4.1.1.37: uroporphyrinogen decarboxylase
This is an abbreviated version!
For detailed information about uroporphyrinogen decarboxylase, go to the full flat file.
Word Map on EC 4.1.1.37
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4.1.1.37
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porphyria
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cutanea
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tarda
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heme
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erythrocyte
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porphyrinogenic
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hexachlorobenzene
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urinary
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hepatoerythropoietic
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porphobilinogen
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overload
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photosensitivity
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ferrochelatase
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protoporphyrin
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hemochromatosis
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5-aminolaevulinate
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heptacarboxylic
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hexachlorobenzene-induced
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hypertrichosis
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phlebotomy
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erythropoietic
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delta-aminolaevulinic
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polyhalogenated
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5-aminolevulinic
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protoporphyrinogen
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uroporphyria
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tetrapyrrole
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sun-exposed
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blister
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siderosis
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diagnostics
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3,4,3\',4\'-tetrachlorobiphenyl
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medicine
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hcb-induced
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miliae
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coproporphyria
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bulla
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agriculture
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hepta
- 4.1.1.37
- porphyria
-
cutanea
- tarda
- heme
- erythrocyte
-
porphyrinogenic
- hexachlorobenzene
- urinary
-
hepatoerythropoietic
- porphobilinogen
- overload
-
photosensitivity
-
ferrochelatase
- protoporphyrin
- hemochromatosis
-
5-aminolaevulinate
-
heptacarboxylic
-
hexachlorobenzene-induced
- hypertrichosis
-
phlebotomy
-
erythropoietic
-
delta-aminolaevulinic
-
polyhalogenated
-
5-aminolevulinic
- protoporphyrinogen
-
uroporphyria
- tetrapyrrole
-
sun-exposed
- blister
- siderosis
- diagnostics
-
3,4,3\',4\'-tetrachlorobiphenyl
- medicine
-
hcb-induced
-
miliae
- coproporphyria
- bulla
- agriculture
-
hepta
Reaction
Synonyms
ch-UroD, Decarboxylase, uroporphyrinogen, Hem12p, PCL, Porphyrinogen carboxy-lyase, rl-UroD, tobacco UROD, UORO-D, UPD, URO-D, Uro-decarboxylase, uro-III decarboxylase, UroD, UROD protein, UROD1, uroporphyrinogen decarboxylase, uroporphyrinogen decarboxylase 1, Uroporphyrinogen III decarboxylase, uroporphyrinogen-decarboxylase, uroporphyrinogen-III decarboxylase
ECTree
4.1.1.37 uroporphyrinogen decarboxylaseAdvanced search results
results (
results (Engineering
Engineering on EC 4.1.1.37 - uroporphyrinogen decarboxylase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A80S
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less than 12% of the specific activity of wild-type enzyme, Q38R-glutathione S-transferase fusion protein
F217Y
G170D
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the missense mutation is associated with hepatoerythropoietic porphyria and shows erythrocyte UROD activity of 42% of normal. The recombinant UROD protein shows a relative activity of 17% and 60% of wild type to uroporphyrinogen I and III respectively
G318R
little effect on the structure or activity of recombinant uroporphyrinogen decarboxylase, but the protein displays reduced stability in vitro
K297N
little effect on the structure or activity of recombinant uroporphyrinogen decarboxylase, but the protein displays reduced stability in vitro
M1I
the absence of an initial methionine codon within the messenger RNA (mRNA) Kozac consensus sequence is predicted to lead to a loss of translation from the mutant allele
Q116X
this may yield a truncated protein of 115 amino acids or nonsense-mediated mRNA decay
Q38R
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less than 0.2% of the specific activity of wild-type enzyme, Q38R-glutathione S-transferase fusion protein
T160I
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3.4% of the specific activity of wild-type enzyme, Q38R-glutathione S-transferase fusion protein
Y164G
K150T
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the mutation does not have a significant effect on Vmax, but decreases Km by 25%
K150T/K219E/K277P
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the mutant shows no significant change in Km, but the Vmax increases by 3.7fold
additional information
F217Y
recombinant mutant of the single chain of both modules substrate uroporphyrinogen-I, 2.5% of recombinant wild-type
F217Y
recombinant mutant of the single chain of both modules substrate uroporphyrinogen-III, 14.5% of recombinant wild-type
F217Y
recombinant mutant of the single chain of the first module substrate uroporphyrinogen-I, 41.3% of recombinant wild-type
F217Y
recombinant mutant of the single chain of the first module substrate uroporphyrinogen-II, 50.9% of recombinant wild-type
F217Y
recombinant mutant of the single chain of the second module substrate uroporphyrinogen-I, 46.2% of recombinant wild-type
F217Y
recombinant mutant of the single chain of the second module substrate uroporphyrinogen-III, 52.7% of recombinant wild-type
F217Y
recombinant mutant substrate uroporphyrinogen-I, 2.6% of recombinant wild-type
Y164G
recombinant mutant of the single chain of the first module substrate uroporphyrinogen-I, 13.2% of recombinant wild-type
Y164G
recombinant mutant substrate uroporphyrinogen-I, 8.1% of recombinant wild-type
additional information
5del10, this may yield a truncated protein of 115 amino acids or nonsense-mediated mRNA decay
additional information
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5del10, this may yield a truncated protein of 115 amino acids or nonsense-mediated mRNA decay
additional information
construction of a single-chain protein (single-chain URO-D) in which the two subunits are connected by a flexible linker. The crystal structure of this protein is shown to be superimposable with wild-type activity and to have comparable catalytic activity
additional information
variants of the linked dimer in which either of the active sites is inactivated by site-directed mutagenesis maintained approximately half of the wildtype catalytic activity, all four decarboxylations can be catalyzed at a single active site and shuttling of intermediates between active sites of the uroporphyrinogen decarboxylase dimer is not required
