Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Mauzerall, D.; Granick, S.
    Porphyrin biosynthesis in erythrocytes. III. Uroporphyrinogen and its decarboxylase (1958), J. Biol. Chem., 232, 1141-1162.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.37 Cu2+ strong Oryctolagus cuniculus
4.1.1.37 Hg2+ strong Oryctolagus cuniculus
4.1.1.37 iodoacetamide strong Oryctolagus cuniculus
4.1.1.37 Mn2+ strong Oryctolagus cuniculus
4.1.1.37 O2 autooxidation of uroporphyrinogen Oryctolagus cuniculus
4.1.1.37 PCMB strong Oryctolagus cuniculus

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.37 Oryctolagus cuniculus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.1.1.37 reticulocyte
-
Oryctolagus cuniculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.37 uroporphyrinogen I at 50% of the activity with uroporphyrinogen III Oryctolagus cuniculus coproporphyrinogen I + 4 CO2
-
?
4.1.1.37 Uroporphyrinogen III
-
Oryctolagus cuniculus Coproporphyrinogen III + 4 CO2
-
?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.37 6.8
-
-
Oryctolagus cuniculus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.1.1.37 5.3 8 pH 5.3: about 60% of maximal activity, pH 8.0: about 65% of maximal activity Oryctolagus cuniculus