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Literature summary for 1.18.1.2 extracted from
- The apicomplexan Cryptosporidium parvum possesses a single mitochondrial-type ferredoxin and ferredoxin:NADP+ reductase system (2010), Protein Sci., 19, 2073-2084.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| mtFNR, sequence comparison and phylogenetic analysis, real-time quantitative RT-PCR expression ananlysis, recombinant expression of the His-tagged enzyme in Escherichia coli strain Rosetta (DE3) | Cryptosporidium parvum |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics, overview | Cryptosporidium parvum | |
| 0.0037 | - |
NADPH | pH 7.4, temperature not specified in the publication, recombinant enzyme | Cryptosporidium parvum |  |
| 0.0094 | - |
NADPH | pH 8.2, temperature not specified in the publication, recombinant enzyme | Cryptosporidium parvum | |
| 0.0242 | - |
NADPH | pH 6.8, temperature not specified in the publication, recombinant enzyme | Cryptosporidium parvum | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| mitochondrion | mtFNR | Cryptosporidium parvum | 5739 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 reduced ferredoxin + NADP+ | Cryptosporidium parvum | - |
2 oxidized ferredoxin + NADPH + H+ | - |
r | |
| 2 reduced ferredoxin + NADP+ | Cryptosporidium parvum IOWA-1 | - |
2 oxidized ferredoxin + NADPH + H+ | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Cryptosporidium parvum | - |
single copy FNR | - |
| Cryptosporidium parvum IOWA-1 | - |
single copy FNR | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged mtFNR to homogeneity from Escherichia coli by nickel affinity chromatography | Cryptosporidium parvum |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| additional information | CpmtFd and CpmtFNR genes are constitutively transcribed during the complex parasite life cycle, real-time quantitative RT-PCR expression analysis, overview | Cryptosporidium parvum | - |
| sporozoite | - |
Cryptosporidium parvum | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 reduced ferredoxin + NADP+ | - |
Cryptosporidium parvum | 2 oxidized ferredoxin + NADPH + H+ | - |
r | |
| 2 reduced ferredoxin + NADP+ | cyt c-coupled assay, electron transfer system, overview | Cryptosporidium parvum | 2 oxidized ferredoxin + NADPH + H+ | - |
r | |
| 2 reduced ferredoxin + NADP+ | - |
Cryptosporidium parvum IOWA-1 | 2 oxidized ferredoxin + NADPH + H+ | - |
r | |
| 2 reduced ferredoxin + NADP+ | cyt c-coupled assay, electron transfer system, overview | Cryptosporidium parvum IOWA-1 | 2 oxidized ferredoxin + NADPH + H+ | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the mtFNR enzymatic region contains at least six highly conserved domains or motifs, including three FAD-diphosphate binding and one NADP+-diphosphate binding motifs | Cryptosporidium parvum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ferredoxin:NADP+ reductase | - |
Cryptosporidium parvum |
| mitochondrial-type ferredoxin:NADP+ reductase | - |
Cryptosporidium parvum |
| mtFNR | - |
Cryptosporidium parvum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Cryptosporidium parvum |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.24 | - |
NADPH | pH 7.4, temperature not specified in the publication, recombinant enzyme | Cryptosporidium parvum | |
| 0.6 | - |
NADPH | pH 8.2, temperature not specified in the publication, recombinant enzyme | Cryptosporidium parvum | |
| 21.71 | - |
NADPH | pH 6.8, temperature not specified in the publication, recombinant enzyme | Cryptosporidium parvum | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.8 | - |
- |
Cryptosporidium parvum |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6.8 | 8.2 | assay range | Cryptosporidium parvum |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | - |
Cryptosporidium parvum | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | in the photosystem I, an oxidized ferredoxin molecule, Fdox, first receives an electron driven by light energy to form a reduced ferredoxin, Fdred. The FAD-containing FNR then catalyzes the transfer of the electron to NADP+, which recycles Fdred back to Fdox. On the other hand, FNR mainly catalyzes the conversion from Fdox to Fdred in reactions other than photosynthesis | Cryptosporidium parvum |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.000000064 | - |
NADPH | pH 7.4, 25°C, recombinant enzyme | Cryptosporidium parvum | |
| 0.000000064 | - |
NADPH | pH 8.2, 25°C, recombinant enzyme | Cryptosporidium parvum | |
| 0.0000009 | - |
NADPH | pH 6.8, 25°C, recombinant enzyme | Cryptosporidium parvum | |
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