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Information on EC 3.4.16.6 - carboxypeptidase D and Organism(s) Saccharomyces cerevisiae and UniProt Accession P09620
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3.4.16.6 carboxypeptidase DSpecify your search results
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- 3.4.16.6
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
cpd, carboxypeptidase d, kex1p, wheat carboxypeptidase ii, cpdw-ii, kex1deltap, kex1 protease, kex1 carboxypeptidase, kex-1 endopeptidase, saccharomyces cerevisiae kex1 gene product, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
carboxypeptidase Kex1
-
-
-
-
cereal serine carboxypeptidase II
-
-
-
-
CP-MII.1
-
-
-
-
CP-MII.2
-
-
-
-
CP-MII.3
-
-
-
-
CP-WII
-
-
-
-
CPD
-
-
-
-
CPDW-II
-
-
-
-
gene KEX1 serine carboxypeptidase
-
-
-
-
KEX1 carboxypeptidase
-
-
-
-
KEX1 proteinase
-
-
-
-
Saccharomyces cerevisiae KEX1 gene product
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
153967-26-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-factor-Lys-Arg + H2O
mature active alpha-factor + Lys + Arg
-
maturation takes place in sequential manner
-
?
furylacryloyl-Ala-Arg + H2O
furylacryloyl-Ala + Arg
-
activity assay
-
-
?
additional information
?
-
the enzyme has a narrow specificity for lysyl ar arginyl residues at the C-terminus of the substrate
-
-
?
additional information
?
-
-
the enzyme has a narrow specificity for lysyl ar arginyl residues at the C-terminus of the substrate
-
-
?
additional information
?
-
-
role in the processing of both the alpha-pheromone and the killer toxin precursors
-
-
?
additional information
?
-
-
involved in the C-terminal processing of the lysine and arginine residues from the precursors of K1 and K2 killer toxins and alpha-factor (mating pheromone)
-
-
?
additional information
?
-
-
plays a role in polypeptide processing in yeast
-
-
?
additional information
?
-
-
specific for the removal of basic amino acids from prohormone processing intermediates, in mammalian cells
-
-
?
additional information
?
-
-
preferential release of a C-terminal arginine or lysine residue
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
role in the processing of both the alpha-pheromone and the killer toxin precursors
-
-
?
additional information
?
-
-
involved in the C-terminal processing of the lysine and arginine residues from the precursors of K1 and K2 killer toxins and alpha-factor (mating pheromone)
-
-
?
additional information
?
-
-
plays a role in polypeptide processing in yeast
-
-
?
additional information
?
-
-
specific for the removal of basic amino acids from prohormone processing intermediates, in mammalian cells
-
-
?
additional information
?
-
-
preferential release of a C-terminal arginine or lysine residue
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
absence of Kex1p diminishes HOCl-induced production of reactive oxygen species, apoptosis and protein modification
physiological function
-
protease Kex1p mediates HOCl-induced lethality
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of KEX1DELTAp, an enzyme form lacking the acidic and the membrane-spanning domain at 2.4 A resolution
structure of Kex1DELTAp, an enzyme that lacks the acidic domain and membrane-spanning portion of Kex1p
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
lack of the Kex1 protease results in fusion defects during yeast mating
additional information
-
studies of dependence of Saccharomyces cerevisiae K2 preprotoxin killing and immunity properties modulated by the action of Kex1p and Kex2p enzymes show that the lack of Kex1p carboxypeptidase 10times decreases toxin activity, and the deficiency of Kex2p endopeptidase completely removes killing ability
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
KEX1 gene from Saccharomyces cerevisiae expressed using the baculovirus/insect cell system
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
-
Kex2 and Kex1 may promote cell fusion by proteolytically processing substrates that act in parallel to Prm1 (pheromone-regulated membrane protein 1) as an alternative fusion machine, as cell wall components, or both
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Remington, S.J.; Breddam, K.
Carboxypeptidases C and D
Methods Enzymol.
244
231-248
1994
Saccharomyces cerevisiae, Triticum aestivum
Dmochowska, A.; Dignard, D.; Henning, D.; Thomas, D.Y.; Bussey, H.
Yeast KEX1 gene encodes a putative protease with a carboxypeptidase B-like function involved in killer toxin and alpha-factor precursor processing
Cell
50
573-584
1987
Saccharomyces cerevisiae
Shilton, B.H.; Thomas, D.Y.; Cygler, M.
Crystal structure of Kex1deltap, a prohormone-processing carboxypeptidase from Saccharomyces cerevisiae
Biochemistry
36
9002-9012
1997
Saccharomyces cerevisiae (P09620), Saccharomyces cerevisiae
Latchinian-Sadek, L.; Thomas, D.Y.
Secretion, purification and characterization of a soluble form of the yeast KEX1-encoded protein from insect-cell cultures
Eur. J. Biochem.
219
647-652
1994
Saccharomyces cerevisiae
Thomas, L.; Cooper, A.; Bussey, H.; Thomas, G.
Yeast KEX1 protease cleaves a prohormone processing intermediate in mammalian cells
J. Biol. Chem.
265
10821-10824
1990
Saccharomyces cerevisiae
Shilton, B.H.; Li, Y.; Tessier, D.; Thomas, D.Y.; Cygler, M.
Crystallization of a soluble form of the Kex1p serine carboxypeptidase from Saccharomyces cerevisiae
Protein Sci.
5
395-397
1996
Saccharomyces cerevisiae
Latchinian-Sadek, L.; Thomas, D.Y.
Expression, purification, and characterization of the yeast KEX1 gene product, a polypeptide precursor processing carboxypeptidase
J. Biol. Chem.
268
534-540
1993
Saccharomyces cerevisiae
Serviene, E.; Cepononyte, S.; Lebionka, A.; Melvydas, V.
Influence of Kex1p and Kex2p proteases on the function of Saccharomyces cerevisiae K2 preprotoxin
Biologija (Vilnius)
53
35-38
2007
Saccharomyces cerevisiae
-
Heiman, M.G.; Engel, A.; Walter, P.
The Golgi-resident protease Kex2 acts in conjunction with Prm1 to facilitate cell fusion during yeast mating
J. Cell Biol.
176
209-222
2007
Saccharomyces cerevisiae
Hauptmann, P.; Lehle, L.
Kex1 protease is involved in yeast cell death induced by defective N-glycosylation, acetic acid, and chronological aging
J. Biol. Chem.
283
19151-19163
2008
Saccharomyces cerevisiae
Carmona-Gutierrez, D.; Alavian-Ghavanini, A.; Habernig, L.; Bauer, M.A.; Hammer, A.; Rossmann, C.; Zimmermann, A.S.; Ruckenstuhl, C.; Buettner, S.; Eisenberg, T.; Sattler, W.; Malle, E.; Madeo, F.
The cell death protease Kex1p is essential for hypochlorite-induced apoptosis in yeast
Cell Cycle
12
1704-1712
2013
Saccharomyces cerevisiae
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