BRENDA - Enzyme Database show
show all sequences of 3.4.23.22

The interaction of aspartic proteinases with naturally-occurring inhibitors from actinomycetes and Ascaris lumbricoides

Valler, M.J.; Kay, J.; Aoyagi, T.; Dunn, B.M.; J. Enzyme Inhib. 1, 77-82 (1985)

Data extracted from this reference:

Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Cryphonectria parasitica
-
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Other publictions for EC 3.4.23.22
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)
717977
Koester
A small nonrule of 3 compatibl ...
Cryphonectria parasitica
J. Med. Chem.
54
7784-7796
2011
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670005
Vidossich
Binding of phosphinate and pho ...
Cryphonectria parasitica
J. Phys. Chem. B
110
1437-1442
2006
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679599
Coates
X-ray, neutron and NMR studies ...
Cryphonectria parasitica
Eur. Biophys. J.
35
559-566
2006
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668786
Cooper
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Endothiapepsin ...
Cryphonectria parasitica
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
104-107
2004
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670837
Alexov
Calculating proton uptake/rele ...
Cryphonectria parasitica
Proteins
56
572-584
2004
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649236
Coates
The structure of endothiapepsi ...
Cryphonectria parasitica
Acta Crystallogr. Sect. D
59
978-981
2003
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652883
Coates
Five atomic resolution structu ...
Cryphonectria parasitica
J. Mol. Biol.
318
1405-1415
2002
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1
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6
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650030
Coates
A neutron Laue diffraction stu ...
Endothia sp.
Biochemistry
40
13149-13157
2001
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649119
Cooper
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A preliminary neutron Laue dif ...
Endothia sp.
Acta Crystallogr. Sect. D
56
246-248
2000
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653831
Stultz
Dynamic ligand design and comb ...
Endothia sp.
Proteins
40
258-289
2000
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30639
Bailey
A structural comparison of 21 ...
Cryphonectria parasitica
Protein Sci.
3
2129-2143
1994
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30636
Bailey
X-ray-crystallographic studies ...
Cryphonectria parasitica
Biochem. J.
289
363-371
1993
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30635
Cooper
X-ray crystallographic analysi ...
Cryphonectria parasitica
Biochemistry
31
8142-8150
1992
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30634
Brown
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Purification of two fungal asp ...
Cryphonectria parasitica
Agric. Biol. Chem.
54
1563-1565
1990
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30637
Veerapandian
X-ray analyses of aspartic pro ...
Cryphonectria parasitica
J. Mol. Biol.
216
1017-1029
1990
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30638
Sali
High-resolution X-ray diffract ...
Cryphonectria parasitica
EMBO J.
8
2179-2188
1989
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30631
Barkholt
Amino acid sequence of endothi ...
Cryphonectria parasitica
Eur. J. Biochem.
167
327-338
1987
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30633
Cooper
The structure of a synthetic p ...
Cryphonectria parasitica
Eur. J. Biochem.
169
215-221
1987
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30640
Valler
The interaction of aspartic pr ...
Cryphonectria parasitica
J. Enzyme Inhib.
1
77-82
1985
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30616
Subramanian
Homology among acid proteases: ...
Cryphonectria parasitica
Proc. Natl. Acad. Sci. USA
74
556-559
1977
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30630
Williams
Hydrolysis of peptide bonds of ...
Cryphonectria parasitica
Arch. Biochem. Biophys.
149
52-61
1972
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30629
Whitaker
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Protease of Endothia parasitic ...
Cryphonectria parasitica
Methods Enzymol.
19
436-445
1970
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