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
-
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
- 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
Advanced search results
Reaction
Reaction on EC 4.2.1.75 - uroporphyrinogen-III synthase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
hydroxymethylbilane = uroporphyrinogen III + H2O
in the presence of hydroxymethylbilane synthase EC 4.3.1.8, enzyme forms uroporphyrinogen III from porphobilinogen, reaction mechanism, does not require acid/base catalysis, active site structure
-
hydroxymethylbilane = uroporphyrinogen III + H2O
in the presence of hydroxymethylbilane synthase EC 4.3.1.8, enzyme forms uroporphyrinogen III from porphobilinogen, reaction mechanism, does not require acid/base catalysis, active site structure
hydroxymethylbilane = uroporphyrinogen III + H2O
in the presence of hydroxymethylbilane synthase EC 4.3.1.8, enzyme forms uroporphyrinogen III from porphobilinogen, Tyr166 is essential for catalysis and/or substrate binding
-
hydroxymethylbilane = uroporphyrinogen III + H2O
reaction mechanism via azafulvene and azofulvene intermediates, the product binds between the two domains and is held in place by a network of hydrogen bonds between the products side chain carboxylates and the proteins main chain amides. Interactions of the product A and B ring carboxylate side chains with both structural domains of U3S appear to dictate the relative orientation of the domains in the closed enzyme conformation and likely remain intact during catalysis. The product C and D rings are less constrained in the structure, consistent with the conformational changes required for the catalytic cyclization with inversion of D ring orientation. A conserved tyrosine residue is potentially positioned to facilitate loss of a hydroxyl from the substrate to initiate the catalytic reaction, overview
hydroxymethylbilane = uroporphyrinogen III + H2O
reaction mechanism, modelling, overview
hydroxymethylbilane = uroporphyrinogen III + H2O
reaction mechanism, modeling involving Tyr168, overview
-
hydroxymethylbilane = uroporphyrinogen III + H2O
reaction mechanism via azafulvene and azofulvene intermediates, the product binds between the two domains and is held in place by a network of hydrogen bonds between the products side chain carboxylates and the proteins main chain amides. Interactions of the product A and B ring carboxylate side chains with both structural domains of U3S appear to dictate the relative orientation of the domains in the closed enzyme conformation and likely remain intact during catalysis. The product C and D rings are less constrained in the structure, consistent with the conformational changes required for the catalytic cyclization with inversion of D ring orientation. A conserved tyrosine residue is potentially positioned to facilitate loss of a hydroxyl from the substrate to initiate the catalytic reaction, overview
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-