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Literature summary for 1.4.1.13 extracted from

  • Jeelani, G.; Husain, A.; Sato, D.; Ali, V.; Suematsu, M.; Soga, T.; Nozaki, T.
    Two atypical L-cysteine-regulated NADPH-dependent oxidoreductases involved in redox maintenance, L-cystine and iron reduction, and metronidazole activation in the enteric protozoan Entamoeba histolytica (2010), J. Biol. Chem., 285, 26889-26899.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, sequence comparison, quantitative real-time PCR expression analysis, recombinant expression in Escherichia coli strain BL21(DE3) Entamoeba histolytica

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ 2[4Fe-4S]-containing enzyme Entamoeba histolytica

Organism

Organism UniProt Comment Textmining
Entamoeba histolytica C4LUA1 EhNO1
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Entamoeba histolytica C8KIP3 EhNO2
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Entamoeba histolytica HM1:IMSS cl 6 C4LUA1 EhNO1
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Entamoeba histolytica HM1:IMSS cl 6 C8KIP3 EhNO2
-

Source Tissue

Source Tissue Comment Organism Textmining
trophozoite
-
Entamoeba histolytica
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the FAD and 2[4Fe-4S]-containing enzyme does not act as glutamate synthase, which is supported by phylogenetic analyses. Rather, it catalyzes the NADPH-dependent reduction of oxygen to hydrogen peroxide and L-cystine to L-cysteine and also function as ferric and ferredoxin-NADP+ reductase. EhNO1 and EhNO2 show notable differences in substrate specificity and catalytic efficiency. EhNO1 has lower Km and higher kcat/Km values for ferric ion and ferredoxin than EhNO2, whereas EhNO2 prefers L-cystine as a substrate. EhNO1 and EhNO2 also reduce metronidazole Entamoeba histolytica ?
-
?
additional information the FAD and 2[4Fe-4S]-containing enzyme does not act as glutamate synthase, which is supported by phylogenetic analyses. Rather, it catalyzes the NADPH-dependent reduction of oxygen to hydrogen peroxide and L-cystine to L-cysteine and also function as ferric and ferredoxin-NADP+ reductase. EhNO1 and EhNO2 show notable differences in substrate specificity and catalytic efficiency. EhNO1 has lower Km and higher kcat/Km values for ferric ion and ferredoxin than EhNO2, whereas EhNO2 prefers L-cystine as a substrate. EhNO1 and EhNO2 also reduce metronidazole Entamoeba histolytica HM1:IMSS cl 6 ?
-
?

Synonyms

Synonyms Comment Organism
EhNO1
-
Entamoeba histolytica
EhNO2
-
Entamoeba histolytica
GOGAT
-
Entamoeba histolytica

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Entamoeba histolytica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Entamoeba histolytica

Cofactor

Cofactor Comment Organism Structure
FAD
-
Entamoeba histolytica
NADPH
-
Entamoeba histolytica

General Information

General Information Comment Organism
physiological function the small subunit-like protein of glutamate synthase might play an important role in redox maintenance, L-cysteine/L-cystine homeostasis, iron reduction, and the activation of metronidazole Entamoeba histolytica