Information on EC 3.4.14.6 - dipeptidyl-dipeptidase

for references in articles please use BRENDA:EC3.4.14.6
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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
3.4.14.6
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RECOMMENDED NAME
GeneOntology No.
dipeptidyl-dipeptidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
preferential release of dipeptides from a tetrapeptide, e.g. Ala-Gly-/-Ala-Gly. Acts more slowly on Ala-Ala-/-Ala-Ala and Gly-Gly-/-Gly-Gly
show the reaction diagram
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dipeptidyl ligase activity
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-
hydrolysis of peptide bond
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-
exopeptidase, N-terminus, dipeptide
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CAS REGISTRY NUMBER
COMMENTARY hide
91608-92-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cabbage
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ala-Gly
Ala-Gly-Ala-Gly + H2O
show the reaction diagram
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-
-
r
Ala-Gly-Ala-Gly + H2O
2 Ala-Gly
show the reaction diagram
-
-
-
r
Gly-Gly + H2O
Gly-Gly-Gly-Gly
show the reaction diagram
-
-
-
r
Gly-Gly-Gly-Gly + H2O
Gly-Gly
show the reaction diagram
-
-
-
r
Gly-L-Ala + H2O
Gly-Ala-Gly-Ala
show the reaction diagram
-
-
-
?
L-Ala-L-Ala + H2O
Ala-Ala-Ala-Ala
show the reaction diagram
-
-
-
?
L-Met-Gly + H2O
?
show the reaction diagram
-
very slowly
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-
?
additional information
?
-
-
tetrapeptides are formed from Ala-Ala, Gly-Gly, Ala-Gly and Gly-Ala without prior activation of the carboxyl group, condensation reaction: substrate specificity for a dipeptide with either two Ala residues or one Ala and one Gly residue, not hydrolyzed: pentaglycine, no condensation reaction with: Ser-Gly, Ala-Ala-Gly, Gly-Gly-Ala, Gly-Gly-Gly, Gly-Gly-leu, beta-Ala-Gly, Gly-leu, D-Ala-L-Ala, Gly-D-Ala
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diisopropylfluorophosphate
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alone slightly and in combination with p-hydroxymercuribenzoate strong
dithiothreitol
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slight
p-hydroxymercuribenzoate
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puromycin
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0.005 M: no effect, 0.025 M: complete inhibition, Ala-Gly-Ala-Gly synthesis
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiols
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activate, strict requirement for reduced sulfhydryl group
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00867
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-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.8
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pH 6.0: about 50% of activity maximum, pH 8.8: about 5% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
enzyme activity is promoted by integrin subunit alpha2 blockade but decreased after subunit alpha6 blockade. Proliferative blockade using mitomycin C or hydroxyurea prevent the effects of subunit alpha2 ligation on differentiation
Manually annotated by BRENDA team
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 3.4.14.6)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)