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Literature summary extracted from

  • Saito, M.; Watanabe, S.; Yoshikawa, H.; Nakamoto, H.
    Interaction of the molecular chaperone HtpG with uroporphyrinogen decarboxylase in the cyanobacterium Synechococcus elongatus PCC 7942 (2008), Biosci. Biotechnol. Biochem., 72, 1394-1397.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.37 expressed in Escherichia coli Synechococcus elongatus

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.37 HtpG suppresses HemE activity at 0.25 nmol or 1.25 nmol Synechococcus elongatus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.37 64000
-
SDS-PAGE Synechococcus elongatus

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.37 Synechococcus elongatus
-
strain PCC 7942
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.37 Ni-NTA column chromatography Synechococcus elongatus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.37 Uroporphyrinogen III
-
Synechococcus elongatus Coproporphyrinogen III + 4 CO2
-
?

Subunits

EC Number Subunits Comment Organism
4.1.1.37 homodimer gel filtration Synechococcus elongatus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.1.1.37 45
-
the HemE dimer is stable up to 45°C Synechococcus elongatus