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Information on EC 3.4.16.6 - carboxypeptidase D
for references in articles please use BRENDA:EC3.4.16.6
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.16 Serine-type carboxypeptidases
3.4.16.6 carboxypeptidase D
IUBMB Comments
A carboxypeptidase with optimum pH 4.5-6.0, inhibited by diisopropyl fluorophosphate, and sensitive to thiol-blocking reagents (reviewed in ). In peptidase family S10 (carboxypeptidase C family).
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 3.4.16.6
- pyrimidine
-
cyclobutane
-
cigarette
-
smoking
- smokers
- peritoneal
- dialysis
-
uv-induced
- photoproducts
-
skill
-
grate
-
practitioner
-
professionals
-
acuity
-
photolyase
- nurses
- vision
-
gratings
-
profession
-
quit
-
nursing
-
satisfaction
-
monocular
-
accredit
-
photopic
-
photoreactivation
-
career
- cotinine
-
curriculum
- disproportion
-
dentist
-
thematic
-
workforce
-
diopter
-
midwives
-
postgraduate
-
translesion
-
psychophysical
-
leadership
-
wavefront
-
mentor
- astigmatism
-
stakeholder
-
learner
-
therapist
-
logmar
-
lasik
- biotechnology
-
posttransfusion
-
employers
-
phacoemulsification
- molecular biology
showSynonyms
cpd, carboxypeptidase d, kex1p, wheat carboxypeptidase ii, kex1 protease, cpdw-ii, kex1deltap, kex1 carboxypeptidase, kex-1 endopeptidase, saccharomyces cerevisiae kex1 gene product, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
carboxypeptidase Kex1
-
-
-
-
cereal serine carboxypeptidase II
-
-
-
-
CP-MII.1
-
-
-
-
CP-MII.2
-
-
-
-
CP-MII.3
-
-
-
-
CP-WII
-
-
-
-
CPD
CPDW-II
-
-
-
-
EC 3.4.12.1
-
-
formerly
-
EC 3.4.16.1
-
-
formerly
-
EC 3.4.21.13
-
-
formerly
-
gene KEX1 serine carboxypeptidase
-
-
-
-
h-TLL
-
the transthyretin-like domain belonging to the first catalytic domain of human metallocarboxypeptidase D
KEX1 carboxypeptidase
-
-
-
-
KEX1 proteinase
-
-
-
-
Saccharomyces cerevisiae KEX1 gene product
-
-
-
-
CPD
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
preferential release of a C-terminal arginine or lysine residue
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
153967-26-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-factor-Lys-Arg + H2O
mature active alpha-factor + Lys + Arg
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Substrates: maturation takes place in sequential manner
Products: -
Products: -
?
angiotensin 1 + H2O
?
-
Substrates: truncated KexA releases amino acid residues from the C terminus of angiotensin I
Products: -
Products: -
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + L-arginine
-
Substrates: enzyme shows very low activity
Products: -
Products: -
?
benzoyl-Phe-Ala-Arg + H2O
benzoyl-Phe-Ala + Arg
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Gly-Lys + H2O
benzyloxycarbonyl-Gly + L-lysine
-
Substrates: enzyme shows very low activity
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + L-leucine
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Substrates: enzyme shows very low activity
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Tyr-Leu + H2O
benzyloxycarbonyl-Phe-Tyr + L-leucine
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Tyr-Leu + H2O
benzyloxycarbonyl-Tyr + L-leucine
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Substrates: enzyme shows very low activity
Products: -
Products: -
?
bradykinin I + H2O
?
-
Substrates: truncated KexA releases amino acid residues from the C terminus of bradykinin I
Products: -
Products: -
?
Dansyl-Phe-Ala-Arg + H2O
Dansyl-Phe-Ala + Arg
-
Substrates: -
Products: -
Products: -
?
furylacryloyl-Ala-Lys + H2O
furylacryloyl-Ala + Lys
-
Substrates: -
Products: -
Products: -
?
dansyl-L-Ala-L-Arg + H2O
dansyl-L-Ala + L-Arg
-
Substrates: -
Products: -
Products: -
?
furylacryloyl-Ala-Arg + H2O
furylacryloyl-Ala + Arg
-
Substrates: -
Products: -
Products: -
?
furylacryloyl-Ala-Arg + H2O
furylacryloyl-Ala + Arg
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Substrates: activity assay
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme functions in processing of proteins that transit the secretory pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferential release of a C-terminal arginine or lysine residue
Products: -
Products: -
?
additional information
?
-
Substrates: specificity
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme has a narrow specificity for lysyl ar arginyl residues at the C-terminus of the substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has a narrow specificity for lysyl ar arginyl residues at the C-terminus of the substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: role in the processing of both the alpha-pheromone and the killer toxin precursors
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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)
Products: -
Products: -
?
additional information
?
-
-
Substrates: plays a role in polypeptide processing in yeast
Products: -
Products: -
?
additional information
?
-
-
Substrates: specific for the removal of basic amino acids from prohormone processing intermediates, in mammalian cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferential release of a C-terminal arginine or lysine residue
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
Substrates: the enzyme functions in processing of proteins that transit the secretory pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferential release of a C-terminal arginine or lysine residue
Products: -
Products: -
?
additional information
?
-
-
Substrates: role in the processing of both the alpha-pheromone and the killer toxin precursors
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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)
Products: -
Products: -
?
additional information
?
-
-
Substrates: plays a role in polypeptide processing in yeast
Products: -
Products: -
?
additional information
?
-
-
Substrates: specific for the removal of basic amino acids from prohormone processing intermediates, in mammalian cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: preferential release of a C-terminal arginine or lysine residue
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-[[(3,4-dinitrophenyl)carbonyl]amino]-2-(6-hydroxy-3-oxo-3H-xanthen-9-yl)benzoic acid
-
-
chymostatin
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pH 5.6, 50% inhibition at 13000 nM, pH 6.5, 50% inhibition at 2200 nM. Comparison with inhibitory effect on other peptidases
ebelactone B
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pH 5.6, 50% inhibition at 2100 nM, pH 6.5, 50% inhibition at 1500 nM. Comparison with inhibitory effect on other peptidases
lactacystin
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pH 5.6, 50% inhibition at 1400 nM, pH 6.5, 50% inhibition at 4300 nM. Comparison with inhibitory effect on other peptidases
omuralide
-
i.e. (1S,4S,5R)-1-[(1S)-1-hydroxy-2-methylpropyl]-4-methyl-6-oxa-2-azabicyclo[3.2.0]heptane-3,7-dione, pH 5.6, 50% inhibition at 4.8 nM, pH 6.5, 50% inhibition at 2 nM. Comparison with inhibitory effect on other peptidases
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.6
6.5 - 7
-
and 5.6. Activity maximum at pH 5.6 is due to activity of domain II, at pH 6.5-7.0 due to domain I
5.6
-
and 6.5-7.0. Activity maximum at pH 5.6 is due to activity of domain II, at pH 6.5-7.0 due to domain I
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cytokine-inducible isoform CPD-N with incomplete N-terminal domain and intact domains II and III
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-
brenda
KEX1 gene from Saccharomyces cerevisiae expressed using the baculovirus/insect cell system
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-
brenda
truncated KEX1 gene expressed in the baculovirus/insect cell system
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
Schneider 2 cell line, each splice variant of enzyme occurs in this cell line. Short enzyme forms containing a single carboxypeptidase domain are secreted from S2 cells, while long forms containing three carboxypeptidase domains, a transmembrane domain, and one out of two cytosolic domains are retained. C-terminal tail 2 leads to Golgi localization. The two C-terminal tails result in different internalization efficiencies from the cell surface
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme isoforms bearing C-terminal tail sequence 2
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
absence of Kex1p diminishes HOCl-induced production of reactive oxygen species, apoptosis and protein modification
malfunction
-
kexA deletion strain shows slightly lower growth speed. Deletion strain exhibits scarcely branched hyphae, whereas an kexA-overexpressing strain exhibits a hyperbranching phenotype
malfunction
-
LNCap cells treated with CPD siRNA show a decreased NO production and cell viability, but increased apoptosis
malfunction
-
targeted reduction of CPD in Huh7 cells results in decreased growth and enhanced apoptosis of Huh 7 cells in vitro
physiological function
-
CPD-mediated production of nitrix oxide promotes the survival of LNCaP cells
physiological function
-
protease Kex1p mediates HOCl-induced lethality
physiological function
CpD is the only endogenous carboxypeptidase that cleaves antibody heavy chain C-terminal lysine in CHO cells. Knockdown of CpD by RNAi increases C-terminal lysine levels of antibodies, whereas there is no obvious change in C-terminal lysine levels when carboxypeptidase CpM, CpN, CpB, or CpE is knocked downIn a CpD knockout mutant, C-terminal lysine cleavage is completely abolished
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8700
-
gel filtration of the transthyretin-like domain belonging to the first catalytic domain of human metallocarboxypeptidase D (h-TTL)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
-
the transthyretin-like domain belonging to the first catalytic domain of human metallocarboxypeptidase D (h-TTL) is a monomer in solution
additional information
additional information
-
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
additional information
-
enzyme co-immunoprecipitates with protein phosphatase 2A and alpha4 phosphoprotein
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E353Q
-
cells infected with the mutant enzyme show considerable carboxypeptidase activity, mutation eliminates the activity of domain 1
E771Q
-
cells infected with the mutant enzyme show considerable carboxypeptidase activity, mutation eliminates the activity of domain 2
additional information
additional information
-
enzyme is encoded by silver gene svr. Mutant lines svrPG33 do not survive past the early larval stage, having a P-element insertion upstream of the initiation ATG. Mutant lines svr1 and svrpoi are viable, with silvery body color and poited wings. svr1 gene has a three-nucleotide deletion in exon 6, svrpoi has a 1072-bp duplication of the gene that introduces a stop codon into the open reading frame. Both mutations eliminate enzyme activity of the second carboxypeptidase-like domain, which reduces levels of the long forms of enzyme but does not affect the levels of the short forms
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
maximum temperature at which the enzyme has residual activity of over 60% relative to maximum activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
archieved by a two-step chromatographic process using cation-exchange, SP Sepharose, followed by anion-exchange, DEAE Sepharose FF resin
-
domain 1B and 2 expressed in Sf9 cells using baculovirus expression system
-
KEX1 gene from Saccharomyces cerevisiae expressed using the baculovirus/insect cell system
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a truncated form of Kex-1, Kex-1-C611, is constructed comprising the amino acid residues from 104-611 and lacks the transmembrane domain
-
a truncated form of KexA (amino acid residues 1 to 526 of KexA), which lack the potential transmembrane region and the succeeding C-terminal sequence (amino acid residues 527 to 625 of KexA) is expressed by using a protein expression system with the pIECS3 vector and Aspergillus nidulans
-
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
-
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
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
Kex-1-C611 is proposed as a convenient biotechnological reagent for the cleavage of fusion proteins
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
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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
brenda
Liao, D.I.; Breddam, K.; Sweet, R.M.; Bullock, T.; Remington, S.J.
Refined atomic model of wheat serine carboxypeptidase II at 2.2-A resolution
Biochemistry
31
9796-9812
1992
Triticum aestivum
brenda
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
brenda
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
brenda
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
brenda