Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Grochowski, L.L.; Xu, H.; White, R.H.
    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.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.5.1.102 dithiothreitol ArfB is not active in the absence of 2 mM dithiothreitol Methanocaldococcus jannaschii

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.102 in Escherichia coli Methanocaldococcus jannaschii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.102 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

EC Number Metals/Ions Comment Organism Structure
3.5.1.102 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
3.5.1.102 Mg2+ enzyme contains both 1.4 mol Fe2+ and 6.2 mol Mg2+ per mol of protomer Methanocaldococcus jannaschii
3.5.1.102 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
3.5.1.102 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.102 25000
-
 2 * 25000 Methanocaldococcus jannaschii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.102 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

EC Number Organism UniProt Comment Textmining
3.5.1.102 Methanocaldococcus jannaschii Q57580
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.102 purified by anion-exchange chromatography Methanocaldococcus jannaschii

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.5.1.102 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.102 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
-
 ?
3.5.1.102 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

EC Number Subunits Comment Organism
3.5.1.102 dimer 2 * 25000 Methanocaldococcus jannaschii

Synonyms

EC Number Synonyms Comment Organism
3.5.1.102 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate deformylase
-
 Methanocaldococcus jannaschii
3.5.1.102 ArfB
-
 Methanocaldococcus jannaschii
3.5.1.102 MJ0116
-
 Methanocaldococcus jannaschii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.102 70
-
 assay at Methanocaldococcus jannaschii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.1.102 80
-
 stable at Methanocaldococcus jannaschii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.102 7.2
-
 assay at Methanocaldococcus jannaschii

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.5.1.102 6.5 8.5 pH 6.5: about 80% of maximal activity, pH 8.5: about 40% of maximal activity Methanocaldococcus jannaschii