3.4.23.22: Endothiapepsin

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

Reaction

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 =

Synonyms

Aspartate protease, Aspartic proteinase, EC 3.4.23.10, EC 3.4.23.6, EC 3.4.4.17, Endothia acid proteinase, Endothia aspartic proteinase, Endothia parasitica acid proteinase, Endothia parasitica aspartic proteinase, Proteinase, Endothia aspartic

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.23 Aspartic endopeptidases

                3.4.23.22 Endothiapepsin

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Results	in table
2	AA Sequence
3	Application
1	CAS Registry Number
1	Cloned(Commentary)
18	Crystallization (Commentary)
1	General Stability
23	IC50 Value
66	Inhibitors
12	Ki Value [mM]
2	KM Value [mM]
6	Molecular Weight [Da]
29	Organism
780	PDB ID
3	pH Optimum
2	pH Stability
1	pI Value
1	Posttranslational Modification
4	Purification (Commentary)
3	Reaction
1	Reaction Type
29	Reference
2	Specific Activity [micromol/min/mg]
11	Substrates and Products (Substrate)
4	Subunits
10	Synonyms
1	Temperature Optimum [°C]

Substrates Products

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Substrates Products on EC 3.4.23.22 - Endothiapepsin

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SUBSTRATE

PRODUCT                       

REACTION DIAGRAM

ORGANISM

UNIPROT

COMMENTARY
(Substrate)

LITERATURE
(Substrate)

COMMENTARY
(Product)

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

Cryphonectria parasitica

P11838

-

717977, 753901, 754611

-

-

?

casein + H2O

?

Cryphonectria parasitica

-

splits 29.0% of the peptide bonds

30629

-

-

?

FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O

FVN + Gln + HLCGSHL + VEALY + LVCGERGF + FYTPKA

Cryphonectria parasitica

-

i.e. oxidized insulin B chain, cleavage site specificity

668786

-

-

?

kappa-casein + H2O

?

Cryphonectria parasitica

-

reaction contributes to milk-clotting activity, cleavage site specificity for Ser104-Phe105

668786

-

-

?

Oxidized B-chain of insulin + H2O

?

Cryphonectria parasitica

-

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

30630

-

-

?

Pepsin + H2O

?

Cryphonectria parasitica

-

splits 8.0% of the peptide bonds

30629

-

-

?

Rennin + H2O

?

Cryphonectria parasitica

-

splits 10.2% of the peptide bonds

30629

-

-

?

additional information

?

-

2 entries

additional information

?

-

Cryphonectria parasitica

-

clots milk, not: benzyloxycarbonyl-L-Glu-L-Tyr

30629

-

-

?

additional information

?

-

Cryphonectria parasitica

-

the enzyme prefers protein substrates with hydrophobic amino acid residues at P1 and P1' positions

668786

-

-

?