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Literature summary for 1.13.11.49 extracted from

  • Mahor, D.; Pueschmann, J.; Adema, D.R.; Strampraad, M.J.F.; Hagedoorn, P.L.
    Unexpected photosensitivity of the well-characterized heme enzyme chlorite dismutase (2020), J. Biol. Inorg. Chem., 25, 1129-1138 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) pLysS cells Azospira oryzae

General Stability

General Stability Organism
Illumination of the recombinantly expressed enzyme with a high-intensity light source results in disruption of the bond between FeIII and the axial histidine. This leads to the enzyme losing its heme cofactor and changing its oligomeric state and loss of activity Azospira oryzae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
140000
-
gel filtration Azospira oryzae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
chlorite Azospira oryzae
-
chloride + O2
-
?

Organism

Organism UniProt Comment Textmining
Azospira oryzae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-Sepharose 6 column chromatography Azospira oryzae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
chlorite
-
Azospira oryzae chloride + O2
-
?

Subunits

Subunits Comment Organism
homopentamer or homohexamer 5 or 6 * 30300, calculated from amino acid sequence Azospira oryzae

Synonyms

Synonyms Comment Organism
chlorite dismutase
-
Azospira oryzae
CLD
-
Azospira oryzae

Cofactor

Cofactor Comment Organism Structure
heme
-
Azospira oryzae