BRENDA - Enzyme Database show
show all sequences of 3.4.16.6

Characterization of Drosophila carboxypeptidase D

Sidyelyeva, G.; Fricker, L.D.; J. Biol. Chem. 277, 49613-49620 (2002)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
individual domains of the enzyme are expressed in insect Sf9 cells using the baculovirus expression system. Medium from domain 1B-expressing cells and domain 2-expressing cells shows substantial enzymatic activity, whereas medium from domain 1A-expressing cells is not different from cells infected with wild-type virus. The individual domains 1A, 1B, and 2 are expressed in baculovirus under the polyhedrin promoter and with the signal peptide of the rat enzyme
Drosophila melanogaster
Engineering
Amino acid exchange
Commentary
Organism
E353Q
cells infected with the mutant enzyme show considerable carboxypeptidase activity, mutation eliminates the activity of domain 1
Drosophila melanogaster
E771Q
cells infected with the mutant enzyme show considerable carboxypeptidase activity, mutation eliminates the activity of domain 2
Drosophila melanogaster
Inhibitors
Inhibitors
Commentary
Organism
Structure
4-[[(3,4-dinitrophenyl)carbonyl]amino]-2-(6-hydroxy-3-oxo-3H-xanthen-9-yl)benzoic acid
-
Drosophila melanogaster
EDTA
-
Drosophila melanogaster
Guanidinoethylmercaptosuccinic acid
domain 1B and domain
Drosophila melanogaster
PCMB
domain 1B and domain
Drosophila melanogaster
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.208
-
dansyl-Phe-Ala-Arg
pH 7.4, 37°C, domain 1B
Drosophila melanogaster
0.246
-
dansyl-Phe-Ala-Arg
pH 5.7, 37°C, domain 2
Drosophila melanogaster
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Drosophila melanogaster
the enzyme functions in processing of proteins that transit the secretory pathway
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Drosophila melanogaster
-
-
-
Purification (Commentary)
Commentary
Organism
domain 1B and 2 expressed in Sf9 cells using baculovirus expression system
Drosophila melanogaster
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Dansyl-Phe-Ala-Arg + H2O
-
647241
Drosophila melanogaster
Dansyl-Phe-Ala + Arg
-
-
-
?
additional information
activity of individual domains of the enzyme. Domain 1B is more active at neutral pH and greatly prefers C-terminal Arg over Lys, whereas domain 2 is more active at pH 5-6 and slightly prefers C-terminal Lys over Arg
647241
Drosophila melanogaster
?
-
-
-
-
additional information
the enzyme functions in processing of proteins that transit the secretory pathway
647241
Drosophila melanogaster
?
-
-
-
-
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3.86
-
dansyl-Phe-Ala-Arg
pH 5.7, 37°C, domain 2
Drosophila melanogaster
32.6
-
dansyl-Phe-Ala-Arg
pH 7.4, 37°C, domain 1B
Drosophila melanogaster
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5
7
wild-type enzyme
Drosophila melanogaster
5.6
-
domain 1B
Drosophila melanogaster
7.4
-
domain 2
Drosophila melanogaster
Cloned(Commentary) (protein specific)
Commentary
Organism
individual domains of the enzyme are expressed in insect Sf9 cells using the baculovirus expression system. Medium from domain 1B-expressing cells and domain 2-expressing cells shows substantial enzymatic activity, whereas medium from domain 1A-expressing cells is not different from cells infected with wild-type virus. The individual domains 1A, 1B, and 2 are expressed in baculovirus under the polyhedrin promoter and with the signal peptide of the rat enzyme
Drosophila melanogaster
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
E353Q
cells infected with the mutant enzyme show considerable carboxypeptidase activity, mutation eliminates the activity of domain 1
Drosophila melanogaster
E771Q
cells infected with the mutant enzyme show considerable carboxypeptidase activity, mutation eliminates the activity of domain 2
Drosophila melanogaster
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
4-[[(3,4-dinitrophenyl)carbonyl]amino]-2-(6-hydroxy-3-oxo-3H-xanthen-9-yl)benzoic acid
-
Drosophila melanogaster
EDTA
-
Drosophila melanogaster
Guanidinoethylmercaptosuccinic acid
domain 1B and domain
Drosophila melanogaster
PCMB
domain 1B and domain
Drosophila melanogaster
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.208
-
dansyl-Phe-Ala-Arg
pH 7.4, 37°C, domain 1B
Drosophila melanogaster
0.246
-
dansyl-Phe-Ala-Arg
pH 5.7, 37°C, domain 2
Drosophila melanogaster
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Drosophila melanogaster
the enzyme functions in processing of proteins that transit the secretory pathway
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
domain 1B and 2 expressed in Sf9 cells using baculovirus expression system
Drosophila melanogaster
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Dansyl-Phe-Ala-Arg + H2O
-
647241
Drosophila melanogaster
Dansyl-Phe-Ala + Arg
-
-
-
?
additional information
activity of individual domains of the enzyme. Domain 1B is more active at neutral pH and greatly prefers C-terminal Arg over Lys, whereas domain 2 is more active at pH 5-6 and slightly prefers C-terminal Lys over Arg
647241
Drosophila melanogaster
?
-
-
-
-
additional information
the enzyme functions in processing of proteins that transit the secretory pathway
647241
Drosophila melanogaster
?
-
-
-
-
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3.86
-
dansyl-Phe-Ala-Arg
pH 5.7, 37°C, domain 2
Drosophila melanogaster
32.6
-
dansyl-Phe-Ala-Arg
pH 7.4, 37°C, domain 1B
Drosophila melanogaster
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5
7
wild-type enzyme
Drosophila melanogaster
5.6
-
domain 1B
Drosophila melanogaster
7.4
-
domain 2
Drosophila melanogaster
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
-
-
1
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
731593
Jin
SiRNA-targeted carboxypeptidas ...
Homo sapiens
Cell Biol. Int.
37
929-939
2013
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
1
1
1
1
-
-
731598
Carmona-Gutierrez
The cell death protease Kex1p ...
Saccharomyces cerevisiae
Cell Cycle
12
1704-1712
2013
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
731176
Morita
Serine-type carboxypeptidase K ...
Aspergillus oryzae
Appl. Environ. Microbiol.
78
8154-8157
2012
-
-
1
-
-
-
3
-
-
-
1
-
-
3
-
-
1
-
-
-
-
-
7
-
-
-
1
-
1
-
1
-
-
-
-
-
-
1
-
-
-
-
-
3
-
-
-
-
1
-
-
-
-
1
-
-
-
-
7
-
-
-
1
-
1
-
1
-
-
1
1
-
-
-
732850
Thomas
Testosterone and prolactin inc ...
Homo sapiens
Prostate
72
450-460
2012
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
2
2
1
-
-
698771
Hauptmann
Kex1 protease is involved in y ...
Saccharomyces cerevisiae
J. Biol. Chem.
283
19151-19163
2008
-
-
1
-
-
-
-
-
2
-
-
1
-
3
-
-
1
-
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
701056
Pozzuolo
Efficient bacterial expression ...
Kluyveromyces lactis
Protein Expr. Purif.
59
334-341
2008
-
1
1
-
-
-
-
-
-
1
2
1
-
4
-
-
1
-
-
-
1
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
1
2
1
-
-
-
1
-
-
1
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
683223
Serviene
-
Influence of Kex1p and Kex2p p ...
Saccharomyces cerevisiae
Biologija (Vilnius)
53
35-38
2007
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
683695
Heiman
The Golgi-resident protease Ke ...
Saccharomyces cerevisiae
J. Cell Biol.
176
209-222
2007
-
1
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
669448
Sidyelyeva
Characterization of the molecu ...
Drosophila melanogaster
J. Biol. Chem.
281
13844-13852
2006
-
-
-
-
1
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
669602
Kalinina
Drosophila S2 cells produce mu ...
Drosophila melanogaster
J. Cell. Biochem.
99
770-783
2006
-
-
-
-
-
-
-
-
2
-
-
-
-
5
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
667510
O'Malley
Characterization of a novel, c ...
Homo sapiens, Rattus norvegicus
Biochem. J.
390
665-673
2005
-
-
-
-
-
-
4
2
2
-
-
-
-
6
-
-
-
-
-
3
-
-
2
1
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
2
2
-
-
-
-
-
-
-
-
3
-
-
2
1
-
-
-
-
3
-
-
-
-
-
-
-
-
-
665316
Satoh
Microbial serine carboxypeptid ...
Triticum aestivum
J. Antibiot.
57
316-325
2004
-
-
-
-
-
-
4
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
647241
Sidyelyeva
Characterization of Drosophila ...
Drosophila melanogaster
J. Biol. Chem.
277
49613-49620
2002
-
-
1
-
2
-
4
2
-
-
-
1
-
4
-
-
1
-
-
-
-
-
3
-
-
-
-
2
3
-
-
-
-
-
-
-
-
1
-
-
2
-
-
4
-
2
-
-
-
1
-
-
-
1
-
-
-
-
3
-
-
-
-
2
3
-
-
-
-
-
-
-
-
-
647233
Shilton
Crystal structure of Kex1delta ...
Saccharomyces cerevisiae
Biochemistry
36
9002-9012
1997
-
-
-
1
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
647236
Shilton
Crystallization of a soluble f ...
Saccharomyces cerevisiae
Protein Sci.
5
395-397
1996
-
-
-
1
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
647192
Remington
Carboxypeptidases C and D ...
Saccharomyces cerevisiae, Triticum aestivum
Methods Enzymol.
244
231-248
1994
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
647234
Latchinian-Sadek
Secretion, purification and ch ...
Saccharomyces cerevisiae
Eur. J. Biochem.
219
647-652
1994
-
-
-
-
-
-
4
1
-
-
1
1
-
1
-
1
-
-
-
-
-
-
2
1
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
4
-
1
-
-
1
1
-
-
1
-
-
-
-
-
2
1
-
-
-
-
1
-
-
1
-
-
-
-
-
-
647238
Latchinian-Sadek
Expression, purification, and ...
Saccharomyces cerevisiae
J. Biol. Chem.
268
534-540
1993
-
-
-
-
-
-
7
3
-
2
-
1
-
2
-
-
1
-
-
-
1
-
9
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
7
-
3
-
2
-
1
-
-
-
1
-
-
1
-
9
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
647231
Liao
Refined atomic model of wheat ...
Triticum aestivum
Biochemistry
31
9796-9812
1992
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
647235
Thomas
Yeast KEX1 protease cleaves a ...
Saccharomyces cerevisiae
J. Biol. Chem.
265
10821-10824
1990
-
-
1
-
-
-
-
-
-
-
-
1
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
647232
Dmochowska
Yeast KEX1 gene encodes a puta ...
Saccharomyces cerevisiae
Cell
50
573-584
1987
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-