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Information on EC 4.1.1.84 - D-dopachrome decarboxylase and Organism(s) Homo sapiens and UniProt Accession P30046

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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:
Homo sapiens
UNIPROT: P30046
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
d-dopachrome decarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-dopachrome tautomerase
-
D-tautomerase
distinct from EC 5.3.3.12, dopachrome isomerase, and from EC 5.3.2.1, phenylpyruvate tautomerase or MIF
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
D-dopachrome
5,6-dihydroxyindole + CO2
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no inhibition by serum or plasma
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.42 - 0.44
D-dopachrome
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
25°C, pH 6.5, wild type enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
lung adenocarcinoma cell line
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
-
-
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DOPD_HUMAN
118
0
12712
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13000
x * 13000, SDS-PAGE
SUBUNIT
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P1A
enzyme activity extremely decreased
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA of 566 base pairs, expressed in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
strong correlation and covariation of enzyme activity with macrophage migration inhibitory factor, MIF, upon UVB-induction
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nishihira, J.; Fujinaga, M.; Kuriyama, T.; Suzuki, M.; Sugimoto, H.; Nakagawa, A.; Tanaka, I.; Sakai, M.
Molecular cloning of human D-dopachrome tautomerase cDNA: N-terminal proline is essential for enzyme activation
Biochem. Biophys. Res. Commun.
243
538-544
1998
Homo sapiens (P30046)
Manually annotated by BRENDA team
Sugimoto, H.; Taniguchi, M.; Nakagawa, A.; Tanaka, I.; Suzuki, M.; Nishihira, J.
Crystal structure of human D-dopachrome tautomerase, a homologue of macrophage migration inhibitory factor, at 1.54 A resolution
Biochemistry
38
3268-3279
1999
Homo sapiens (P30046)
Manually annotated by BRENDA team
Bjoerk, P.; Aman, P.; Hindemith, A.; Odh, G.; Jacobsson, L.; Rosengren, E.; Rorsman, H.
A new enzyme activity in human blood cells and isolation of the responsible protein (D-dopachrome tautomerase) from erythrocytes
Eur. J. Haematol.
57
254-256
1996
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Sonesson, B.; Rosengren, E.; Hansson, A.S.; Hansson, C.
UVB-induced inflammation gives increased d-dopachrome tautomerase activity in blister fluid which correlates with macrophage migration inhibitory factor
Exp. Dermatol.
12
278-282
2003
Homo sapiens (P30046)
Manually annotated by BRENDA team
Sugimoto, H.; Taniguchi, M.; Nakagawa, A.; Tanaka, I.; Suzuki, M.; Nishihira, J.
Crystallization and preliminary x-ray analysis of human D-dopachrome tautomerase
J. Struct. Biol.
120
105-108
1997
Homo sapiens (P30046)
Manually annotated by BRENDA team
Coleman, A.M.; Rendon, B.E.; Zhao, M.; Qian, M.W.; Bucala, R.; Xin, D.; Mitchell, R.A.
Cooperative regulation of non-small cell lung carcinoma angiogenic potential by macrophage migration inhibitory factor and its homolog, D-dopachrome tautomerase
J. Immunol.
181
2330-2337
2008
Mus musculus (O35215), Homo sapiens (P30046)
Manually annotated by BRENDA team
Garai, J.; Lorand, T.
Macrophage migration inhibitory factor (MIF) tautomerase inhibitors as potential novel anti-inflammatory agents: current developments
Curr. Med. Chem.
16
1091-1114
2009
Homo sapiens
Manually annotated by BRENDA team