Any feedback?
Literature summary for 3.5.1.102 extracted from
- An iron(II) dependent formamide hydrolase catalyzes the second step in the archaeal biosynthetic pathway to riboflavin and 7,8-didemethyl-8-hydroxy-5-deazariboflavin (2009), Biochemistry, 48, 4181-4188.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| dithiothreitol | ArfB is not active in the absence of 2 mM dithiothreitol | Methanocaldococcus jannaschii |  |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| in Escherichia coli | Methanocaldococcus jannaschii |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1 | - |
2-amino-5-formylamino-6-(D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate | pH 7.2, 70°C, apparent Km-value is about 1 mM at a concentration of 2 mM Fe2+, type of curve is typically indicative of homomeric cooperativity and suggests that ArfB may exhibit positive cooperative substrate binding | Methanocaldococcus jannaschii | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | addition of more than 1 mM Fe2+ increases the rate of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate production by more than 10fold, purified enzyme contains both 1.4 mol iron and 6.2 mol magnesium per mol of protomer, maximum activity of Chelex-treated enzyme with added Fe2+ is 30% that of the untreated enzyme indicating that the apoenzyme cannot be fully reconstituted with the addition of just one metal | Methanocaldococcus jannaschii | |
| Mg2+ | enzyme contains both 1.4 mol Fe2+ and 6.2 mol Mg2+ per mol of protomer | Methanocaldococcus jannaschii | |
| Mn2+ | addition of more than 1 mM Mn2+ increases the rate of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate production by more than 10fold, maximum activity of Chelex-treated enzyme with added Mn2+ is 30% that of the untreated enzyme indicating that the apoenzyme cannot be fully reconstituted with the addition of just one metal | Methanocaldococcus jannaschii | |
| Zn2+ | zinc is associated with the purified protein, 1.5 mol/protomer, despite the presence of zinc in the protein, addition of Zn(II) to the incubation mixture containing purified enzyme or apo-enzyme does not activate ArfB | Methanocaldococcus jannaschii | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 25000 | - |
2 * 25000 | Methanocaldococcus jannaschii |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2-amino-5-formylamino-6-(D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + H2O | Methanocaldococcus jannaschii | enzyme catalyzes the second step in archaeal riboflavin and 7,8-didemethyl-8-hydroxy-5-deazariboflavin biosynthesis. The archaeal pathway begins with an archaeal-specific GTP cyclohydrolase IIa (EC 3.5.4.29) that hydrolyzes the imidazole ring of GTP. The bacterial enzyme, EC 3.5.4.25 (GTP cyclohydrolase II) catalyzes both reactions | 2,5-diamino-6-(D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + formate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanocaldococcus jannaschii | Q57580 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| purified by anion-exchange chromatography | Methanocaldococcus jannaschii |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 6 | - |
Vmax at a concentration of 2 mM Fe2+, 5 mM MgCl2, 10 mM dithiothreitol and 25 mM TES, pH 7.2 | Methanocaldococcus jannaschii |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2-amino-5-formylamino-6-(D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + H2O | - |
Methanocaldococcus jannaschii | 2,5-diamino-6-(D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + formate | - |
? | |
| 2-amino-5-formylamino-6-(D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + H2O | enzyme catalyzes the second step in archaeal riboflavin and 7,8-didemethyl-8-hydroxy-5-deazariboflavin biosynthesis. The archaeal pathway begins with an archaeal-specific GTP cyclohydrolase IIa (EC 3.5.4.29) that hydrolyzes the imidazole ring of GTP. The bacterial enzyme, EC 3.5.4.25 (GTP cyclohydrolase II) catalyzes both reactions | Methanocaldococcus jannaschii | 2,5-diamino-6-(D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + formate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 25000 | Methanocaldococcus jannaschii |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate deformylase | - |
Methanocaldococcus jannaschii |
| ArfB | - |
Methanocaldococcus jannaschii |
| MJ0116 | - |
Methanocaldococcus jannaschii |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
assay at | Methanocaldococcus jannaschii |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 80 | - |
stable at | Methanocaldococcus jannaschii |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
assay at | Methanocaldococcus jannaschii |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | 8.5 | pH 6.5: about 80% of maximal activity, pH 8.5: about 40% of maximal activity | Methanocaldococcus jannaschii |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
