4.2.1.75: uroporphyrinogen-III synthase
This is an abbreviated version!
For detailed information about uroporphyrinogen-III synthase, go to the full flat file.
Word Map on EC 4.2.1.75
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4.2.1.75
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porphyria
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erythropoietic
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heme
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photosensitivity
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5-aminolevulinic
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tetrapyrrole
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coproporphyrins
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delta-aminolevulinic
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ferrochelatase
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pbgase
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mutilate
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erythrodontia
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transfusion-dependent
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protoporphyria
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hypertrichosis
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urologists
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coproporphyrinogen
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aymaras
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amerindian
- 4.2.1.75
- porphyria
-
erythropoietic
- heme
-
photosensitivity
-
5-aminolevulinic
- tetrapyrrole
- coproporphyrins
-
delta-aminolevulinic
-
ferrochelatase
-
pbgase
-
mutilate
-
erythrodontia
-
transfusion-dependent
- protoporphyria
-
hypertrichosis
-
urologists
- coproporphyrinogen
-
aymaras
-
amerindian
Reaction
Synonyms
CobA/HemD, Hydroxymethylbilane hydrolyase [cyclizing], hydroxymethylbilane hydrolyase, cyclizing, Isomerase, uroporphyrinogen, Porphobilinogenase, Synthase, uroporphyrinogen III co-, U3S, URO synthase, uro'gen III synthase, URO-synthase, UROIIIS, Uroporphyrinogen III co-synthase, Uroporphyrinogen III cosynthase, Uroporphyrinogen III synthase, Uroporphyrinogen isomerase, Uroporphyrinogen-III cosynthase, Uroporphyrinogen-III cosynthetase, uroporphyrinogen-III-synthase, UROS
ECTree
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Temperature Stability
Temperature Stability on EC 4.2.1.75 - uroporphyrinogen-III synthase
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30
37
about 20% loss of activity after 48 h, about 50% loss of activity after 72 h, buffer containing 1 mM DTT
45
60
additional information
additional information
purified enzyme shows remarkable thermostability, particularly when kept in phosphate buffer containing DTT and EDTA, indicating that the activity may depend on its oxidation state
additional information
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purified enzyme shows remarkable thermostability, particularly when kept in phosphate buffer containing DTT and EDTA, indicating that the activity may depend on its oxidation state
additional information
UROIIIS is a thermolabile enzyme undergoing irreversible denaturation, unfolding kinetics of wild-type UROIIIS and mutants, circular dichroism, overview. A helical region in the molecule is essential to retain the kinetic stability of the folded conformation
additional information
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UROIIIS is a thermolabile enzyme undergoing irreversible denaturation, unfolding kinetics of wild-type UROIIIS and mutants, circular dichroism, overview. A helical region in the molecule is essential to retain the kinetic stability of the folded conformation
additional information
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the enzyme is metathermostabile, irreversible denaturation process. At physiological temperature and in vitro, UROIIIS has a half-life time of 61.1 h, a long time for the enzyme to exert its function in the cell, dynamic behavior of the protein, three-state model, overview. Thermodynamic versus kinetic stability, overview