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Information on EC 3.4.23.19 - Aspergillopepsin II
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EC Tree
3.4.23.19 Aspergillopepsin IISpecify your search results
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Reaction Schemes
preferential cleavage in B chain of insulin: Asn3-/-Gln, Gly13-/-Ala, Tyr26-/-Thr
Synonyms
acid proteinase, aspergillopepsin ii, acid proteinase a, aspergilloglutamic peptidase, non-pepsin type acid proteinase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aspergilloglutamic peptidase
Aspergillus niger var. macrosporus aspartic proteinase
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EC 3.4.23.6
Proctase A
Proteinase A
additional information
EC 3.4.23.6
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formerly
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Proctase A
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Proteinase A
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-
additional information
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the enzyme belongs to the A4 peptidase family
additional information
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the enzyme belongs to the G1 peptidase family
additional information
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the enzyme belongs to the G1 peptidase family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
preferential cleavage in B chain of insulin: Asn3-/-Gln, Gly13-/-Ala, Tyr26-/-Thr
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preferential cleavage in B chain of insulin: Asn3-/-Gln, Gly13-/-Ala, Tyr26-/-Thr
catalytic residues are Glu219 and Glu133, numbering from the preproform, Glu219 and Glu133 form a catalytic dyad
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preferential cleavage in B chain of insulin: Asn3-/-Gln, Gly13-/-Ala, Tyr26-/-Thr
catalytic residues are GluB110 and GluB24, catalytic mechanism
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preferential cleavage in B chain of insulin: Asn3-/-Gln, Gly13-/-Ala, Tyr26-/-Thr
catalytic residues are GluB110 and GluB24, detailed catalytic mechanism, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY
9025-49-4
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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
Hemoglobin + H2O
Hydrolyzed hemoglobin
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acid denatured hemoglobin
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?
oxidized insulin B chain + H2O
FVN + QHLCGSHLVE + ALYLVCGERGFFY + TPKA
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substrate from Bos taurus, cleavage site specificity
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-
?
oxidized pancreatic ribonuclease A + H2O
?
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substrate from Bos taurus
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-
?
Oxidized insulin B-chain + H2O
Hydrolyzed insulin B-chain
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major cleavage sites: Asn3-Gln4, Glu13-Ala14, Tyr26-Thr27, minor site: Gly20-Glu21
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-
?
Oxidized insulin B-chain + H2O
Hydrolyzed insulin B-chain
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major cleavage sites: Asn3-Gln4, Glu13-Ala14, Tyr26-Thr27, minor site: Gly20-Glu21
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?
additional information
?
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enzyme seems to cleave only peptides which contain large residues at p2 site, hardly influenced by the charges of the residues
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?
additional information
?
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the enzyme is a non-pepsin-type acid proteinase, and shows a primary specificity for Tyr, Phe, His, Asn, Asp, Gln, and Glu at P1 position, cleavage site specificity overview
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?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
synthetic propeptides
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wild-type sequence Ala1-Asn41 and diverse truncated or mutated propeptides, overview, Ala1-Asn41 shows specific competitive inhibition, while mutants, especially R19A and H20A, show weak inhibitory effects, detailed overview
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Diazoacetyl-DL-norleucine methyl ester
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in the presence of Cu2+; pH-profile
additional information
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no inhibition by diisopropyl fluorophosphate; no inhibition by pepstatin
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additional information
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insensitive to pepstatin, diazoacetyl-DL-norleucine methyl ester, and 1,2-epoxy-3-(p-nitrophenoxy)propane
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additional information
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no inhibition by pepstatin, DAN, and 1.2-epoxy-3-(4-nitrophenoxy)propane
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acromegaly
Human nasal septal cartilage: local distribution of different enzyme activities in healthy adults and acromegalic patients.
Aspergillosis
Investigation of extracellular elastase, acid proteinase and phospholipase activities as putative virulence factors in clinical isolates of Aspergillus species.
Brain Diseases
[Ammonia release and binding processes and the activity of acid proteinase and glycolysis enzymes in the dynamics of experimental toxic adrenal encephalopathy]
Breast Neoplasms
A lysosomal pepstatin-insensitive proteinase as a novel biomarker for breast carcinoma.
Breast Neoplasms
Cathepsin D expression levels in nongynecological solid tumors: clinical and therapeutic implications.
Candidiasis
Scanning electron microscopy of epidermal adherence and cavitation in murine candidiasis: a role for Candida acid proteinase.
Candidiasis
Serotype distribution and secretory acid proteinase activity of Candida albicans isolated from the oral mucosa of patients with denture stomatitis.
Candidiasis, Oral
Serotype distribution and secretory acid proteinase activity of Candida albicans isolated from the oral mucosa of patients with denture stomatitis.
Candidiasis, Oral
[Experimental oral candidiasis in healthy and immunocompromised BALB/c mice].
Candidiasis, Vulvovaginal
Fluorometric determination of acid proteinase activity in Candida albicans strains from diabetic patients with vulvovaginal candidiasis.
Carcinoma
Activities of proteinases and of a proteinase B inhibitor in tumors of the human uterus.
Carcinoma, Hepatocellular
Multiple forms of basic fibroblast growth factor: amino-terminal cleavages by tumor cell- and brain cell-derived acid proteinases.
Encephalomyelitis, Autoimmune, Experimental
Lysosomal enzymes in experimental allergic encephalomyelitis: time course and evidence of the source.
Hepatitis C
Localization of hepatitis C virus RNA in human liver biopsies by in situ hybridization using thymine-thymine dimerized oligo DNA probes: improved method.
Hypotension
Intramucosal activation of pepsinogens in the pathogenesis of acute gastric erosions and their prevention by the potent semisynthetic amphipathic inhibitor pepstatinyl-glycyl-lysyl-lysine.
Infections
Expression of extracellular acid proteinase by proteolytic Candida spp. during experimental infection of oral mucosa.
Infections
[Investigation of acid proteinase and phospholipase activity as virulence factors in clinical Aspergillus spp. isolates].
Multiple Sclerosis
Acid proteinase activity of white matter and plaques in multiple sclerosis.
Multiple Sclerosis
Lysosomal hydrolases in cerebrospinal fluid of multiple sclerosis patients. A follow-up study.
Multiple Sclerosis
Proteolytic enzyme activity of blood leukocytes and cerebrospinal fluid in multiple sclerosis.
Multiple Sclerosis
The quantitative histochemistry of multiple sclerosis plaques: acid proteinase and other acid hydrolases.
Multiple Sclerosis
[Activation of acid proteinase from rat brain in presence of blood serum from patients with multiple sclerosis and schizophrenia in in vitro experiments]
Neoplasms
Activities of proteinases and of a proteinase B inhibitor in tumors of the human uterus.
Neoplasms
Cathepsin D expression levels in nongynecological solid tumors: clinical and therapeutic implications.
Neoplasms
Changes in the dipeptidase and acid proteinase activities in blood plasma of mice carrying ascites tumors.
Psoriasis
[Change in the activity of acid proteinase and deoxyribonuclease II of blood serum in psoriasis]
Sarcoma
[Proteinases in the muscles of embryos and hens and and in transplantable muscle sarcoma]
Shwartzman Phenomenon
Inhibition of the local hemorrhagic Shwartzman reaction by an acid proteinase.
Starvation
Hormonal and nutritional substrate control of cardiac lysosomal enzyme activities.
Starvation
Lysosomal enzyme activities in muscle following starvation and refeeding in the saithe Pollachius virens L.
Stomach Neoplasms
Conversion of cathepsin E to enzymatic unstable form in gastric cancer cells.
Stomatitis, Denture
Serotype distribution and secretory acid proteinase activity of Candida albicans isolated from the oral mucosa of patients with denture stomatitis.
Vaginitis
Isolation, acid proteinase secretion, and experimental pathogenicity of Candida parapsilosis from outpatients with vaginitis.
Virus Diseases
Astrocytosis and cathepsin D activity in experimental measles encephalomyelitis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
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kinetics, thermodynamics, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
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inhibition kinetics of truncated or mutated propeptides, detailed overview
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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activities of wild-type and mutant enzymes, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
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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proctase powder, crude enzyme powder from waters of Koji cultures
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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the enzyme is secreted
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brenda
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PRTA_ASPNG
282
0
29887
Swiss-Prot
Secretory Pathway (Reliability: 3)
Q8X1C5_TALEM
147
0
15373
TrEMBL
Mitochondrion (Reliability: 5)
B8M952_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
274
0
28652
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0E3Q650_9EURY
271
0
29107
TrEMBL
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Q8X1C6_TALEM
264
0
27438
TrEMBL
Secretory Pathway (Reliability: 3)
A2R6E9_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
265
0
27860
TrEMBL
Secretory Pathway (Reliability: 3)
A2QM02_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
310
0
32362
TrEMBL
Mitochondrion (Reliability: 3)
A0A0F4YW02_TALEM
314
0
32880
TrEMBL
Secretory Pathway (Reliability: 3)
A0A8J8WKE7_9EURO
271
0
28482
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8J8VY82_9EURO
277
0
29063
TrEMBL
Secretory Pathway (Reliability: 5)
A2Q7F7_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
282
0
29979
TrEMBL
Secretory Pathway (Reliability: 2)
A2R370_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
279
0
29843
TrEMBL
Secretory Pathway (Reliability: 4)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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primary, secondary, and tertiary structure analysis, overview
additional information
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secondary and three-dimensional structure determination and analysis, two-fold symmetry, the enzyme consists of a C-terminal light and an N-terminal heavy chain
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
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the zymogen is autocatalytically activated under acidic conditions to the mature enzyme with a two-chain structure. The major pathway of activation includes initial fast cleavage at Glu12-Ala13, followed by stepwise cleavages in the N-terminal and intervening propeptide regions. The same activation profile is obtained with the recombinant zymogen lacking the N-terminal 12-aa sequence
proteolytic modification
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the enzyme is synthesized as preproform and performs autoprocessing to the mature enzyme
proteolytic modification
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the enzyme is synthesized as preproform and performs autoprocessing to the mature enzyme removing the 41-amino acid propeptide and an 11-amino acid intervening peptide
proteolytic modification
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the enzyme is synthesized as preproform and performs autoprocessing to the mature enzyme removing the 41-amino acid propeptide and an 11-amino acid intervening peptide, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme, 100 mg/ml protein in 1.4 M ammonium sulfate, 5% v/v dimethyl sulfoxide, 50 mM glycine, pH 2.1, hanging drop vapour diffusion method, X-ray diffraction structure determination and analysis at 1.4 A resolution, modeling
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D123E/E219D
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site-directed mutagenesis, weak activity against acid-denatured hemoglobin
D125N
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site-directed mutagenesis, markedly active toward acid-denatured hemoglobin
D137N
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site-directed mutagenesis, markedly active toward acid-denatured hemoglobin
D148N
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site-directed mutagenesis, markedly active toward acid-denatured hemoglobin
D160N
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site-directed mutagenesis, markedly active toward acid-denatured hemoglobin
D170N
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site-directed mutagenesis, markedly active toward acid-denatured hemoglobin
D220N
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site-directed mutagenesis, markedly active toward acid-denatured hemoglobin
E152Q
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site-directed mutagenesis, markedly active toward acid-denatured hemoglobin
E189Q
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site-directed mutagenesis, markedly active toward acid-denatured hemoglobin
E222Q
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site-directed mutagenesis, markedly active toward acid-denatured hemoglobin
D123N
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E219A
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site-directed mutagenesis, proform mutant, inactive mutant
E219Q
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site-directed mutagenesis, proform mutant, inactive mutant
N213A
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site-directed mutagenesis, proform mutant, the mutant shows reduced activity compared to the wild-type enzyme
N65A
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site-directed mutagenesis, proform mutant, the mutant shows increased activity compared to the wild-type enzyme
Q133A
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site-directed mutagenesis, proform mutant, inactive mutant
Q133E
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site-directed mutagenesis, proform mutant, inactive mutant
Q133E/E219Q
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site-directed mutagenesis, proform mutant, inactive mutant
S162A
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site-directed mutagenesis, proform mutant, the mutant shows reduced activity compared to the wild-type enzyme
S167A
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site-directed mutagenesis, proform mutant, the mutant shows reduced activity compared to the wild-type enzyme
T126A
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site-directed mutagenesis, proform mutant, the mutant shows reduced activity compared to the wild-type enzyme
T134A
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site-directed mutagenesis, proform mutant, the mutant shows similar activity compared to the wild-type enzyme
T192A
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site-directed mutagenesis, proform mutant, the mutant shows increased activity compared to the wild-type enzyme
T268A
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site-directed mutagenesis, proform mutant, the mutant shows reduced activity compared to the wild-type enzyme
Y151F
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site-directed mutagenesis, proform mutant, the mutant shows reduced activity compared to the wild-type enzyme
Y154F
-
site-directed mutagenesis, proform mutant, the mutant shows reduced activity compared to the wild-type enzyme
Y291F
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site-directed mutagenesis, proform mutant, the mutant shows reduced activity compared to the wild-type enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
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stable up to, unstable above with rapid irreversible inactivation
668805
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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the propeptide stabilizes the enzyme against thermal inactivation
additional information
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thermal stability overview, kinetics, thermodynamics, thermal unfolding is reversible at pH 5.0-6.0, overview, the wild-type propeptide stabilizes the enzyme, effects of truncated or mutated propeptides, overview
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native extracellular enzyme from culture medium by ammonium sulfate fractionation, sulfoethyl resin chromatography, and repeated anion exchange chromatography
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recombinant wild-type and mutant enzymes including denaturation and refolding
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression in Escherichia coli
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes, denaturation by 8 M urea, refolding after dialysis in 50 mM sodium acetate, pH 5.3, 10 mM 2-mercaptoethanol, at 4°C overnight
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tanaka, N.; Takeuchi, M.; Ichishima, E.
Purification of an acid proteinase from Aspergillus saitoi and determination of peptide bond specificity
Biochim. Biophys. Acta
485
406-416
1977
Aspergillus niger
brenda
Chang, W.Y.; Horiuchi, S.; Takahashi, K.; Yamasaki, M.; Yamada, Y.
The structure and function of acid proteases. VI. Effects of acid protease-specific inhibitors on the acid proteases from Aspergillus niger var. macrosporus
J. Biochem.
80
975-981
1976
Aspergillus niger
brenda
Iio, K.; Yamasaki, M.
Specificity of acid proteinase A from Aspergillus niger var. macrosporus towards B-chain of performic acid oxidized bovine insulin
Biochim. Biophys. Acta
429
912-924
1976
Aspergillus niger
brenda
Tanokura, M.; Sasaki, H.; Muramatsu, T.; Iwata, S.; Hamaya, T.; Takizawa, T.; Takahashi, K.
A new crystal form of proteinase A, a non-pepsin-type acid proteinase from Aspergillus niger var. macrosporus
J. Biochem.
114
457-458
1993
Aspergillus niger
brenda
Takahashi, K.; Kagami, N.; Huang, X.P.; Kojima, M.; Inoue, H.
Aspergillus niger acid proteinase A. Structure and function
Adv. Exp. Med. Biol.
436
275-282
1998
Aspergillus niger
brenda
Komatsu, S.; Nishii, W.; Sasaki, H.; Muramatsu, T.; Tanokura, M.
Substrate specificity of non-pepsin-type acid proteinase, Aspergillus niger proteinase A
Adv. Exp. Med. Biol.
436
345-348
1998
Aspergillus niger
brenda
Maeda, M.; Takeuchi, K.; Kojima, M.; Tanokura, M.; Kimura, K.; Amemiya, Y.; Kihara, H.; Takahashi, K.
Kinetic studies of unfolding process of aspergillopepsin II by pH-jump methods
Biochem. Biophys. Res. Commun.
301
745-750
2003
Aspergillus niger
brenda
Kojima, M.; Tanokura, M.; Maeda, M.; Kimura, K.; Amemiya, Y.; Kihara, H.; Takahashi, K.
pH-dependent unfolding of aspergillopepsin II studied by small-angle X-ray scattering
Biochemistry
39
1364-1372
2000
Aspergillus niger
brenda
Takahashi, K.
The specificity of peptide bond cleavage of acid proteinase A from Aspergillus niger var. macrosporus toward oxidized ribonuclease A
Biosci. Biotechnol. Biochem.
61
381-383
1997
Aspergillus niger
brenda
Huang, X.P.; Kagami, N.; Inoue, H.; Kojima, M.; Kimura, T.; Makabe, O.; Suzuki, K.; Takahashi, K.
Identification of a glutamic acid and an aspartic acid residue essential for catalytic activity of aspergillopepsin II, a non-pepsin type acid proteinase
J. Biol. Chem.
275
26607-26614
2000
Aspergillus niger
brenda
Yabuki, Y.; Kubota, K.; Kojima, M.; Inoue, H.; Takahashi, K.
Identification of a glutamine residue essential for catalytic activity of aspergilloglutamic peptidase by site-directed mutagenesis
FEBS Lett.
569
161-164
2004
Aspergillus niger var. macrosporus
brenda
Takahashi, K.
Aspergillopepsin II
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
221-224
2004
Aspergillus niger var. macrosporus
-
brenda
Kubota, K.; Nishii, W.; Kojima, M.; Takahashi, K.
Specific inhibition and stabilization of aspergilloglutamic peptidase by the propeptide. Identification of critical sequences and residues in the propeptide
J. Biol. Chem.
280
999-1006
2005
Aspergillus niger var. macrosporus
brenda
Sasaki, H.; Nakagawa, A.; Muramatsu, T.; Suganuma, M.; Sawano, Y.; Kojima, M.; Kubota, K.; Takahashi, K.; Tanokura, M.
The three-dimensional structure of aspergilloglutamic peptidase from Aspergillus niger
Proc. Jpn. Acad. Ser. B
80
435-438
2004
Aspergillus niger var. macrosporus
-
brenda
Sasaki, H.; Kojima, M.; Sawano, Y.; Kubota, K.; Suganuma, M.; Muramatsu, T.; Takahashi, K.; Tanokura, M.
A proposed catalytic mechanism of aspergilloglutamic peptidase from Aspergillus niger
Proc. Jpn. Acad. Ser. B
81
441-446
2005
Aspergillus niger var. macrosporus
-
brenda
Huang, X.P.; Yabuki, Y.; Kojima, M.; Inoue, H.; Takahashi, K.
Activation profiles of the zymogen of aspergilloglutamic peptidase
Biol. Chem.
388
129-133
2007
Aspergillus niger
brenda
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