Information on EC 3.4.21.107 - peptidase Do

New: Word Map on EC 3.4.21.107
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.4.21.107
-
RECOMMENDED NAME
GeneOntology No.
peptidase Do
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cleavage of C-N-linkage
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
161108-11-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Borrelia burgdorferi
-
UniProt
Manually annotated by BRENDA team
Borrelia burgdorferi ATCC 35210
-
UniProt
Manually annotated by BRENDA team
a member of the Burkholderia cepacia complex, strains J2315 and K56-2
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain TX01
UniProt
Manually annotated by BRENDA team
K12
-
-
Manually annotated by BRENDA team
strain 10403S
-
-
Manually annotated by BRENDA team
strain 10403S
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Mus musculus BALB/c
Balb/c mice
-
-
Manually annotated by BRENDA team
mucoid strain FRD1 and nonmucoid strain PAO1, gene mucD encoded in the algT-mucABCD operon
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
DegP; strain SL3261, gene degP or htrA
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the HtrA protein family combines chaperone and protease activities and is essential for protein quality control in many organisms. HtrA proteins are composed of a chymotrypsin-like protease domain and one (DegS, HTRA1, HTRA2) or two PDZ domains (DegP, DegQ)
malfunction
metabolism
-
one of the targets of HtrA1 activity during fetal development is the tuberous sclerosis complex 2-tuberous sclerosis complex 1 pathway
physiological function
additional information
enzyme structure analysis of the 12 and 24mer states in complex with model substrates, overview. DegQ PDZ domains are located adjacent to substrate density and their presence is required for chaperone activity
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADAM9 + H2O
?
show the reaction diagram
-
54% cleavage
-
-
?
aggrecan + H2O
aggrecan fragments
show the reaction diagram
-
the HtrA1-specific cleavage site is VQTV3562357TWPD within the interglobular domain of aggrecan
-
-
?
alpha-casein + H2O
?
show the reaction diagram
alpha-lactalbumin + H2O
?
show the reaction diagram
alpha-Tubulin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha2-macroglobulin + H2O
?
show the reaction diagram
-
55% cleavage
-
-
?
amylase MalS + H2O
?
show the reaction diagram
-
-
-
?
Arc repressor + H2O
?
show the reaction diagram
-
-
-
?
autolysin AcmA + H2O
?
show the reaction diagram
-
-
?
azocasein + H2O
?
show the reaction diagram
-
-
-
?
basic membrane protein D + H2O
?
show the reaction diagram
beta-casein + H2O
?
show the reaction diagram
beta-casein + H2O
beta-casein peptide fragments
show the reaction diagram
beta-tubulin + H2O
?
show the reaction diagram
-
-
-
-
?
biglycan + H2O
?
show the reaction diagram
BODIPY TR-X casein + H2O
?
show the reaction diagram
-
-
-
-
?
bone morphogenetic protein + H2O
?
show the reaction diagram
-
substrate of isoform HTRA1
-
-
?
Bovine serum albumin + H2O
?
show the reaction diagram
casein + H2O
?
show the reaction diagram
casein-FITC + H2O
?
show the reaction diagram
chemotaxis signal transduction phosphatase CheX + H2O
?
show the reaction diagram
chloride intracellular channel protein 1 + H2O
?
show the reaction diagram
-
51% cleavage
-
-
?
citrate synthase + H2O
?
show the reaction diagram
-
acts on the thermally unfolded synthase but not on the native form
-
?
clusterin + H2O
?
show the reaction diagram
-
50% cleavage
-
-
?
colicin A lysis protein + H2O
?
show the reaction diagram
colicin A lysis protein precursor + H2O
?
show the reaction diagram
-
-
-
?
competence-stimulating peptide CSP-1 + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
degrades photodamaged D1 protein of photosystem II
-
?
decorin + H2O
?
show the reaction diagram
-
substrate of isoforms HTRA1 and HTRA3
-
-
?
decorin + H2O
decorin peptide fragments
show the reaction diagram
DPMFKLV-4-nitroanilide + H2O
DPMFKLV + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
E-cadherin + H2O
85 kDa N-terminal fragment + 40 kDa C-terminal fragment
show the reaction diagram
-
selective substrate
-
-
?
E-cadherin + H2O
?
show the reaction diagram
Faa1p + H2O
?
show the reaction diagram
-
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
-
-
?
fascin + H2O
?
show the reaction diagram
-
40% cleavage
-
-
?
fibromodulin + H2O
?
show the reaction diagram
-
90% cleavage
-
-
?
Fibronectin + H2O
?
show the reaction diagram
fibronectin + H2O
fibronectin peptide fragments
show the reaction diagram
filamentous haemagglutinin precursor + H2O
?
show the reaction diagram
-
DegP contributes to degrading the filamentous haemagglutinin precursor when it is blocked intracellularly
-
-
?
FkpA + H2O
?
show the reaction diagram
gamma-tubulin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
Globin + H2O
?
show the reaction diagram
-
-
-
?
glypican-4 + H2O
?
show the reaction diagram
-
-
-
?
HCLS1-associated X1 + H2O
?
show the reaction diagram
-
substrate of isoform HTRA2
-
-
?
HYTAVVKKSSAV + H2O
?
show the reaction diagram
-
model substrate
-
?
IciA protein + H2O
?
show the reaction diagram
-
inhibitor of DNA replication initiation
-
?
insulin beta-chain + H2O
?
show the reaction diagram
insulin growth factor-binding protein 5 + H2O
?
show the reaction diagram
-
substrate of isoform HTRA1
-
-
?
LamB + H2O
?
show the reaction diagram
-
DegP functions as a geniune chaperone
-
-
?
lambda repressor + H2O
?
show the reaction diagram
-
N-terminal domain
-
?
lysozmye + H2O
?
show the reaction diagram
-
-
-
-
?
Lysozyme + H2O
?
show the reaction diagram
-
can only be digested in the presence of reducing agents
-
?
malate dehydrogenase + H2O
?
show the reaction diagram
MalE + H2O
?
show the reaction diagram
-
periplasmic maltose-binding protein
-
-
?
matrix Gla protein + H2O
processed matrix Gla protein + 12 kDa peptide
show the reaction diagram
N-acetyl-L-tyrosine ethyl ester + H2O
N-acetyl-L-tyrosine + ethanol
show the reaction diagram
OmpA + H2O
?
show the reaction diagram
-
outer membrane porin protein
-
-
?
OmpC + H2O
?
show the reaction diagram
-
outer membrane porin protein
-
-
?
OmpF + H2O
?
show the reaction diagram
-
outer membrane porin protein
-
-
?
OmpW + H2O
?
show the reaction diagram
-
outer membrane porin protein
-
-
?
OmpX + H2O
?
show the reaction diagram
-
outer membrane porin protein
-
-
?
outer membrane protein + H2O
?
show the reaction diagram
-
-
-
?
outer membrane protein A + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
-
-
?
PapA + H2O
?
show the reaction diagram
-
major pilin subunit of the Pap pilus
-
?
PMMGKASPV-4-nitroanilide + H2O
PMMGKASPV + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
pro-transforming growth factor-beta1 + H2O
mature transforming growth factor-beta1 + latency-associated peptide
show the reaction diagram
-
-
latency-associated peptide is the N-terminal of pro-transforming growth factor-beta1
-
?
Protein + H2O
?
show the reaction diagram
PVFNTLPMMGKASPV-4-nitroanilide + H2O
PVFNTLPMMGKASPV + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
reaction centre protein D1 + H2O
?
show the reaction diagram
reaction centre protein D2 + H2O
?
show the reaction diagram
reduced alkaline phosphatase + H2O
?
show the reaction diagram
-
-
-
-
?
RseA + H2O
?
show the reaction diagram
-
physiological substrate of DegP
-
-
?
SPMFKGV-4-nitroanilide + H2O
SPMFKGV + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Staphylococcus aureus nuclease Nuc precursor + H2O
?
show the reaction diagram
-
-
?
succinyl-Leu-Leu-Val-Tyr-4-methylcoumarin 7-amide + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
syndecan-4 + H2O
?
show the reaction diagram
-
-
-
?
talin-1 + H2O
?
show the reaction diagram
-
21% cleavage
-
-
?
transforming growth factor-beta + H2O
?
show the reaction diagram
-
substrate of isoform HTRA1
-
-
?
tuberous sclerosis complex 2 protein + H2O
?
show the reaction diagram
-
specific substrate for HtrA1 which is cleaved both in vitro and in vivo
-
-
?
VFNTLPMMGKASPV-4-nitroanilide + H2O
VFNTLPMMGKASPV + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Vitronectin + H2O
?
show the reaction diagram
-
54% cleavage
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADAM9 + H2O
?
show the reaction diagram
-
54% cleavage
-
-
?
aggrecan + H2O
aggrecan fragments
show the reaction diagram
-
the HtrA1-specific cleavage site is VQTV3562357TWPD within the interglobular domain of aggrecan
-
-
?
alpha-Tubulin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha2-macroglobulin + H2O
?
show the reaction diagram
-
55% cleavage
-
-
?
beta-tubulin + H2O
?
show the reaction diagram
-
-
-
-
?
biglycan + H2O
?
show the reaction diagram
-
substrate of isoforms HTRA1 and HTRA3
-
-
?
bone morphogenetic protein + H2O
?
show the reaction diagram
-
substrate of isoform HTRA1
-
-
?
chloride intracellular channel protein 1 + H2O
?
show the reaction diagram
-
51% cleavage
-
-
?
clusterin + H2O
?
show the reaction diagram
-
50% cleavage
-
-
?
decorin + H2O
?
show the reaction diagram
-
substrate of isoforms HTRA1 and HTRA3
-
-
?
decorin + H2O
decorin peptide fragments
show the reaction diagram
-
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
-
?
E-cadherin + H2O
85 kDa N-terminal fragment + 40 kDa C-terminal fragment
show the reaction diagram
-
selective substrate
-
-
?
E-cadherin + H2O
?
show the reaction diagram
-
-
-
-
?
Faa1p + H2O
?
show the reaction diagram
-
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
-
-
?
fascin + H2O
?
show the reaction diagram
-
40% cleavage
-
-
?
fibromodulin + H2O
?
show the reaction diagram
-
90% cleavage
-
-
?
Fibronectin + H2O
?
show the reaction diagram
fibronectin + H2O
fibronectin peptide fragments
show the reaction diagram
filamentous haemagglutinin precursor + H2O
?
show the reaction diagram
-
DegP contributes to degrading the filamentous haemagglutinin precursor when it is blocked intracellularly
-
-
?
FkpA + H2O
?
show the reaction diagram
-
periplasmic peptidyl-prolyl cistrans isomerase, chaperone
-
-
?
gamma-tubulin + H2O
?
show the reaction diagram
-
-
-
-
?
HCLS1-associated X1 + H2O
?
show the reaction diagram
-
substrate of isoform HTRA2
-
-
?
insulin beta-chain + H2O
?
show the reaction diagram
-
-
-
-
?
insulin growth factor-binding protein 5 + H2O
?
show the reaction diagram
-
substrate of isoform HTRA1
-
-
?
LamB + H2O
?
show the reaction diagram
-
DegP functions as a geniune chaperone
-
-
?
MalE + H2O
?
show the reaction diagram
-
periplasmic maltose-binding protein
-
-
?
matrix Gla protein + H2O
processed matrix Gla protein + 12 kDa peptide
show the reaction diagram
-
the protein substrate is present in cartilage, bone, and arteries
-
-
?
OmpA + H2O
?
show the reaction diagram
-
outer membrane porin protein
-
-
?
OmpC + H2O
?
show the reaction diagram
-
outer membrane porin protein
-
-
?
OmpF + H2O
?
show the reaction diagram
-
outer membrane porin protein
-
-
?
OmpW + H2O
?
show the reaction diagram
-
outer membrane porin protein
-
-
?
OmpX + H2O
?
show the reaction diagram
-
outer membrane porin protein
-
-
?
outer membrane protein + H2O
?
show the reaction diagram
P0C0V0
-
-
-
?
outer membrane protein A + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
-
-
?
Protein + H2O
?
show the reaction diagram
reaction centre protein D1 + H2O
?
show the reaction diagram
reaction centre protein D2 + H2O
?
show the reaction diagram
talin-1 + H2O
?
show the reaction diagram
-
21% cleavage
-
-
?
transforming growth factor-beta + H2O
?
show the reaction diagram
-
substrate of isoform HTRA1
-
-
?
tuberous sclerosis complex 2 protein + H2O
?
show the reaction diagram
-
specific substrate for HtrA1 which is cleaved both in vitro and in vivo
-
-
?
Vitronectin + H2O
?
show the reaction diagram
-
54% cleavage
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CaCl2
-
stimulates at 5 mM
Fe2+
-
10 mM, up to 112% stimulation of the protease activity
K+
-
10 mM, up to 134% stimulation of the protease activity
MgSO4
-
activates at 20 mM
MnCl2
-
stimulates at 5 mM
additional information
-
largely independent of divalent cations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AEBSF
-
-
cardiolipin
-
-
diisopropyl fluorophosphate
diisopropyl fluorophosphates
-
-
diisopropylfluorophosphate
DnaJ
-
chaperone protein
-
Hg2+
-
1 mM, complete inhibition
HpHtrA inhibitor
-
small-molecule inhibitor that completely blocks E-cadherin cleavage by HtrA at 0.03 mM
-
HtrA1 inhibitor
-
-
-
N-(tert-butoxycarbonyl)-L-valyl-N-[(1R)-1-(diphenoxyphosphoryl)-2-methylpropyl]prolinamide
phosphatidylglycerol
-
inhibits activity at 50-55C
PMMGKASPV-chloromethylketone
-
49% residual activity at 0.5 mM
PVFNTLPMMGKASPV-chloromethylketone
-
63% residual activity at 0.5 mM
Sodium dodecyl sulfate
-
1 mM, 61% resiudal activity
SPMFKGV-chloromethylketone
-
3% residual activity at 0.5 mM
Triton X-100
-
5 mM, 71% residual activity
VFNTLPMMGKASPV-chloromethylketone
-
57% residual activity at 0.5 mM
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15 residue presenilin-1 peptide
-
activation
-
cardiolipin
enhances DegP proteolytic activity at high temperatures
CPII
-
cleavage of aggrecan by HtrA1 is strongly enhanced by HtrA1 agonists such as CPII, a C-terminal hexapeptide derived from the C-propeptide of procollagen IIalpha1
-
dermatan sulfate
triggers HtrA1-induced peteriorization, overview
DKVLVVWAGQQ
-
MalS-derived peptide sequence
DNRNGNVYDF
-
-
DNRNGNVYFF
-
thermodynamic binding affinities of the peptide
DNRNGNVYGF
-
-
DNRNGNVYIF
-
-
DNRNGNVYKF
-
-
DNRNGNVYLF
-
thermodynamic binding affinities of the peptide
DNRNGNVYQF
-
-
DNRNGNVYSF
-
-
DNRNGNVYWF
-
-
DNRNGNVYYF
-
-
DTT
-
only when incubated in the presence of 20 mM dithiothreitol, which reduces the structural disulfide bonds and unfold the protein, and above 34C, is CtHtrA able to proteolyse alpha-lactalbumin
heparan sulfate
triggers HtrA1-induced peteriorization, overview
IVALGLVYQF
-
OmpC-derived peptide sequence
OMP C-terminal tripeptide YYF-COOH
-
activation less efficient as compared to 15 residue presenilin-1 peptide
phosphatidyl glycerol
enhances DegP proteolytic activity at high temperatures
phosphatidylglycerol
-
activates at 37-45C
puromycin
-
increases level of misfolded proteins, HtrA is required for growth under conditions in which misfolded proteins accumulate
Tyr-Tyr-Phe
tripeptide stimulates activity
-
YTMKAAGLGK
-
PhoA-derived peptide sequence
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000247
CSP-1 FRET peptide
-
pH 7.4, 37C
-
0.0346
succinyl-Leu-Leu-Val-Tyr-4-methylcoumarin 7-amide
pH 7.0, temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00021
HtrA1 inhibitor
Homo sapiens
-
pH 8.5, 37C, recombinant enzyme
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.001
-
using PMMGKASPV-4-nitroanilide as substrate, in 50 mM NaH2PO4, pH 8.0, temperature not specified in the publication
0.018
-
using PVFNTLPMMGKASPV-4-nitroanilide as substrate, in 50 mM NaH2PO4, pH 8.0, temperature not specified in the publication; using SPMFKGV-4-nitroanilide as substrate, in 50 mM NaH2PO4, pH 8.0, temperature not specified in the publication
0.032
-
using VFNTLPMMGKASPV-4-nitroanilide as substrate, in 50 mM NaH2PO4, pH 8.0, temperature not specified in the publication
0.473
-
using DPMFKLV-4-nitroanilide as substrate, in 50 mM NaH2PO4, pH 8.0, temperature not specified in the publication
79.3
-
pH 8.0, 37C
additional information
-
DegP protease exhibits a concentration effect: an 8fold increase in the concentration of DegP results in an 2.4fold increase in the specific protease activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 6
-
HtrA in the absence of Ca2+
5.5 - 6.5
-
HhoB activity shows an optimum at pH 5.5-6.5 in the presence of 10 mM Ca2+
7.6
-
protease assay
8.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8 - 10
-
proteolytic activity is largely independent of the pH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
reduced alkaline phosphatase is efficiently degraded at 20C, both in vivo and in vitro. The cleavage is most efficient in the case of a C57A/C69A mutant, lacking its internal SS bond
42
-
substrate-binding using mutant S210A and protease assay
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 85
-
at least 50% of maximum activity
20 - 30
-
almost no activity below 20C, activity rapidly increases above 30C
30 - 42
-
enzyme activity is constant within this temperature range
34 - 55
-
low activity below 34C, rapid loss of activity at 55C
37 - 44
-
the HtrA mutant forms colonies with the same frequency as the wild type at 37C and 42C, the ability of the mutant to form colonies at 44C was greatly reduced as compared to the wild type
37 - 45
37 - 55
-
activity rapidly increases with temperature
44
-
at 44 C function of DegP in mutant strain CLC198 can be complemented by HtrA2
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6
-
isoeletric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
mast cells
Manually annotated by BRENDA team
-
primary chondrocyte
Manually annotated by BRENDA team
-
alternative splice form lacing exons 3 and 7
Manually annotated by BRENDA team
-
recombinant HtrA
Manually annotated by BRENDA team
-
high level of enzyme expression in decidua capsularis specifically at the decidual-trophoblast interface where active involution occurs
Manually annotated by BRENDA team
-
high HtrA1 expression levels
Manually annotated by BRENDA team
-
the luteinizing granulosa cells of the corpus luteum express the highest levels of Htra3
Manually annotated by BRENDA team
-
alternative splice form lacing exons 3 and 7
Manually annotated by BRENDA team
-
primary cell
Manually annotated by BRENDA team
-
high HtrA1 expression levels
Manually annotated by BRENDA team
-
elevated synovial HtrA1 levels in fluids obtained from rheumatoid and osteoarthritis patients
Manually annotated by BRENDA team
-
alternative splice form lacing exons 3 and 7
Manually annotated by BRENDA team
-
HtrA1 especially expressed in giant cells during the early stages of placental development
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
intracellular HtrA1 associates with centrosomes
Manually annotated by BRENDA team
-
isoform DEG2 only
Manually annotated by BRENDA team
-
isoform HTRA1
-
Manually annotated by BRENDA team
-
Nma111p does not shuttle between the nucleus and cytoplasm
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26000
-
SDS-PAGE, protease domain
42000
-
Western blot analysis, processed protein
44840
enzyme monomer, mass spectrometry
45000
-
SDS-PAGE with coomassie staining
48000
-
SDS-PAGE
51000
-
precursor protein, SDS-PAGE
200000
-
above, gel filtration
270100
enzyme dodecamer, mass spectrometry
274000
-
sedimentation analysis
281000
-
hexameric form, gel filtration
300000
307000
-
recombinant enzyme, gel filtration
328000
-
heptameric form, gel filtration
500000
-
gel filtration, 2 forms: 300000 Da and 500000 Da
553100
enzyme tetracosamer, mass spectrometry
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decamer
-
10 * 54000, SDS-PAGE, enzyme exists in 3 different forms: pentamer, hexamer and decamer
dodecamer
heptamer
-
7 * 46000, mass spectroscopy
hexamer
homooligomer
DegP of Escherichia coli assembles into large homooligomers with an internal cavity combining both chaperone and protease activity
homotrimer
-
-
multimer
oligomer
pentamer
-
5 * 54000, SDS-PAGE, enzyme exists in 3 different forms: pentamer, hexamer and decamer
tetracosamer
trimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
mutant S266A, to 2.6 A resolution. The protein trimer contains two calcium ions in a central channel, suggesting a link between photodamage control and calcium ions in chloroplasts. Protein contains no PDZ domain and the trimeric structure reveals a catalytic triad conformation where His147 in the alternative conformation is rotated anticlockwise by 120, preventing formation of the His147-Asp188 hydrogen bond; mutant S292A, to 2.0 A resolution. Isoform Deg8 forms a hexamer in the crystals. The catalytic triad of Deg8 consists of His171, Asp214 and Ser292. In the Deg8 (S292A) structure the triad fails to form catalytically competent hydrogen bonds owing to the anticlockwise rotation of the chi1 angle of His171 by 120. His171 can form a hydrogen bond to Gln272 of loop L3
modeling of 3D structure
-
a theoretical model of the three-dimensional structure of the LA loop as per the resting state of enzyme HtrA. hydrophobic interactions connect the LA loops of the hexamer and polar contacts between the LA', i.e. the LA loop on an opposite subunit, and L1 loops on opposite subunits. Disturbance of these interactions causes the stimulation of HtrA proteolytic activity. LA loops contribute to the preservation of the integrity of the HtrA oligomer and to the stability of the monomer
-
crystal structure of the DegP24 multimer-outer membrane protein complex is solved by the single-wavelength anomalous dispersion method: The 24-mer of DegP forms a spherical shell with 432 symmetry. In the crystal structure of DegP24, eight trimers are located at the vertices of an octahedron that assembles a protein shell of about 31 A thickness enclosing a large internal cavity about 110 A in diameter
-
vapor diffusion method
-
structure determination and analysis of the 24meric enzyme with complexed substrate beta-casein, cryo-electron microscopy images and three-dimensional structures, overview
hanging drop vapor diffusion method
-
protease domain
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 25
-
low proteolytic activity is recorded for the Deg/HtrA proteases HtrA, HhoA, and HhoB at a temperature ranging from 10 to 25C
20 - 45
the proteolysis of casein at 20C is negligible, then it increases in almost linear fashion up to 45C. At the temperature range of 40-45C, the activity is approximately 1.5fold higher than at 37C
45
-
stable for at least 4 h
55 - 75
-
denaturation of the enzyme starts at 55C and ends at 75C
55
-
stable for at least 1 h
60
-
drastic decrease of activity within 5 min
70
-
1 h, 30% residual activity
additional information
-
interaction with phosphatidylgycerol leads to a remarkable decrease in the thermal stability
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme cleaves itself under reducing conditions in the presence of 2-mercaptoethanol or dithiothreitol
-
native enzyme undergoes slow self cleavage
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
90% purity
-
by Ni affinity chromatography
-
glutathione-Sepharose bead chromatography
-
HisTrap column chromatography, gel filtration
-
near homogeneity
-
Ni-NTA agarose column chromatography
Ni-NTA column chromatography
Ni-NTA column chromatography and His GraviTrap affinity column chromatography
-
recombinant His-tagged HtrA1 lacking the N-terminal insulin-like growth factor-binding protein and serine protease inhibitor domain from Escherichia coli by affinity chromatography
-
recombinant HtrA S210A mutant from overproducing strain K38
-
recombinant HtrA1 from 293-EBNA cell culture medium partially by ultrafiltration and dialysis
-
using Ni-NTA chromatography
-
wild-type, htrA22 and htrA63 mutant
-
wild-type, S210A and H105R mutant