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Literature summary for 1.3.3.4 extracted from

  • Zwerschke, D.; Karrie, S.; Jahn, D.; Jahn, M.
    Leishmania major possesses a unique HemG-type protoporphyrinogen IX oxidase (2014), Biosci. Rep., 34, 391-400 .
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
gene LMJF_06_1280, the gene forms a potential transcriptional unit with gene LMJF_06_1270 encoding CPO, coproporphyrinogen III oxidase, EC 1.3.3.3, and with gene LMJF_06_1290 for a cytochrome b5, functional complementation of the Escherichia coli C43(DE3) LG285 DELTAhemG strain, recombinant expression of wild-type and mutant enzymes Leishmania major

Protein Variants

Protein Variants Comment Organism
R142A site-directed mutagenesis, the mutant shows 50fold reduced activity compared to the wild-type enzyme Leishmania major
Y134F site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Leishmania major
Y137A site-directed mutagenesis, inactive mutant Leishmania major
Y137F site-directed mutagenesis, inactive mutant Leishmania major
Y137S site-directed mutagenesis, inactive mutant Leishmania major

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Leishmania major the enzyme from Leishmania major also shows a physiological ferrochelatase activity ?
-
?
protoporphyrinogen IX + 3 O2 Leishmania major
-
protoporphyrin IX + 3 H2O2
-
?

Organism

Organism UniProt Comment Textmining
Leishmania major Q4QIU7
-
-

Source Tissue

Source Tissue Comment Organism Textmining
amastigote
-
Leishmania major
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme from Leishmania major also shows a physiological ferrochelatase activity Leishmania major ?
-
?
additional information purified recombinant Leishmania major HemG gene product reveals PPO activity in vitro using different ubiquinones and triphenyltetrazolium as electron acceptors. FMN is identified as the physiological Leishmania major HemG cofactor Leishmania major ?
-
?
protoporphyrinogen IX + 3 O2
-
Leishmania major protoporphyrin IX + 3 H2O2
-
?

Subunits

Subunits Comment Organism
? x * 42000, recombinant wild-type enzyme, SDS-PAGE Leishmania major

Synonyms

Synonyms Comment Organism
HemG
-
Leishmania major
HemG-type PPO
-
Leishmania major
HemG-type protoporphyrinogen IX oxidase
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Leishmania major
LMJF_06_1280
-
Leishmania major

Cofactor

Cofactor Comment Organism Structure
FMN
-
Leishmania major
additional information purified recombinant Leishmania major HemG gene product reveals PPO activity in vitro using different ubiquinones and triphenyltetrazolium as electron acceptors. FMN is identified as the physiological Leishmania major HemG cofactor Leishmania major

General Information

General Information Comment Organism
evolution HemG proteins are highly related to flavodoxin proteins, crystal structure analysis Leishmania major
additional information the active site residues are essential for HemG catalysis, spectral analysis of heme biosynthesis, overview Leishmania major
physiological function the enzyme also shows a physiological ferrochelatase activity. Partial heme biosynthesis from phagocyte-derived heme precursors in Leishmania major is highly probable. It serves most probably to haemoprotein formation during the amastigotic state in the macrophage, model for the intracellular localization of heme synthetic enzymes and heme trafficking in Leishmania major amastigotes, overview Leishmania major