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Information on EC 3.4.23.21 - Rhizopuspepsin
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3.4.23.21 RhizopuspepsinSpecify your search results
Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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, rhizopuspepsin, rhizopuspepsinogen, rhizopus aspartic proteinase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Aspartate protease
-
-
-
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EC 3.4.23.6
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-
formerly
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EC 3.4.23.9
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formerly
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EC 3.4.4.17
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formerly, part transferred
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EC 3.4.99.25
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formerly, part transferred
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Neurase
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-
-
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Proteinase, Rhizopus acid
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-
-
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Rhizopus acid protease
Rhizopus acid proteinase
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-
-
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Rhizopus aspartic proteinase
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-
-
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additional information
Rhizopus acid protease
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-
-
-
additional information
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the enzyme belongs to the A1 peptidase family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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
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-
-
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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
aspartate protease which requires also a His residue for catalytic activity
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
aspartic endopeptidase
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CAS REGISTRY NUMBER
COMMENTARY
9074-09-3
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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
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-
-
-
?
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
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-
-
?
KLIEF p-nitrophenylalanine-RL + H2O
KLIEF + p-nitrophenylalanine-RL
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-
-
?
KPAEF p-nitrophenylalanine-RL + H2O
KPAEF + p-nitrophenylalanine-RL
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-
-
?
KPALF p-nitrophenylalanine-RL + H2O
KPALF + p-nitrophenylalanine-RL
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-
-
?
KPDEF p-nitrophenylalanine-RL + H2O
KPDEF + p-nitrophenylalanine-RL
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-
-
?
KPIAF p-nitrophenylalanine-RL + H2O
KPIAF + p-nitrophenylalanine-RL
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-
-
?
KPIDF p-nitrophenylalanine-RL + H2O
KPIDF + p-nitrophenylalanine-RL
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-
-
?
KPIEF p-nitrophenylalanine-RL + H2O
KPIEF + p-nitrophenylalanine-RL
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-
-
?
KPILF p-nitrophenylalanine-RL + H2O
KPILF + p-nitrophenylalanine-RL
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-
-
?
KPISF p-nitrophenylalanine-RL + H2O
KPISF + p-nitrophenylalanine-RL
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-
-
?
KPLEF p-nitrophenylalanine-RL + H2O
KPLEF + p-nitrophenylalanine-RL
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-
-
?
KPREF p-nitrophenylalanine-RL + H2O
KPREF + p-nitrophenylalanine-RL
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-
-
?
KPRRPYILKRGSYYY + H2O
KPRRPYIL + KRGSYYY
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synthetic neurotensin-like peptide, cleavage site specificity
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-
?
KPSEF p-nitrophenylalanine-RL + H2O
KPSEF + p-nitrophenylalanine-RL
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-
-
?
KSIEF p-nitrophenylalanine-RL + H2O
KSIEF + p-nitrophenylalanine-RL
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-
-
?
L-Orn-L-Leu-D-Phe-L-Pro-L-Val-OH + H2O
L-Orn + L-Val + L-Leu-D-Phe-L-Pro-OH
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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
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-
-
?
Lys-Pro-Ile-Glu-Phe-(NO2)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (NO2)Phe-Arg-Leu
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-
-
?
Na-Polyglutamate + H2O
Glu + Glu-Glu + unknown compound
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-
-
?
Polylysine-HCl + H2O
Lys-Lys + Lys-Lys-Lys + higher oligolysine
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?
Z-Ala-Ala-Lys-Ala-Ala-Ala + H2O
Z-Ala-Ala-Lys + Ala-Ala-Ala
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-
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?
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
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i.e. insulin B chain, cleavage site specificity
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-
?
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
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i.e. insulin B chain, cleavage site specificity
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-
?
Oxidized insulin B-chain + H2O
Proteolytically cleaved oxidized insulin B-chain
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primarily the Leu15-Tyr16 bond and the Tyr16-Leu17 bond is hydrolyzed, additional cleavage of the bonds Ala14-Leu15 and Phe24-Phe25
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-
?
Oxidized insulin B-chain + H2O
Proteolytically cleaved oxidized insulin B-chain
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splits at twelve sites, preferentially Leu-Val, Tyr-Leu and Phe-Phe
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?
Oxidized insulin B-chain + H2O
Proteolytically cleaved oxidized insulin B-chain
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bovine insulin
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?
Oxidized insulin B-chain + H2O
Proteolytically cleaved oxidized insulin B-chain
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-
-
?
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
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-
?
Peptides + H2O
?
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specificity towards the tetradecapeptide: Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser
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?
Peptides + H2O
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role of the Asp77 in facilitating the cleavage of oligopeptide substrates with lysine in P1
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?
additional information
?
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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
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?
additional information
?
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the enzyme shows milk clotting activity with skim milk as substrate
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?
additional information
?
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very broad substrate specificity, overview
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?
additional information
?
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peptide bonds susceptible to the action of the enzyme posess mainly bulky amino acids
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?
additional information
?
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trypsinogen activation (at pH 3.4)
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?
additional information
?
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very broad substrate specificity, overview
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?
additional information
?
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very broad substrate specificity, overview
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?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ac-NA-Val-3-hydroxy 4-amino 6-methyl heptanoic acid-2-aminobutanoyl-NA-amide
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Co2+
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0.3% residual activity at 10 mM; about 36% residual activity at 10 mM
CTAB
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in the presence of CTAB, 20 and 10 % relative activities are maintained at concentrations of 0.1% (w/v) and 1% (w/v), respectively
dithiothreitol
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the peptidase shows residual activities of 50 and 40% following incubation with 100 or 150 mM dithiothreitol, respectively
guanidine
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the enzyme maintains approximately 70 and 60% of proteolytic activity at 100 and 150 mM guanidine, respectively
Peptide inhibitor
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sequence: D-His-Pro-Phe-His-Phe(Psi)[CH2-NH]Phe-Val-Tyr
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Piper hispidum essential oil
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less than 10% residual activity at 0.048 mg/ml
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Piper tmarginatum essential oil
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less than 50% residual activity at 0.048 mg/ml
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Piper tuberculatum essential oil
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less than 10% residual activity at 0.048 mg/ml
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SDS
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the peptidase maintains approximately 50 % of activity in the presence of 0.02 % (w/v) SDS andloses nearly all activity during incubation with 0.08 % (w/v) SDS
Triton X-100
-
approximately 60% residual activity at 0.2 % (v/v) Triton X-100
1,2-epoxy-3-(4-nitrophenoxy)propane
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amino acid sequence around the 1,2-epoxy-3-(4-nitrophenoxy)propane-reactive residues
Diazoacetyl-DL-norleucine methyl ester
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Cu2+ essential for this reaction
Diazoacetyl-DL-norleucine methyl ester
-
Cu2+ essential for this reaction; rate of reaction of this inhibitor with the enzyme is decreased in the presence of pepstatin; the rate of inactivation accelerates with increasing concentration of Cu2+
Diazoacetyl-DL-norleucine methyl ester
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Cu2+ essential for this reaction
additional information
-
development of petidomimetic inhibitors
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenoma
A novel aspartate protease gene, ALP56, is related to morphological features of colorectal adenomas.
Alzheimer Disease
Molecular Docking and 3D Qsar Studies of C000000956 as a Potent Inhibitor of Bace-1.
Alzheimer Disease
Multiple e-Pharmacophore Modeling Combined with High-Throughput Virtual Screening and Docking to Identify Potential Inhibitors of ?-Secretase(BACE1).
Asthma
Recognition of Fungal Protease Activities Induces Cellular Activation and Eosinophil-Derived Neurotoxin Release in Human Eosinophils.
Breast Neoplasms
Ribozyme-targeting procathepsin D and its effect on invasion and growth of breast cancer cells: an implication in breast cancer therapy.
Carcinoma
Diagnostic and Prognostic Role of Immunohistochemical Expression of Napsin-A Aspartic Peptidase in Clear Cell and Papillary Renal Cell Carcinoma: A Study Including 233 Primary and Metastatic Cases.
Carcinoma, Renal Cell
Diagnostic and Prognostic Role of Immunohistochemical Expression of Napsin-A Aspartic Peptidase in Clear Cell and Papillary Renal Cell Carcinoma: A Study Including 233 Primary and Metastatic Cases.
cathepsin l deficiency
Epidermal differentiation: the role of proteases and their inhibitors.
Chagas Disease
Aspartic Peptidases of Human Pathogenic Trypanosomatids: Perspectives and Trends for Chemotherapy.
Chagas Disease
Decoding the anti-Trypanosoma cruzi action of HIV peptidase inhibitors using epimastigotes as a model.
Chromoblastomycosis
Fonsecaea pedrosoi Sclerotic Cells: Secretion of Aspartic-Type Peptidase and Susceptibility to Peptidase Inhibitors.
Coinfection
Decoding the anti-Trypanosoma cruzi action of HIV peptidase inhibitors using epimastigotes as a model.
Colitis
Chlorogenic Acid Suppresses miR-155 and Ameliorates Ulcerative Colitis through the NF-?B/NLRP3 Inflammasome Pathway.
Colonic Neoplasms
Increased expression of cathepsin D is required for L1-mediated colon cancer progression.
Colorectal Neoplasms
A novel aspartate protease gene, ALP56, is related to morphological features of colorectal adenomas.
Insulin Resistance
Altered amyloid precursor protein processing regulates glucose uptake and oxidation in cultured rodent myotubes.
Leishmaniasis
Aspartic Peptidases of Human Pathogenic Trypanosomatids: Perspectives and Trends for Chemotherapy.
Neoplasms
A novel aspartate protease gene, ALP56, is related to morphological features of colorectal adenomas.
Neoplasms
Ribozyme-targeting procathepsin D and its effect on invasion and growth of breast cancer cells: an implication in breast cancer therapy.
Opportunistic Infections
The Widespread Anti-Protozoal Action of HIV Aspartic Peptidase Inhibitors: Focus on Plasmodium spp., Leishmania spp. and Trypanosoma cruzi.
Papillon-Lefevre Disease
Epidermal differentiation: the role of proteases and their inhibitors.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000077
Ac-NA-Nva-3-hydroxy 4-amino 6-methyl heptanoic acid-Nva-NA-amide
-
pH 3.0, 37°C
0.0000029
Ac-NA-Val-3-hydroxy 4-amino 6-methyl heptanoic acid-2-aminobutanoyl-NA-amide
-
pH 3.0, 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 65
-
the enzyme maintains around 80% activity at 40-50°C. 90 and 80% proteolytic activities are maintained at 60 and 65°C, respectively
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM