proteolytic degradation. DegP functions as a geniune chaperone
-
-
?
outer membrane protein F + H2O
?
in contrast to misfolded model substrates, which are degraded within a few min, the co-purified outer-membrane proteins are stable. Even in the presence of externally applied proteases, the bound outer-membrane proteins are almost entirely resistant to proteolytic degradation. DegP functions as a geniune chaperone
-
-
?
pro-transforming growth factor-beta1 + H2O
mature transforming growth factor-beta1 + latency-associated peptide
-
-
latency-associated peptide is the N-terminal of pro-transforming growth factor-beta1
-
?
PVFNTLPMMGKASPV-4-nitroanilide + H2O
PVFNTLPMMGKASPV + 4-nitroaniline
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-4-methylcoumarin 7-amide + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
?
tau protein + H2O
?
enzyme degrades aggregated and fibrillar tau, a protein critically involved in various neurological disorders
-
-
?
tuberous sclerosis complex 2 protein + H2O
?
-
specific substrate for HtrA1 which is cleaved both in vitro and in vivo
-
-
?
VFNTLPMMGKASPV-4-nitroanilide + H2O
VFNTLPMMGKASPV + 4-nitroaniline
-
-
-
-
?
alpha-lactalbumin + H2O
?
-
only when incubated in the presence of 20 mM dithiothreitol, which reduces the structural disulfide bonds and unfold the protein, and above 34°C, is CtHtrA able to proteolyse alpha-lactalbumin
-
-
?
alpha-lactalbumin + H2O
?
-
acts on the fully unfolded protein but not on the native form
-
?
beta-casein + H2O
?
-
cleaves beta-casein yielding several polypeptide fragments
-
?
beta-casein + H2O
?
-
little uncleaved beta-casein remains in assays with recombinant HtrA, and a prominent degradation fragment appears. Recombinant HhoA completely degrades the excess of beta-casein, whereas recombinant HhoB shows only little activity and generates a prominent degradation fragment with a slightly lower molecular mass than intact beta-casein. The C-terminal cleavage sites Val162, Gln141 and Val130 are identified for recombinant HtrA. A common cleavage site at Leu165 is found for HhoA and HhoB, however, HhoA additionally cleaves beta-casein at Ala101 generating two proteolytic fragments, the N-terminal 1-101 as well as the C-terminal 102-199 amino acid fragments
-
-
?
beta-casein + H2O
beta-casein peptide fragments
-
the cleavage activity at 37°C is ATP independent, not significantly influenced by buffer composition, active over a broad range of pH, and with a broad optimum at pH 6.5, and 20 mM salts, e.g. magnesium sulfate, magnesium chloride, or sodium chloride, improving activity, determination of cleavage sites
-
-
?
Bovine serum albumin + H2O
?
-
85% of the activity with casein
-
-
?
chemotaxis signal transduction phosphatase CheX + H2O
?
-
-
-
?
chemotaxis signal transduction phosphatase CheX + H2O
?
-
-
-
?
decorin + H2O
decorin peptide fragments
-
a small leucine-rich proteoglycan
-
-
?
decorin + H2O
decorin peptide fragments
-
the small leucine-rich proteoglycan is highly expressed in bone and regulates type I collagen fibril assembly
generation of fragments ranging from 150 to 75 kDa
-
?
decorin + H2O
decorin peptide fragments
-
a small leucine-rich proteoglycan, human substrate
generation of fragments ranging from 150 to 75 kDa
-
?
E-cadherin + H2O
?
enzyme cleaves E-cadherin on host cells
-
-
?
fibronectin + H2O
fibronectin peptide fragments
-
HtrA is involved in cartilage catabolism
-
-
?
fibronectin + H2O
fibronectin peptide fragments
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a major noncollagenous component of mineralized bone matrix
generation of fragments ranging from 200 to 150 kDa
-
?
fibronectin + H2O
fibronectin peptide fragments
-
human plasma-derived substrate
generation of fragments ranging from 200 to 150 kDa
-
?
FkpA + H2O
?
-
periplasmic peptidyl-prolyl cistrans isomerase, chaperone
-
-
?
FkpA + H2O
?
-
periplasmic peptidyl-prolyl cis-trans isomerase, chaperone
-
-
?
insulin beta-chain + H2O
?
-
oxidized beta-chain which is fully unfolded
-
?
Lysozyme + H2O
?
-
can only be digested in the presence of reducing agents
-
?
malate dehydrogenase + H2O
?
-
acts on the thermally unfolded protein but not on the native form
-
?
matrix Gla protein + H2O
processed matrix Gla protein + 12 kDa peptide
-
the protein substrate is present in cartilage, bone, and arteries
-
-
?
matrix Gla protein + H2O
processed matrix Gla protein + 12 kDa peptide
-
cleavage of MGP at the C terminus
-
-
?
N-acetyl-L-tyrosine ethyl ester + H2O
N-acetyl-L-tyrosine + ethanol
-
51% of the activity with casein
-
-
?
N-acetyl-L-tyrosine ethyl ester + H2O
N-acetyl-L-tyrosine + ethanol
-
51% of the activity with casein
-
-
?
Protein + H2O
?
-
cleaves model substrates at discrete Val/Xaa or Ile/Xaa sites
-
?
Protein + H2O
?
-
cleaves preferably at hydrophobic side chains at the P1 position
-
?
Protein + H2O
?
-
denatured proteins aggregate to form a distinct S fraction, one third of the isolated S fraction is converted to trichloroacetic acid-soluble products
-
?
Protein + H2O
?
-
denatured proteins aggregate to form a distinct S fraction, one third of the isolated S fraction is converted to trichloroacetic acid-soluble products, enzyme has a preference for valine or isoleucine as the residue preceding the cleavage site
-
?
Protein + H2O
?
-
enzyme recognizes an ssrA-encoded peptide tag which is tagged to misfolded proteins or protein fragments
-
?
reaction centre protein D2 + H2O
?
-
substrate of isoforms DEG1, DEG5, DEG7 and DEG8
-
-
?
reaction centre protein D2 + H2O
?
-
substrate of isoforms DEG1, DEG5, DEG7 and DEG8
-
-
?
additional information
?
-
-
involved in the degradation of damaged proteins
-
?
additional information
?
-
-
the enzyme plays a role in the Burkholderia cenocepacia stress response, HtrABCAL2829 is required for growth of Burkholderia cenocepacia upon exposure to osmotic stress by NaCl or KCl, and thermal stress at 44°C
-
-
?
additional information
?
-
-
HtrA sequence specificity, overview, no activity with albumin and myoglobin at 37°C, HtrA acts as both a chaperone and protease, HtrA mutant S247A is able to chaperone insulin B-chain, irrespective of temperature, but at 30°C only HtrA and not mutant S247A displays significant chaperone activity for alpha-lactalbumin, overview
-
-
?
additional information
?
-
-
acts on substrates that are at least partially unfolded, does not cleave stably folded proteins, acts as a general chaperone forming stable complexes with several misfolded proteins
-
?
additional information
?
-
-
no substrates are: bovine serum albumin, ovalbumin, globin, insulin and other peptides that are routinely used as protease substrates
-
?
additional information
?
-
-
no substrates are: native bovine serum albumin, insulin, growth hormone or a variety of commonly used peptide substrates
-
?
additional information
?
-
-
heat shock serine protease that degrades misfolded proteins at high temperatures
-
?
additional information
?
-
-
involved in the degradation of damaged proteins
-
?
additional information
?
-
-
involved in the degradation of damaged proteins
-
?
additional information
?
-
-
involved in the degradation of damaged proteins
-
?
additional information
?
-
-
involved in the degradation of damaged proteins
-
?
additional information
?
-
-
involved in the degradation of damaged proteins
-
?
additional information
?
-
-
involved in the degradation of damaged proteins
-
?
additional information
?
-
-
involved in the degradation of damaged proteins
-
?
additional information
?
-
involved in the degradation of damaged proteins
-
?
additional information
?
-
involved in the degradation of damaged proteins
-
?
additional information
?
-
-
involved in the degradation of damaged proteins
-
?
additional information
?
-
-
involved in the degradation of damaged proteins, enzyme is indispensable for bacterial survival at elevated temperatures
-
?
additional information
?
-
-
involved in the degradation of damaged proteins, enzyme is indispensable for bacterial survival at temperatures above 42°C
-
?
additional information
?
-
-
involved in the degradation of damaged proteins, enzyme is indispensable for bacterial survival at temperatures above 42°C
-
?
additional information
?
-
-
involved in the degradation of damaged proteins, participate in removal of aggregated proteins
-
?
additional information
?
-
-
involved in the degradation of damaged proteins, switches from chaperone to protease function in a temperature-dependent manner
-
?
additional information
?
-
-
involved in the degradation of denatured and unfolded proteins
-
?
additional information
?
-
-
involved in the degradation of misfolded proteins
-
?
additional information
?
-
-
involved in the degradation of unfolded proteins
-
?
additional information
?
-
-
unable to cleave inhibitor of apoptosis protein
-
-
?
additional information
?
-
-
allosteric activation of DegP by stress signals during bacterial protein quality control, regulation mechanism, pathway scheme, overview
-
-
?
additional information
?
-
-
HtrA inhibits the unfolded lysozyme substrate aggregation over the range of temperatures at 30-45°C, HtrA is able to bind to the denatured polypeptides and as a consequence limits their ability to form large aggregates, overview, HtrA may protect the bacterial cells from deleterious effects of heat shock not only by degrading the damaged proteins but by combination of the proteolytic and chaperoning activities
-
-
?
additional information
?
-
-
HtrA shows chaperone-like activity, overview
-
-
?
additional information
?
-
-
when unfolded proteins bind to CpxP, DegP efficiently degrades this protein complex
-
-
?
additional information
?
-
-
almost no activity towards SDAEFRHDSGYEV-4-nitroanilide, SDAEFRHDSGYEV-4-nitroanilide, SGRVVPGYGHA-4-nitroanilide, SPLPEGV-4-nitroanilide , GLATGNVSTAELQDATPA-4-nitroanilide, KGKNSGSGATPV-4-nitroanilide, KGASVPGAGLV-4-nitroanilide, SPAKGGEEPLPEGV-4-nitroanilide, and benzoyl-L-Arg-4-nitroanilide
-
-
?
additional information
?
-
-
identification of beta-barrel outer membrane proteins, OMPs, as major natural substrates by photo-crosslinking using non-natural amino acid DiZPK, 3-(3-methyl-3H-diazirine-3-yl)-propaminocarbonyl-Nepsilon-L-lysine, as the photo-crosslinker. Isoform DegP primarily functions as a protease, at both low and high temperatures, to eliminate unfolded outer membrane proteins, with hardly any appreciable chaperone activity in cells. The toxic and cell membrane-damaging misfolded outer membrane proteins would accumulate in DegP-lacking cells cultured under heat shock conditions
-
-
?
additional information
?
-
the enzyme shows chaperone-like activity with substrate lysozyme, and protease activity. The PDZ domains are needed for DegQ chaperone activity. Up to six lysozyme substrates bind inside the DegQ dodecamer cage, binding of a well-ordered lysozyme to four DegQ protomers, overview
-
-
?
additional information
?
-
-
the enzyme does not cleave recombinant immunoglobulin A, epidermal growth factor receptor or junctional adhesion molecule
-
-
?
additional information
?
-
enzyme cuts preferentially after valine at P1, with serine, leucine and isoleucine in decreasing order of preference. No substrate: native lysozyme
-
-
?
additional information
?
-
-
enzyme cuts preferentially after valine at P1, with serine, leucine and isoleucine in decreasing order of preference. No substrate: native lysozyme
-
-
?
additional information
?
-
-
involved in the degradation of damaged proteins, involved in arthritis, cell growth, stress response, apoptosis and aging, possible tumor suppressor function
-
?
additional information
?
-
-
HtrA1 expression is regulated by cisplatin and paclitaxel, and upregulation results in catalytic activation of HtrA1, overview, HtrA1 influences tumor response to chemotherapy by modulating hemotherapy-induced cytotoxicity, HtrA1 in ovarian and gastric cancers may contribute to in vivo chemoresistance, overview
-
-
?
additional information
?
-
-
HtrA1 plays a role in arthritic disease, within the context of arthritis pathology HtrA1 contributes to cartilage degradation, overview
-
-
?
additional information
?
-
-
HTRA1 does not cleave CFH protein, complement component C3 and complement component C3b
-
-
?
additional information
?
-
-
HTRA1 interacts with presenilin 1 to cleave one product of gamma-secretase
-
-
?
additional information
?
-
-
HTRA1 fails to cleave mature transforming growth factor-beta1
-
-
?
additional information
?
-
-
HtrA1 shows no activity towards tuberous sclerosis complex 1 protein and bovine serum albumin
-
-
?
additional information
?
-
role in extracellular proteolysis, proteolysis occurs during or after export to the cell surface, involved in the degradation of abnormal exported proteins
-
?
additional information
?
-
-
role in extracellular proteolysis, proteolysis occurs during or after export to the cell surface, involved in the degradation of abnormal exported proteins
-
?
additional information
?
-
-
HtrA is involved in the stress response of several important Gram-negative, as well as gram-positive, pathogens, HtrA is required for efficient Listeria monocytogenes biofilm formation at high temperatures
-
-
?
additional information
?
-
-
HtrA is involved in the stress response of several important Gram-negative, as well as gram-positive, pathogens, HtrA is required for efficient Listeria monocytogenes biofilm formation at high temperatures
-
-
?
additional information
?
-
-
involved in the degradation of damaged proteins, acts as protease, chaperone and regulator of apoptosis
-
?
additional information
?
-
-
HtrA is specific for mature mucosal mast cells
-
-
?
additional information
?
-
-
HtrA1 degrades specific matrix-associated proteins, HtrA1 inhibits mineral deposition by osteoblasts, the protease domain and the PDZ domain are essential for the inhibition of osteoblast mineralization by HtrA1, overview
-
-
?
additional information
?
-
-
HtrA1 is a secreted multidomain protein with serine protease activity
-
-
?
additional information
?
-
-
HtrA is specific for mature mucosal mast cells
-
-
?
additional information
?
-
-
MucD negatively regulates alginate production on genetic level, MucD-deficient strain show temperature-dependent alginate production, while MucD-containing strains do not, which is independent of MucD proteolytic activity, overview
-
-
?
additional information
?
-
-
DegP degrades unfolded or misfolded, secreted, and accumulated inactive proteins and is important for cell survival, especially in the absence of DsbA
-
-
?
additional information
?
-
-
mutants are deficient in their ability to survive in mice or macrophages
-
?
additional information
?
-
the enzyme is involved in survival of the bacteria under heat shock stress conditions in vitro and in vivo, overview
-
-
?
additional information
?
-
-
involved in the degradation of damaged proteins
-
?
additional information
?
-
-
enzyme displays a preference for substrates with non-polar residues at the P1 site
-
-
?
additional information
?
-
-
HtrA is essential for the maturation of cysteine protease streptococcal pyrogenic exotoxin B, SpeB, but is unable to directly process SpeB zymogen, proSpeB to the active form in vitro, thus playing an indirect role in the maturation, overview
-
-
?
additional information
?
-
-
no activity with correctly folded globular bovine serum albumin or lysozyme
-
-
?
additional information
?
-
-
involved in the degradation of damaged proteins
-
?
additional information
?
-
-
involved in the degradation of damaged proteins, chaperone and proteolytic activity
-
?
additional information
?
-
HtrA1 promotes posterior development in mRNA-injected Xenopus laevis embryos, e.g. induces secondary tail-like structures, expansion of mesoderm, and formation of ectopic neurons in an FGF-dependent manner, HtrA1 activates FGF/ERK signaling and the transcription of FGF genes by cleaving proteoglycans and releasing cell surface-bound FGF ligands, overview
-
-
?
additional information
?
-
-
deletion mutant is unable to grow at an elevated temperature and to survive within macrophages after phagocytosis
-
?
