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Literature summary for 4.1.1.37 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)

Cloned (Comment) Organism
expressed in Escherichia coli Synechococcus elongatus

Inhibitors

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Synechococcus elongatus
-
strain PCC 7942
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
homodimer gel filtration Synechococcus elongatus

Temperature Stability [°C]

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