BRENDA - Enzyme Database show
show all sequences of 3.4.16.6

Amyloid formation by human carboxypeptidase D transthyretin-like domain under physiological conditions

Garcia-Pardo, J.; Grana-Montes, R.; Fernandez-Mendez, M.; Ruyra, A.; Roher, N.; Aviles, F.X.; Lorenzo, J.; Ventura, S.; J. Biol. Chem. 289, 33783-33796 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
the transthyretin-like domain belonging to the first catalytic domain of human metallocarboxypeptidase D (residues 386-460, h-TTL), is cloned into the pET-22B vector to encode a C-terminal hexahistidine fusion protein. Expression carried out in Escherichia coli
Homo sapiens
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
8700
-
gel filtration of the transthyretin-like domain belonging to the first catalytic domain of human metallocarboxypeptidase D (h-TTL)
Homo sapiens
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
-
-
Subunits
Subunits
Commentary
Organism
monomer
the transthyretin-like domain belonging to the first catalytic domain of human metallocarboxypeptidase D (h-TTL) is a monomer in solution
Homo sapiens
More
the transthyretin-like domain belonging to the first catalytic domain of human metallocarboxypeptidase D (h-TTL) carboxypeptidase D aggregates under close to physiological conditions into amyloid structures, with the population of folded but aggregation-prone states being controlled by the conformational stability of the domain
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
the transthyretin-like domain belonging to the first catalytic domain of human metallocarboxypeptidase D (residues 386-460, h-TTL), is cloned into the pET-22B vector to encode a C-terminal hexahistidine fusion protein. Expression carried out in Escherichia coli
Homo sapiens
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
8700
-
gel filtration of the transthyretin-like domain belonging to the first catalytic domain of human metallocarboxypeptidase D (h-TTL)
Homo sapiens
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
the transthyretin-like domain belonging to the first catalytic domain of human metallocarboxypeptidase D (h-TTL) is a monomer in solution
Homo sapiens
More
the transthyretin-like domain belonging to the first catalytic domain of human metallocarboxypeptidase D (h-TTL) carboxypeptidase D aggregates under close to physiological conditions into amyloid structures, with the population of folded but aggregation-prone states being controlled by the conformational stability of the domain
Homo sapiens
Other publictions for EC 3.4.16.6
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)
732160
Garcia-Pardo
Amyloid formation by human car ...
Homo sapiens
J. Biol. Chem.
289
33783-33796
2014
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731593
Jin
SiRNA-targeted carboxypeptidas ...
Homo sapiens
Cell Biol. Int.
37
929-939
2013
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1
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731598
Carmona-Gutierrez
The cell death protease Kex1p ...
Saccharomyces cerevisiae
Cell Cycle
12
1704-1712
2013
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2
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731176
Morita
Serine-type carboxypeptidase K ...
Aspergillus oryzae
Appl. Environ. Microbiol.
78
8154-8157
2012
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732850
Thomas
Testosterone and prolactin inc ...
Homo sapiens
Prostate
72
450-460
2012
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1
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698771
Hauptmann
Kex1 protease is involved in y ...
Saccharomyces cerevisiae
J. Biol. Chem.
283
19151-19163
2008
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701056
Pozzuolo
Efficient bacterial expression ...
Kluyveromyces lactis
Protein Expr. Purif.
59
334-341
2008
-
1
1
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1
2
1
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4
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683223
Serviene
-
Influence of Kex1p and Kex2p p ...
Saccharomyces cerevisiae
Biologija (Vilnius)
53
35-38
2007
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1
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683695
Heiman
The Golgi-resident protease Ke ...
Saccharomyces cerevisiae
J. Cell Biol.
176
209-222
2007
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669448
Sidyelyeva
Characterization of the molecu ...
Drosophila melanogaster
J. Biol. Chem.
281
13844-13852
2006
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669602
Kalinina
Drosophila S2 cells produce mu ...
Drosophila melanogaster
J. Cell. Biochem.
99
770-783
2006
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667510
O'Malley
Characterization of a novel, c ...
Homo sapiens, Rattus norvegicus
Biochem. J.
390
665-673
2005
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2
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1
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3
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665316
Satoh
Microbial serine carboxypeptid ...
Triticum aestivum
J. Antibiot.
57
316-325
2004
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647241
Sidyelyeva
Characterization of Drosophila ...
Drosophila melanogaster
J. Biol. Chem.
277
49613-49620
2002
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1
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2
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4
2
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4
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3
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3
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647233
Shilton
Crystal structure of Kex1delta ...
Saccharomyces cerevisiae
Biochemistry
36
9002-9012
1997
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647236
Shilton
Crystallization of a soluble f ...
Saccharomyces cerevisiae
Protein Sci.
5
395-397
1996
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647192
Remington
Carboxypeptidases C and D ...
Saccharomyces cerevisiae, Triticum aestivum
Methods Enzymol.
244
231-248
1994
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647234
Latchinian-Sadek
Secretion, purification and ch ...
Saccharomyces cerevisiae
Eur. J. Biochem.
219
647-652
1994
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647238
Latchinian-Sadek
Expression, purification, and ...
Saccharomyces cerevisiae
J. Biol. Chem.
268
534-540
1993
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7
3
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9
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9
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647231
Liao
Refined atomic model of wheat ...
Triticum aestivum
Biochemistry
31
9796-9812
1992
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647235
Thomas
Yeast KEX1 protease cleaves a ...
Saccharomyces cerevisiae
J. Biol. Chem.
265
10821-10824
1990
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647232
Dmochowska
Yeast KEX1 gene encodes a puta ...
Saccharomyces cerevisiae
Cell
50
573-584
1987
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1
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