BRENDA - Enzyme Database show
show all sequences of 3.4.23.42

Thermopsin, a thermostable acid protease from Sulfolobus acidocaldarius

Lin, X.; Fusek, M.; Tang, J.; Adv. Exp. Med. Biol. 306, 255-257 (1991)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Sulfolobus acidocaldarius
Inhibitors
Inhibitors
Commentary
Organism
Structure
1,2-epoxy-3-(p-nitrophenoxy)propane
-
Sulfolobus acidocaldarius
diazoacetyl-DL-norleucine
-
Sulfolobus acidocaldarius
Hg(CH3COO)2
-
Sulfolobus acidocaldarius
pepstatin
-
Sulfolobus acidocaldarius
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Sulfolobus acidocaldarius
-
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
side-chain modification
glycoprotein
Sulfolobus acidocaldarius
Purification (Commentary)
Commentary
Organism
-
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
additional information
The characteristic active site amino acid sequence for aspartic proteases, Asp Thr Gly, which is present in all aspartic proteases even with only distant evolutionary relatedness, is absent in thermopsin from Sulfolobus acidocaldarius, suggesting that a different catalytic mechanisms is employed.
137310
Sulfolobus acidocaldarius
?
-
-
-
?
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2
-
-
Sulfolobus acidocaldarius
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Sulfolobus acidocaldarius
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
1,2-epoxy-3-(p-nitrophenoxy)propane
-
Sulfolobus acidocaldarius
diazoacetyl-DL-norleucine
-
Sulfolobus acidocaldarius
Hg(CH3COO)2
-
Sulfolobus acidocaldarius
pepstatin
-
Sulfolobus acidocaldarius
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
side-chain modification
glycoprotein
Sulfolobus acidocaldarius
Purification (Commentary) (protein specific)
Commentary
Organism
-
Sulfolobus acidocaldarius
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
The characteristic active site amino acid sequence for aspartic proteases, Asp Thr Gly, which is present in all aspartic proteases even with only distant evolutionary relatedness, is absent in thermopsin from Sulfolobus acidocaldarius, suggesting that a different catalytic mechanisms is employed.
137310
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
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1
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4
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9
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1
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1
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1
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1
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9
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1
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1
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1
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726440
Cannio
Identification of a cell-bound ...
Saccharolobus solfataricus, Saccharolobus solfataricus P2
Protein Pept. Lett.
17
78-85
2010
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3
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1
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1
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3
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1
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6
1
1
1
1
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1
1
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3
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1
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1
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1
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6
1
1
1
1
-
1
1
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1
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1
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-
668807
Tang
-
Thermopsin ...
Sulfolobus acidocaldarius
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
225-227
2004
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1
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8
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1
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1
2
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1
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1
1
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1
1
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5
1
1
1
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1
1
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6
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1
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8
6
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1
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1
2
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1
1
1
1
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5
1
1
1
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1
1
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137308
Lin
Thermopsin ...
Sulfolobus acidocaldarius
Methods Enzymol.
248
156-168
1995
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1
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4
1
1
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1
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1
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1
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1
1
4
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1
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1
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1
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4
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1
1
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1
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1
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1
1
4
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1
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1
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137309
Lin
Heterologous expression of the ...
Sulfolobus acidocaldarius
Enzyme Microb. Technol.
14
696-701
1992
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1
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1
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1
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4
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5
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1
1
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1
1
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1
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1
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1
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5
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1
1
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1
1
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137310
Lin
Thermopsin, a thermostable aci ...
Sulfolobus acidocaldarius
Adv. Exp. Med. Biol.
306
255-257
1991
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1
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4
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2
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1
1
1
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1
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1
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1
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4
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1
1
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1
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1
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137306
Fusek
Enzymic properties of thermops ...
Sulfolobus acidocaldarius
J. Biol. Chem.
265
1496-1501
1990
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7
1
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2
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1
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6
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1
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1
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7
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1
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6
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1
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1
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137307
Lin
Purification, characterization ...
Sulfolobus acidocaldarius
J. Biol. Chem.
265
1490-1495
1990
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1
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1
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3
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4
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2
1
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1
1
1
1
2
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1
2
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2
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1
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5
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2
2
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1
2
2
1
2
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2
2
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