BRENDA - Enzyme Database show
show all sequences of 3.4.23.21

Molecular and enzymatic properties of an aspartic proteinase from Rhizopus hangchow

Ichishima, E.; Ojima, M.; Yamagata, Y.; Hanzawa, S.; Nakamura, T.; Phytochemistry 38, 27-30 (1995)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
Diazoacetyl-DL-norleucine methyl ester
-
Rhizopus oryzae
pepstatin
A
Rhizopus oryzae
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36000
-
Rhizopus hangchow, FPLC gel filtration
Rhizopus oryzae
37600
-
1 * 37600, Rhizopus hangchow, SDS-PAGE
Rhizopus oryzae
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rhizopus oryzae
-
-
-
Purification (Commentary)
Commentary
Organism
-
Rhizopus oryzae
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Rhizopus oryzae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
casein + H2O
-
30621
Rhizopus oryzae
?
-
-
-
-
additional information
milk clotting activity
30621
Rhizopus oryzae
?
-
-
-
-
additional information
trypsinogen activation
30621
Rhizopus oryzae
?
-
-
-
-
Oxidized insulin B-chain + H2O
primarily the Leu15-Tyr16 bond and the Tyr16-Leu17 bond is hydrolyzed, additional cleavage of the bonds Ala14-Leu15 and Phe24-Phe25
30621
Rhizopus oryzae
Proteolytically cleaved oxidized insulin B-chain
-
-
-
-
Subunits
Subunits
Commentary
Organism
monomer
1 * 37600, Rhizopus hangchow, SDS-PAGE
Rhizopus oryzae
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
45
-
pH 3, 5 min, stable
Rhizopus oryzae
50
-
pH 3, 5 min, complete inactivation
Rhizopus oryzae
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3
4
trypsinogen activation
Rhizopus oryzae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Diazoacetyl-DL-norleucine methyl ester
-
Rhizopus oryzae
pepstatin
A
Rhizopus oryzae
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36000
-
Rhizopus hangchow, FPLC gel filtration
Rhizopus oryzae
37600
-
1 * 37600, Rhizopus hangchow, SDS-PAGE
Rhizopus oryzae
Purification (Commentary) (protein specific)
Commentary
Organism
-
Rhizopus oryzae
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Rhizopus oryzae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
casein + H2O
-
30621
Rhizopus oryzae
?
-
-
-
-
additional information
milk clotting activity
30621
Rhizopus oryzae
?
-
-
-
-
additional information
trypsinogen activation
30621
Rhizopus oryzae
?
-
-
-
-
Oxidized insulin B-chain + H2O
primarily the Leu15-Tyr16 bond and the Tyr16-Leu17 bond is hydrolyzed, additional cleavage of the bonds Ala14-Leu15 and Phe24-Phe25
30621
Rhizopus oryzae
Proteolytically cleaved oxidized insulin B-chain
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 37600, Rhizopus hangchow, SDS-PAGE
Rhizopus oryzae
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
45
-
pH 3, 5 min, stable
Rhizopus oryzae
50
-
pH 3, 5 min, complete inactivation
Rhizopus oryzae
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3
4
trypsinogen activation
Rhizopus oryzae
Other publictions for EC 3.4.23.21
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)
670726
Kumar
-
Extracellular acid protease fr ...
Rhizopus oryzae
Process Biochem.
40
1701-1705
2005
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1
1
1
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1
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1
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1
1
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668787
Dunn
-
Rhizopuspepsin ...
Rhizopus microsporus var. chinensis, Rhizopus niveus, Rhizopus oryzae
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
108-111
2004
-
1
3
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1
1
3
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3
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3
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1
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1
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8
1
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1
1
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2
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1
3
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1
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1
3
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3
1
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1
-
8
1
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1
1
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-
2
-
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649214
Prasad
Effect of pH on the structure ...
Rhizopus sp.
Acta Crystallogr. Sect. D
59
1755-1761
2003
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1
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1
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653780
Athauda
Cleavage specificities of aspa ...
Rhizopus sp.
Protein Pept. Lett.
9
289-294
2002
-
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1
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1
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1
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649344
Kalra
Free-energy analysis of enzyme ...
Rhizopus sp.
Appl. Biochem. Biotechnol.
96
93-108
2001
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-
1
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1
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1
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650516
Bhatt
Chimeric aspartic proteinases ...
Rhizopus sp.
Bioorg. Chem.
28
374-393
2000
-
1
1
1
-
-
5
27
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2
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16
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27
1
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3
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-
1
1
-
1
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5
3
27
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16
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27
1
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653719
Flentke
Purification and crystallizati ...
Rhizopus sp.
Protein Expr. Purif.
16
213-220
1999
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1
1
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1
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1
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1
1
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1
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653777
Lowther
-
The promiscuous active site sp ...
Rhizopus microsporus var. chinensis
Protein Pept. Lett.
5
303-316
1998
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1
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30621
Ichishima
Molecular and enzymatic proper ...
Rhizopus oryzae
Phytochemistry
38
27-30
1995
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2
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2
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2
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4
1
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1
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1
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4
1
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2
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1
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30625
Lowther
Engineering the substrate spec ...
Rhizopus sp.
Protein Sci.
4
689-702
1995
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5
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1
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30626
Sing
High-performance hydrophobic i ...
Rhizopus sp.
J. Chromatogr.
598
181-187
1992
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30559
Majima
-
Comparative study on the speci ...
Rhizopus sp.
Agric. Biol. Chem.
52
787-793
1988
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1
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30611
Takahashi
Determination of the amino aci ...
Rhizopus microsporus var. chinensis
J. Biochem.
103
162-167
1988
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30612
Horiuchi
Isolation and sequencing of a ...
Rhizopus niveus
J. Bacteriol.
170
272-278
1988
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1
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2
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30624
Nakatani
Kinetic study on the interacti ...
Rhizopus microsporus var. chinensis
Arch. Biochem. Biophys.
263
311-314
1988
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30607
Suguna
Binding of a reduced peptide i ...
Rhizopus microsporus var. chinensis
Proc. Natl. Acad. Sci. USA
84
7009-7013
1987
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30615
Takahashi
The amino acid sequence of rhi ...
Rhizopus microsporus var. chinensis
J. Biol. Chem.
262
1468-1478
1987
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30619
Delaney
Amino acid sequence of rhizopu ...
Rhizopus microsporus var. chinensis
J. Biol. Chem.
262
1461-1467
1987
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1
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30620
Suguna
Structure and refinement at 1. ...
Rhizopus microsporus var. chinensis
J. Mol. Biol.
196
877-900
1987
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30599
Hofmann
Effect of pH on the activities ...
Rhizopus sp.
Biochemistry
23
635-643
1984
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2
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1
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30617
Bott
Three-dimensional structure of ...
Rhizopus microsporus var. chinensis
Biochemistry
21
6956-6962
1982
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30627
Ohtsuru
Purification and characterizat ...
Rhizopus microsporus var. chinensis
Int. J. Biochem.
14
925-932
1982
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2
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30622
Nakamura
The structure and function of ...
Rhizopus microsporus var. chinensis
J. Biochem.
84
1593-1600
1978
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2
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30608
Gripon
N-terminal amino acid sequence ...
Rhizopus microsporus var. chinensis
Can. J. Biochem.
55
504-506
1977
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30616
Subramanian
Homology among acid proteases: ...
Rhizopus microsporus var. chinensis
Proc. Natl. Acad. Sci. USA
74
556-559
1977
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1
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30623
Nakamura
Amino acid sequences around 1, ...
Rhizopus microsporus var. chinensis
J. Biochem.
81
805-807
1977
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1
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30568
Takahashi
The structure and function of ...
Rhizopus microsporus var. chinensis
J. Biochem.
80
497-506
1976
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3
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1
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3
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30614
Subramanian
The crystal at 5.5A resolution ...
Rhizopus microsporus var. chinensis
Biochem. Biophys. Res. Commun.
68
875-880
1976
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1
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1
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30609
Mizobe
The structure and function of ...
Rhizopus microsporus var. chinensis
J. Biochem.
73
61-68
1973
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3
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30628
Graham
Rhizopus acid proteinases (rhi ...
Rhizopus microsporus var. chinensis
Can. J. Biochem.
51
789-796
1973
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1
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2
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30606
Kurono
-
Isolation of a protease from a ...
Rhizopus niveus
Agric. Biol. Chem.
35
1668-1675
1971
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1
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3
1
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1
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1
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1
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1
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1
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1
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1
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1
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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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2
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30605
Tsuru
-
Mold proteases. II. Substrat ...
Rhizopus microsporus var. chinensis
Agric. Biol. Chem.
33
1419-1426
1969
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1
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1
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8
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1
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8
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