Information on EC 3.4.23.22 - Endothiapepsin

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The expected taxonomic range for this enzyme is: Cryphonectria parasitica

EC NUMBER
COMMENTARY hide
3.4.23.22
-
RECOMMENDED NAME
GeneOntology No.
Endothiapepsin
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of proteins with specificity similar to that of pepsin A; prefers hydrophobic residues at P1 and P1', but does not cleave Ala14-Leu in the B chain of insulin or Z-Glu-Tyr. Clots milk
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
aspartic endopeptidase
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CAS REGISTRY NUMBER
COMMENTARY hide
37205-60-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Endothia sp.
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Abz-Thr-Ile-Nle-4-nitro-Phe-Gln-Arg-NH2 + H2O
Abz-Thr-Ile-Nle + 4-nitro-Phe-Gln-Arg-NH2
show the reaction diagram
-
-
-
?
casein + H2O
?
show the reaction diagram
-
splits 29.0% of the peptide bonds
-
-
-
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
FVN + Gln + HLCGSHL + VEALY + LVCGERGF + FYTPKA
show the reaction diagram
-
i.e. oxidized insulin B chain, cleavage site specificity
-
-
?
kappa-casein + H2O
?
show the reaction diagram
-
reaction contributes to milk-clotting activity, cleavage site specificity for Ser104-Phe105
-
-
?
Oxidized B-chain of insulin + H2O
?
show the reaction diagram
-
the Phe24-Phe25 bond is hydrolyzed at a maximal rate followed by hydrolysis of the Tyr16-Leu17 and Gln4-His5 bonds. The Leu11-Val12 and Asn3-Gln4 bonds are hydrolyzed at slower rates. The Leu11-Val12 bond appears to be considerably more resistant to hydrolysis in the peptide 5-16 than in the intact oxidized B-chain. The Leu15-Tyr16 bond is very slowly hydrolyzed in the peptide 5-16, no hydrolysis in the intact oxidized B-chain. Phe25 is slowly hydrolyzed from the peptide 25-30 and the bond involving Gly20-Glu21 is slowly hydrolyzed in peptide 12-24 and/or peptide 17-24
-
-
-
Pepsin + H2O
?
show the reaction diagram
-
splits 8.0% of the peptide bonds
-
-
-
Rennin + H2O
?
show the reaction diagram
-
splits 10.2% of the peptide bonds
-
-
-
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
BW624
Endothia sp.
-
-
CP-80,794
-
transition state analogue inhibitor
D-Novo
Endothia sp.
-
-
H261
Endothia sp.
-
-
L363564
-
statine-containing renin inhibitor, hydrogen bonding interaction witht the enzyme, e.g. via Asp32 and Asp215, overview
Oligopeptide inhibitors
-
PD125967 and PD125754
-
PD-129,541
-
transition state analogue inhibitor
PD-130,328
-
transition state analogue inhibitor
PD-135,040
-
gem-diol inhibitor
Pepstatin
pepstatin A
Synthetic human statine-containing renin inhibitor
-
H-189
-
Synthetic polypeptide inhibitor
-
structure
-
Synthetic renin inhibitor
-
CP-69,799
-
Transition-state isostere inhibitor of renin
-
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0016
Abz-Thr-Ile-Nle-4-nitro-Phe-Gln-Arg-NH2
in 0.1 M acetate buffer, pH 4.6, containing 0.01% (v/v) Tween 20, temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000001
H189
-
pH 4.5
0.00006
H256
-
pH 4.5
0.00011
PD-130,328
-
pH 4.5
additional information
additional information
-
pepstatin inhibition kinetics and thermodynamics, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
acidic pH optimum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33800
-
x * 33800
34000 - 37500
-
Endothia parasitica, gel filtration
37000
-
x * 37000, Endothia parasitica, SDS-PAGE
additional information
-
a homologue of pepsin A; amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
structure analysis, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no carbohydrate
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
complexes of pepstatin A and a statine-containing human renin inhibitor with endothiapepsin; X-ray crystallographic analysis
-
crystal structure of enzyme bound to inhibitor Pd130328, inhibitor binding structure and analysis
-
in complex with gem-diol inhibitor PD-135,040, hanging-drop vapour-diffusion method, space group P2(1), unit-cell parameters a : 53.20, b : 73.25, c : 46.00
-
of inhibition of endothiapepsin by cyclohexyl renin inhibitors; X-ray crystallographic analysis
-
of the complex between endothiapepsin and an oligopeptide inhibitor
-
sitting drop vapor diffusion method, using 0.1 M NH4Ac, 0.1 M acetate buffer, pH 4.6, and 26% (w/v) PEG 4000
space group P2(1), in complex with H189 unit cell parameters a : 42.48, b : 75.78, c : 42.99, in complex with CP-80,794 unit cell parameters a : 42.55, b : 74.62, c : 44.43, in complex with CP-129,541 unit cell parameters a : 42.47, b : 74.31, c : 42.81, in complex with PD-130,328 unit cell parameters a : 43.88, b : 75.44, c : 43.23, in complex with H256 unit cell parameters a : 43.88, b : 75.44, c : 43.23
-
three-dimensional structure of endothiapepsin complexed with a transition-state isostere inhibitor of renin
-
using ammonium sulfate as precipitant at pH 4.6, X-ray diffraction structure determination and analysis at 2.1 A resolution, multiple isomorphous replacement
-
-
Endothia sp.
-
complexed with H261, crystals grow in two different crystal forms with the same monoclinic sopace group, P2(1), unit cell parameters a : 43.0A, b : 75.7A, c : 42.9A
Endothia sp.
-
structure studied by neutron crystallography, crystals are monocliic, P2(1), unit cell dimensions a : 43.1 A, b : 75.7 A, c : 42.9 A, endothiapepsin-H261 complex
Endothia sp.
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.8 - 4.5
-
50°C, maximal stability, 30% loss of activity after 30 min
30629
6.5
-
rapid loss of activity above
30629
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Enzyme solution equilibrated against 0.01 M acetate buffer, pH 4.6, and frozen at -25°C to -30°C, may be lyophilized with no loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
nutrition
-
the enzyme can be used as a fungal rennet in cheese production