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Information on EC 4.1.1.84 - D-dopachrome decarboxylase and Organism(s) Rattus norvegicus and UniProt Accession P80254

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.84 D-dopachrome decarboxylase
IUBMB Comments
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)
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This record set is specific for:
Rattus norvegicus
UNIPROT: P80254
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The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
d-dopachrome decarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-dopachrome tautomerase
-
-
phenylpyruvate tautomerase
-
identical with phenylpyruvate tautomerase, EC 5.3.2.1
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-dopachrome = 5,6-dihydroxyindole + CO2
show the reaction diagram
animal experiments with CCl4 injections, results suggest that the increase in DDT is a response to liver damage, accelerates melanin biosynthesis and protects the liver from oxidative stress induced by CCl4
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-dopachrome
5,6-dihydroxyindole + CO2
show the reaction diagram
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
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-hydroxyphenylpyruvate
-
competitive
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5
D-dopachrome
pH 6.0, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.5
pH 6.0, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.09
-
calculated
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DOPD_RAT
118
0
13133
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12000
3 * 12000, SDS-PAGE
12500
3 * 12500, SDS-PAGE
37000
gel filtration
13130
-
calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
5 min, loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, pH 5.5-9.0, several weeks, stable
25°C, overnight, stable
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
DDT may be candidates for key enzymes to protect the liver from oxidative stress induced by various causes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Odh, G.; Hindemith, A.; Rosengren, A-M.; Rosengren, E.; Rorsman, H.
Isolation of a new tautomerase monitored by the conversion of D-dopachrome to 5,6-dihydroxyindole
Biochem. Biophys. Res. Commun.
197
619-624
1993
Rattus norvegicus (P80254)
Manually annotated by BRENDA team
Yoshida, H.; Nishihira, J.; Suzuki, M.; Hikichi, K.
NMR characterization of physicochemical properties of rat D-dopachrome tautomerase
Biochem. Mol. Biol. Int.
42
891-899
1997
Rattus norvegicus (P80254)
Manually annotated by BRENDA team
Rosengren, E.; Thelin, S.; Aman, P.; Hansson, C.; Jacobsson, L.; Rorsman, H.
The protein catalysing the conversion of D-dopachrome to 5,6-dihydroxyindole is a phenylpyruvate tautomerase (EC 5.3.2.1)
Melanoma Res.
7
517-518
1997
Rattus norvegicus
Manually annotated by BRENDA team
Hiyoshi, M.; Konishi, H.; Uemura, H.; Matsuzaki, H.; Tsukamoto, H.; Sugimoto, R.; Takeda, H.; Dakeshita, S.; Kitayama, A.; Takami, H.; Sawachika, F.; Kido, H.; Arisawa, K.
D-Dopachrome tautomerase is a candidate for key proteins to protect the rat liver damaged by carbon tetrachloride
Toxicology
255
6-14
2009
Rattus norvegicus
Manually annotated by BRENDA team