BRENDA - Enzyme Database show
show all sequences of 3.4.23.42

Enzymic properties of thermopsin

Fusek, M.; Lin, X.L.; Tang, J.; J. Biol. Chem. 265, 1496-1501 (1990)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
1,2-epoxy-3-(p-nitrophenoxy)propane
-
Sulfolobus acidocaldarius
acetamide
-
Sulfolobus acidocaldarius
diazoacetyl-DL-norleucine
-
Sulfolobus acidocaldarius
HgCl2
reversible by 2-mercaptoethanol
Sulfolobus acidocaldarius
pepstatin
-
Sulfolobus acidocaldarius
phenylalaninamide
-
Sulfolobus acidocaldarius
Urea
-
Sulfolobus acidocaldarius
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.053
-
Lys-Pro-Ala-Glu-Phe-(4-nitro)Phe-Ala-Leu
-
Sulfolobus acidocaldarius
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Sulfolobus acidocaldarius
-
-
-
Reaction
Reaction
Commentary
Organism
similar in specificity to pepsin A preferring bulky hydrophobic amino acids in P1 and P1'
prefers large hydrophobic residues at both sides of the scissile bond
Sulfolobus acidocaldarius
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Bovine serum albumin + H2O
-
137306
Sulfolobus acidocaldarius
?
-
-
-
?
glyceraldehyde-3-phosphate dehydrogenase + H2O
-
137306
Sulfolobus acidocaldarius
?
-
-
-
?
Hemoglobin + H2O
-
137306
Sulfolobus acidocaldarius
?
-
-
-
?
Lys-Pro-Ala-Glu-Phe-(4-nitro)Phe-Ala-Leu + H2O
-
137306
Sulfolobus acidocaldarius
Lys-Pro-Ala-Glu-Phe + (4-nitro)Phe-Ala-Leu
-
137306
Sulfolobus acidocaldarius
?
ovalbumin + H2O
-
137306
Sulfolobus acidocaldarius
?
-
-
-
?
oxidized insulin B + H2O
following bonds are hydrolyzed: Leu-Val, Leu-Tyr, Phe-Phe, Phe-Tyr, Tyr-Thr
137306
Sulfolobus acidocaldarius
?
-
-
-
?
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
75
-
-
Sulfolobus acidocaldarius
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2
-
-
Sulfolobus acidocaldarius
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
1,2-epoxy-3-(p-nitrophenoxy)propane
-
Sulfolobus acidocaldarius
acetamide
-
Sulfolobus acidocaldarius
diazoacetyl-DL-norleucine
-
Sulfolobus acidocaldarius
HgCl2
reversible by 2-mercaptoethanol
Sulfolobus acidocaldarius
pepstatin
-
Sulfolobus acidocaldarius
phenylalaninamide
-
Sulfolobus acidocaldarius
Urea
-
Sulfolobus acidocaldarius
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.053
-
Lys-Pro-Ala-Glu-Phe-(4-nitro)Phe-Ala-Leu
-
Sulfolobus acidocaldarius
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Bovine serum albumin + H2O
-
137306
Sulfolobus acidocaldarius
?
-
-
-
?
glyceraldehyde-3-phosphate dehydrogenase + H2O
-
137306
Sulfolobus acidocaldarius
?
-
-
-
?
Hemoglobin + H2O
-
137306
Sulfolobus acidocaldarius
?
-
-
-
?
Lys-Pro-Ala-Glu-Phe-(4-nitro)Phe-Ala-Leu + H2O
-
137306
Sulfolobus acidocaldarius
Lys-Pro-Ala-Glu-Phe + (4-nitro)Phe-Ala-Leu
-
137306
Sulfolobus acidocaldarius
?
ovalbumin + H2O
-
137306
Sulfolobus acidocaldarius
?
-
-
-
?
oxidized insulin B + H2O
following bonds are hydrolyzed: Leu-Val, Leu-Tyr, Phe-Phe, Phe-Tyr, Tyr-Thr
137306
Sulfolobus acidocaldarius
?
-
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
75
-
-
Sulfolobus acidocaldarius
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2
-
-
Sulfolobus acidocaldarius
Other publictions for EC 3.4.23.42
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
725163
Gogliettino
A new pepstatin-insensitive th ...
Saccharolobus solfataricus, Saccharolobus solfataricus DSM 1617
Int. J. Mol. Sci.
15
3204-3219
2014
-
-
-
-
-
-
1
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
9
-
1
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
9
-
1
-
1
-
1
-
-
-
-
-
-
-
-
-
726440
Cannio
Identification of a cell-bound ...
Saccharolobus solfataricus, Saccharolobus solfataricus P2
Protein Pept. Lett.
17
78-85
2010
-
-
-
-
-
-
3
-
1
-
1
-
-
3
-
-
1
-
-
-
-
-
6
1
1
1
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
1
-
1
-
-
-
-
1
-
-
-
-
6
1
1
1
1
-
1
1
-
-
1
-
-
1
-
-
668807
Tang
-
Thermopsin ...
Sulfolobus acidocaldarius
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
225-227
2004
-
-
1
-
-
-
8
-
1
-
1
2
-
1
-
1
1
-
1
1
-
-
5
1
1
1
-
-
1
1
-
-
6
-
-
-
-
1
-
-
-
-
-
8
6
-
1
-
1
2
-
-
1
1
1
1
-
-
5
1
1
1
-
-
1
1
-
-
-
-
-
-
-
-
137308
Lin
Thermopsin ...
Sulfolobus acidocaldarius
Methods Enzymol.
248
156-168
1995
-
-
1
-
-
-
4
1
1
-
-
1
-
1
-
-
1
-
-
-
1
1
4
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
4
-
1
1
-
-
1
-
-
-
1
-
-
1
1
4
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
137309
Lin
Heterologous expression of the ...
Sulfolobus acidocaldarius
Enzyme Microb. Technol.
14
696-701
1992
-
-
1
-
-
-
-
-
1
-
-
1
-
4
-
-
-
-
-
-
-
-
5
-
1
1
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
5
-
1
1
-
-
1
1
-
-
-
-
-
-
-
-
137310
Lin
Thermopsin, a thermostable aci ...
Sulfolobus acidocaldarius
Adv. Exp. Med. Biol.
306
255-257
1991
-
-
1
-
-
-
4
-
-
-
-
-
-
2
-
1
1
1
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
4
-
-
-
-
-
-
-
-
1
1
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
137306
Fusek
Enzymic properties of thermops ...
Sulfolobus acidocaldarius
J. Biol. Chem.
265
1496-1501
1990
-
-
-
-
-
-
7
1
-
-
-
-
-
2
-
-
-
1
-
-
-
-
6
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
7
-
1
-
-
-
-
-
-
-
-
-
-
-
-
6
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
137307
Lin
Purification, characterization ...
Sulfolobus acidocaldarius
J. Biol. Chem.
265
1490-1495
1990
-
-
1
-
-
1
-
-
-
-
3
-
-
4
-
2
1
-
-
-
-
-
1
1
1
1
2
-
1
2
-
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
-
-
5
-
-
-
2
2
-
-
-
-
1
2
2
1
2
-
2
2
-
-
-
-
-
-
-
-