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Information on EC 3.4.23.42 - thermopsin and Organism(s) Sulfolobus acidocaldarius and UniProt Accession P17118

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.42 thermopsin
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This record set is specific for:
Sulfolobus acidocaldarius
UNIPROT: P17118 not found.
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Word Map
The taxonomic range for the selected organisms is: Sulfolobus acidocaldarius
The expected taxonomic range for this enzyme is: Archaea, Eukaryota
Reaction Schemes
similar in specificity to pepsin A preferring bulky hydrophobic amino acids in P1 and P1'
Synonyms
mtp-1, thermopsin, ssmtp, sso1175, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the enzyme belongs to the A5 peptidase family
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
similar in specificity to pepsin A preferring bulky hydrophobic amino acids in P1 and P1'
show the reaction diagram
prefers large hydrophobic residues at both sides of the scissile bond
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
126125-05-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Hemoglobin + H2O
?
show the reaction diagram
-
-
-
?
Bovine serum albumin + H2O
?
show the reaction diagram
-
-
-
-
?
carbonic anhydrase + H2O
?
show the reaction diagram
-
-
-
-
?
chicken egg albumin + H2O
?
show the reaction diagram
-
-
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
FVNQHLCGSHL + VEAL + YLVCGERGF + L-Phe + YTPKA
show the reaction diagram
-
substrate insulin B chain
-
-
?
glyceraldehyde-3-phosphate dehydrogenase + H2O
?
show the reaction diagram
-
-
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
?
Lys-Pro-Ala-Glu-Phe-(4-nitro)Phe-Ala-Leu + H2O
Lys-Pro-Ala-Glu-Phe + (4-nitro)Phe-Ala-Leu
show the reaction diagram
Lys-Pro-Ala-Glu-Phe-Nph-Ala-Leu + H2O
Lys-Pro-Ala-Glu-Phe + Nph-Ala-Leu
show the reaction diagram
-
synthetic chromogenic substrate
-
-
?
ovalbumin + H2O
?
show the reaction diagram
-
-
-
-
?
oxidized insulin B + H2O
?
show the reaction diagram
-
following bonds are hydrolyzed: Leu-Val, Leu-Tyr, Phe-Phe, Phe-Tyr, Tyr-Thr
-
-
?
Protein + H2O
?
show the reaction diagram
-
in growth medium
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
?
Protein + H2O
?
show the reaction diagram
-
in growth medium
-
-
?
additional information
?
-
-
the enzyme shows a broad protein substrate specificity, it is involved in supply of nutrients from protein substrates
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-epoxy-3-(4-nitrophenoxy)propane
-
inactivation
1,2-epoxy-3-(p-nitrophenoxy)propane
-
-
diazoacetyl-DL-norleucine
-
-
Diazoacetyl-DL-norleucine methyl ester
-
i.e. DAN, inactivation
HgCl2
-
reversible by 2-mercaptoethanol
Mercuric acetate
-
-
pepstatin A
-
competitive inhibition
phenylalaninamide
-
-
additional information
-
no inhibition by iodoacetate and 4-chloromercuribenzoate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.053
Lys-Pro-Ala-Glu-Phe-(4-nitro)Phe-Ala-Leu
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
400
acetamide
-
-
0.00012 - 0.00049
pepstatin A
10
phenylalaninamide
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.3 - 3.7
pH 1.3: about 60% of maximal activity, pH 3.7: about 55% of maximal activity
0 - 12
-
activity range, highest activity at pH 1.0- pH 5.0, substrate hemoglobin
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 80
-
substrate hemoglobin
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 100
60°C: about 30% of maximal activity, 100°C: about 70% of maximal activity
0 - 100
-
activity range, substrate hemoglobin, slow activity increase between 26°C and 65°C, rapid increase above 65°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
precursor
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
optimal cell cultivation at pH 2.0 and 70°C
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
attached to the cell suface
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32651
1 * 32651, calculated from sequence
46000
gel filtration
51000
1 * 51000, SDS-PAGE
32651
-
x * 32651, amino acid sequence calculation, x * 46000-51000, glycosylated enzyme
46000
gel filtration
51000
1 * 51000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
?
-
x * 32651, amino acid sequence calculation, x * 46000-51000, glycosylated enzyme
monomer
1 * 51000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
the enzyme has 11 potential glycosylation sites, e.g. at Asn24 and Asn28
side-chain modification
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
pH 4.5, 48 h, stable
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
80°C, 48 hours, pH 4.5
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, several months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from cell culture by solubilization with detergents, ultrafiltration and five chromatographic steps to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Baculovirus/Sf9 cells
-
expression in Escherichia coli
-
expression in Escherichia coli inclusion bodies, expression in insect cells
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli inclusion bodies by treatment with 8 M urea, incubation in acid solution, and gel filtration
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fusek, M.; Lin, X.L.; Tang, J.
Enzymic properties of thermopsin
J. Biol. Chem.
265
1496-1501
1990
Sulfolobus acidocaldarius
Manually annotated by BRENDA team
Lin, X.L.; Tang, J.
Purification, characterization, and gene cloning of thermopsin, a thermostable acid protease from Sulfolobus acidocaldarius
J. Biol. Chem.
265
1490-1495
1990
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius (P17118)
Manually annotated by BRENDA team
Lin, X.; Tang, J.
Thermopsin
Methods Enzymol.
248
156-168
1995
Sulfolobus acidocaldarius
Manually annotated by BRENDA team
Lin, X.; Liu, M.; Tang, J.
Heterologous expression of thermopsin, a heat-stable acid proteinase
Enzyme Microb. Technol.
14
696-701
1992
Sulfolobus acidocaldarius
Manually annotated by BRENDA team
Lin, X.; Fusek, M.; Tang, J.
Thermopsin, a thermostable acid protease from Sulfolobus acidocaldarius
Adv. Exp. Med. Biol.
306
255-257
1991
Sulfolobus acidocaldarius
Manually annotated by BRENDA team
Tang, J.; Lin, X.
Thermopsin
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
225-227
2004
Sulfolobus acidocaldarius
-
Manually annotated by BRENDA team