Information on EC 4.1.1.84 - D-dopachrome decarboxylase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.1.1.84
-
RECOMMENDED NAME
GeneOntology No.
D-dopachrome decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-dopachrome = 5,6-dihydroxyindole + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
intramolecular oxidoreduction
-
-
SYSTEMATIC NAME
IUBMB Comments
D-dopachrome carboxy-lyase (5,6-dihydroxyindole-forming)
This enzyme is specific for D-dopachrome as substrate and belongs to the MIF (macrophage migration inhibitory factor) family of proteins. L-Dopachrome, L- or D-alpha-methyldopachrome and dopaminochrome do not act as substrates (see also EC 5.3.3.12, L-dopachrome isomerase)
CAS REGISTRY NUMBER
COMMENTARY hide
184111-06-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-hydroxyphenylpyruvate
4-hydroxyphenylpyruvate
show the reaction diagram
-
enol form
keto form
?
D-dopachrome
5,6-dihydroxyindole + CO2
show the reaction diagram
indole-3-pyruvate
indole-3-pyruvate
show the reaction diagram
-
enol form
keto form
?
Phenylpyruvate
Phenylpyruvate
show the reaction diagram
-
enol form
keto form
?
additional information
?
-
no substrates are: L-dopachrome, dopaminochrome, L-alpha-methyldopachrome, D-alpha-methyldopachrome
-
?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-hydroxyphenylpyruvate
-
competitive
additional information
-
no inhibition by serum or plasma
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.42 - 1.5
D-dopachrome
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.5
-
pH 6.0, 25C
100
-
25C, pH 6.5, wild type enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
broad
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.09
-
calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
lung adenocarcinoma cell line
Manually annotated by BRENDA team
-
murine embryonic fibroblast
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12000
-
3 * 12000, SDS-PAGE
12500
-
3 * 12500, SDS-PAGE
13000
-
x * 13000, SDS-PAGE
13130
-
calculated
37000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 13000, SDS-PAGE
dimer
-
and trimer, crystallization data
trimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dimeric and trimeric enzyme and its selenomethyl derivative
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
5 min, loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, pH 5.5-9.0, several weeks, stable
-
25C, overnight, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA of 566 base pairs, expressed in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P1A
-
enzyme activity extremely decreased
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine