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Information on EC 3.4.14.4 - dipeptidyl-peptidase III and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q08225

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Saccharomyces cerevisiae
UNIPROT: Q08225 not found.
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides.
Synonyms
dpp iii, dipeptidyl peptidase iii, nudt3, enkephalinase b, dppiii, dpp-iii, dipeptidyl aminopeptidase iii, dipeptidyl-peptidase iii, dipeptidylpeptidase iii, dipeptidyl-peptide hydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dipeptidyl peptidase III
-
dipeptidyl aminopeptidase III
-
-
-
-
dipeptidyl arylamidase III
-
-
-
-
dipeptidyl-peptide hydrolase
-
-
-
-
dipeptidylpeptidase III
-
-
-
-
enkephalinase B
-
-
-
-
peptidase, dipeptidyl, III
-
-
-
-
red cell angiotensinase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
77464-87-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ala-Ala-2-naphthylamide + H2O
Ala-Ala + 2-naphthylamine
show the reaction diagram
-
-
-
?
Ala-Phe-2-naphthylamide + H2O
Ala-Phe + 2-naphthylamine
show the reaction diagram
-
-
-
?
Arg-Arg-2-naphthylamide + H2O
Arg-Arg + 2-naphthylamine
show the reaction diagram
assay at pH 8.0, 37°C
-
-
?
His-Ser-2-naphthylamide + H2O
His-Ser + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Ala-L-Ala 2-naphthylamide + H2O
L-Ala-L-Ala + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Arg-L-Arg 2-naphthylamide + H2O
L-Arg-L-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
?
Ala-Ala-2-naphthylamide + H2O
Ala-Ala + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
Ala-Arg-2-naphthylamide + H2O
Ala-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
Arg-Arg-2-naphthylamide + H2O
Arg-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
Leu-Gly-2-naphthylamide + H2O
Leu-Gly + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
Lys-Ala-2-naphthylamide + H2O
Lys-Ala + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
10-100 micromol, potent activation
Zn2+
10 micromol, strong inhibition
Co2+
-
increase of activity
Zn2+
-
zinc-dependent enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4,4'-dithiodipyridine
inactivation of wild-type dipeptidyl peptidase III after incubation at pH 8.0 at 25°C, after 5 min incubation loss of 30% enzyme activity, after 15 min incubation loss of 62% enzyme activity
Zn2+
10 micromol, strong inhibition
1,10-phenanthroline
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
p-chloromercuribenzoate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00889 - 0.01518
Arg-Arg-2-naphthylamide
0.0945 - 0.2316
L-Ala-L-Ala 2-naphthylamide
0.0026 - 0.0251
L-Arg-L-Arg 2-naphthylamide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09 - 0.334
Arg-Arg-2-naphthylamide
0.002 - 7.25
L-Ala-L-Ala 2-naphthylamide
0.003 - 0.953
L-Arg-L-Arg 2-naphthylamide
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10.21 - 32.58
Arg-Arg-2-naphthylamide
0.012 - 76.7
L-Ala-L-Ala 2-naphthylamide
0.133 - 3202
L-Arg-L-Arg 2-naphthylamide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
the protein exists in a mono- and dimeric form, X-ray crystallography
monomer
-
the protein exists in a mono- and dimeric form, X-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the C130S mutant is crystallized by sitting drop vapour diffusion method, in 20% (w/v) polyethylene glycol 3350 and 900 mM MgCl2 in 100 mM Tris-HCl (pH 7.0)
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C113S
mutation of the cysteine residue
C130S
mutant, only existence of dimeric form
C518S
mutation of the cysteine residue
C626S
mutation of the cysteine residue
C639S
mutant, resistance against p-hydroxy-mercuribenzoate
H578D
mutation 122fold lowers the catalytic efficiency for Arg-Arg 2-naphthylamide hydrolysis, and 14fold decreases affinity for hydroxamate inhibitor Tyr-Phe-NHOH
K638L
mutation slightly increases the specificity constant for Arg-Arg 2-naphthylamide hydrolysis. The affinity for Tyr-Phe-NHOH, and activity for the substrates with uncharged P2 side chains such as Ala-Ala-, Ala-Arg- and Phe-Arg 2-naphthylamide are dramatically reduced
R582Q
mutant exhibits an order of magnitude higher activity with all four dipeptide derivatives examined, compared to the wild type, due to a change in the H-bond networking in the R582Q variant active-site region
C130S
-
the mutant exhibits comparable enzymatic activity to the wild type protein
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
4,4'-dithiodipyridine, inactivation of wild-type dipeptidyl peptidase III after incubation at pH 8.0 at 25°C, after 5 min incubation loss of 30% enzyme activity, after 15 min incubation loss of 62% enzyme activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
gel filtration and FPLC on Mono Q column
Ni-NTA resin column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21
expressed in Escherichia coli strain BL21-CodonPlus(DE3)-RIL
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Watanabe, Y.; Kumagai, Y.; Fujimoto, Y.
Presence of a dipeptidyl aminopeptidase III in Saccharomyces cerevisiae
Chem. Pharm. Bull.
38
246-248
1990
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Baral, P.K.; Jajcanin-Jozic, N.; Deller, S.; Macheroux, P.; Abramic, M.; Gruber, K.
The first structure of dipeptidyl-peptidase III provides insight into the catalytic mechanism and mode of substrate binding
J. Biol. Chem.
283
22316-22324
2008
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
Manually annotated by BRENDA team
Jajcanin-Jozic, N.; Deller, S.; Pavkov, T.; Macheroux, P.; Abramic, M.
Identification of the reactive cysteine residues in yeast dipeptidyl peptidase III
Biochimie
92
89-96
2010
Saccharomyces cerevisiae (Q08225), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Jajcanin-Jozic, N.; Tomic, S.; Abramic, M.
Importance of the three basic residues in the vicinity of the zinc-binding motifs for the activity of the yeast dipeptidyl peptidase III
J. Biochem.
155
43-50
2014
Saccharomyces cerevisiae (Q08225), Saccharomyces cerevisiae
Manually annotated by BRENDA team