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Literature summary for 1.3.98.3 extracted from

  • Goto, T.; Aoki, R.; Minamizaki, K.; Fujita, Y.
    Functional differentiation of two analogous coproporphyrinogen III oxidases for heme and chlorophyll biosynthesis pathways in the cyanobacterium Synechocystis sp. PCC 6803 (2010), Plant Cell Physiol., 51, 650-663.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
DTT added to the assay at 2 mM Synechocystis sp.
NADH added to the assay at 0.5 mM Synechocystis sp.

Cloned(Commentary)

Cloned (Comment) Organism
genes sll1876 and sll1917, overexpression of N-terminally Strep-tagged HemNs in Escherichia coli Synechocystis sp.

Protein Variants

Protein Variants Comment Organism
additional information construction of deletion mutants of the HemN genes, growth of the mutant DELTAsll1876 is significantly slower than that of the wild-type under microoxic conditions, while it grows normally under aerobic conditions. Coproporphyrin III is accumulated at a low but significant level in the DELTAsll1876 mutant grown under micro-oxic conditions. No detectable phenotype in DELTAsll1917 under the conditions, phenotypes, overview Synechocystis sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
coproporphyrinogen III + 2 S-adenosyl-L-methionine Synechocystis sp. sll1876 encodes HemN operating under micro-oxic conditions protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
?

Organism

Organism UniProt Comment Textmining
Synechocystis sp.
-
two hemN genes, sll1876 and sll1917
-

Purification (Commentary)

Purification (Comment) Organism
recombinant terminally Strep-tagged HemNs from Escherichia coli to homogeneity Synechocystis sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
coproporphyrinogen III + 2 S-adenosyl-L-methionine sll1876 encodes HemN operating under micro-oxic conditions Synechocystis sp. protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
?
coproporphyrinogen III + 2 S-adenosyl-L-methionine only Sll1876 shows CPO activity under anaerobic conditions, Sll1917 is inactive Synechocystis sp. protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
?

Synonyms

Synonyms Comment Organism
coproporphyrinogen III oxidase
-
Synechocystis sp.
CPO
-
Synechocystis sp.
Sll1876
-
Synechocystis sp.
Sll1917
-
Synechocystis sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Synechocystis sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Synechocystis sp.

Cofactor

Cofactor Comment Organism Structure
iron-sulfur centre in Sll1876 and Sll1917 Synechocystis sp.
S-adenosyl-L-methionine
-
Synechocystis sp.

General Information

General Information Comment Organism
physiological function catalyzes the decarboxylation of coproporphyrinogen III to form protoporphyrinogen IX in heme biosynthesis and is shared in chlorophyll biosynthesis in photosynthetic organisms Synechocystis sp.