3.4.23.21: Rhizopuspepsin
This is an abbreviated version!
For detailed information about Rhizopuspepsin, go to the full flat file.
Word Map on EC 3.4.23.21
Reaction
hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1'. Clots milk and activates trypsinogen. Does not cleave Gln4-His, but does cleave His10-/-Leu and Val12-/-Glu in B chain of insulin =
Synonyms
Aspartate protease, aspartic peptidase, EC 3.4.23.6, EC 3.4.23.9, EC 3.4.4.17, EC 3.4.99.25, More, Neurase, Proteinase, Rhizopus acid, Rhizopus acid protease, Rhizopus acid proteinase, Rhizopus aspartic proteinase, rhizopuspepsinogen
ECTree
3.4.23.21 RhizopuspepsinAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.4.23.21 - Rhizopuspepsin
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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
Ac-Ala-Ala-Lys-(4-nitro)Phe-Ala-Ala + H2O
Ac-Ala-Ala-Lys + (4-nitro)Phe-Ala-Ala
-
-
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
L-Phe + VNQH + LCGSH + L-Leu + L-Val + L-Glu + L-Ala + L-Leu + L-Tyr + LVCG + ERG + L-Phe + L-Phe + YTPKA
KAIEF p-nitrophenylalanine-RL + H2O
KAIEF + p-nitrophenylalanine-RL
-
-
-
?
KLIEF p-nitrophenylalanine-RL + H2O
KLIEF + p-nitrophenylalanine-RL
-
-
-
?
KPAEF p-nitrophenylalanine-RL + H2O
KPAEF + p-nitrophenylalanine-RL
-
-
-
?
KPALF p-nitrophenylalanine-RL + H2O
KPALF + p-nitrophenylalanine-RL
-
-
-
?
KPDEF p-nitrophenylalanine-RL + H2O
KPDEF + p-nitrophenylalanine-RL
-
-
-
?
KPIAF p-nitrophenylalanine-RL + H2O
KPIAF + p-nitrophenylalanine-RL
-
-
-
?
KPIDF p-nitrophenylalanine-RL + H2O
KPIDF + p-nitrophenylalanine-RL
-
-
-
?
KPIEF p-nitrophenylalanine-RL + H2O
KPIEF + p-nitrophenylalanine-RL
-
-
-
?
KPILF p-nitrophenylalanine-RL + H2O
KPILF + p-nitrophenylalanine-RL
-
-
-
?
KPISF p-nitrophenylalanine-RL + H2O
KPISF + p-nitrophenylalanine-RL
-
-
-
?
KPLEF p-nitrophenylalanine-RL + H2O
KPLEF + p-nitrophenylalanine-RL
-
-
-
?
KPREF p-nitrophenylalanine-RL + H2O
KPREF + p-nitrophenylalanine-RL
-
-
-
?
KPRRPYILKRGSYYY + H2O
KPRRPYIL + KRGSYYY
-
synthetic neurotensin-like peptide, cleavage site specificity
-
-
?
KPSEF p-nitrophenylalanine-RL + H2O
KPSEF + p-nitrophenylalanine-RL
-
-
-
?
KSIEF p-nitrophenylalanine-RL + H2O
KSIEF + p-nitrophenylalanine-RL
-
-
-
?
L-Orn-L-Leu-D-Phe-L-Pro-L-Val-OH + H2O
L-Orn + L-Val + L-Leu-D-Phe-L-Pro-OH
-
open chain of gramicidin S that is prepared by the treatment of gramicidin S with Bacillus subtilis alkaline protease
-
?
Lys-Pro-Ala-Lys-Phe-(NO2)Phe-Arg-Leu + H2O
Lys-Pro-Ala-Lys-Phe + (NO2)Phe-Arg-Leu
-
-
-
?
Lys-Pro-Ile-Glu-Phe-(NO2)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (NO2)Phe-Arg-Leu
-
-
-
?
Na-Polyglutamate + H2O
Glu + Glu-Glu + unknown compound
-
-
-
?
Polylysine-HCl + H2O
Lys-Lys + Lys-Lys-Lys + higher oligolysine
-
-
-
?
Z-Ala-Ala-Lys-Ala-Ala-Ala + H2O
Z-Ala-Ala-Lys + Ala-Ala-Ala
-
-
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
L-Phe + VNQH + LCGSH + L-Leu + L-Val + L-Glu + L-Ala + L-Leu + L-Tyr + LVCG + ERG + L-Phe + L-Phe + YTPKA
-
i.e. insulin B chain, cleavage site specificity
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
L-Phe + VNQH + LCGSH + L-Leu + L-Val + L-Glu + L-Ala + L-Leu + L-Tyr + LVCG + ERG + L-Phe + L-Phe + YTPKA
-
i.e. insulin B chain, cleavage site specificity
-
-
?
Oxidized insulin B-chain + H2O
Proteolytically cleaved oxidized insulin B-chain
-
primarily the Leu15-Tyr16 bond and the Tyr16-Leu17 bond is hydrolyzed, additional cleavage of the bonds Ala14-Leu15 and Phe24-Phe25
-
-
?
Oxidized insulin B-chain + H2O
Proteolytically cleaved oxidized insulin B-chain
-
splits at twelve sites, preferentially Leu-Val, Tyr-Leu and Phe-Phe
-
?
Oxidized insulin B-chain + H2O
Proteolytically cleaved oxidized insulin B-chain
-
bovine insulin
-
?
Oxidized insulin B-chain + H2O
Proteolytically cleaved oxidized insulin B-chain
-
-
-
?
Peptides + H2O
?
-
in these examples the term -+- depicts the points of cleavage: Lys-+-Tyr-+-Glu-OH, benzyloxycarbonyl-Glu-+-Tyr-OH, benzyloxycarbonyl-Phe-+-Tyr-OH, benzyloxycarbonyl-Leu-+-Tyr-OH, Gly-Glu-+-Tyr-OH, benzyloxycarbonyl-Glu-+-Tyr-OH, Leu-Tyr-OH, Glu-Tyr-OH, benzyloxycarbonyl-Gly-+-Phe-OH, benzyloxycarbonyl-Glu-+-Phe-OH, Leu-Gly-+-Phe-OHGlu-Gly-+-Phe-OH, Leu-Phe-OH
-
-
?
Peptides + H2O
?
-
specificity towards the tetradecapeptide: Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser
-
-
?
Peptides + H2O
?
-
role of the Asp77 in facilitating the cleavage of oligopeptide substrates with lysine in P1
-
-
?
additional information
?
-
-
the coagulant activity of the peptidase is higher than the proteolytic activity and there is a preference for aromatic, basic, and nonpolar amino acids, particularly methionine, with specific cleavage of the peptide bond between phenylalanine and methionine
-
-
?
additional information
?
-
-
the enzyme shows milk clotting activity with skim milk as substrate
-
-
?
additional information
?
-
-
very broad substrate specificity, overview
-
-
?
additional information
?
-
-
peptide bonds susceptible to the action of the enzyme posess mainly bulky amino acids
-
-
?
additional information
?
-
-
trypsinogen activation (at pH 3.4)
-
-
?
additional information
?
-
-
very broad substrate specificity, overview
-
-
?
additional information
?
-
-
very broad substrate specificity, overview
-
-
?
