Information on EC 3.5.1.102 - 2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase

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The expected taxonomic range for this enzyme is: Methanocaldococcus jannaschii

EC NUMBER
COMMENTARY hide
3.5.1.102
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RECOMMENDED NAME
GeneOntology No.
2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O = 2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + formate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
flavin biosynthesis
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flavin biosynthesis II (archaea)
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Metabolic pathways
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Riboflavin metabolism
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SYSTEMATIC NAME
IUBMB Comments
2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one amidohydrolase
The enzyme catalyses the second step in archaeal riboflavin and 7,8-didemethyl-8-hydroxy-5-deazariboflavin biosynthesis. The first step is catalysed by EC 3.5.4.29 (GTP cyclohydrolase IIa). The bacterial enzyme, EC 3.5.4.25 (GTP cyclohydrolase II) catalyses both reactions.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-amino-5-formylamino-6-(D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + H2O
2,5-diamino-6-(D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + formate
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-amino-5-formylamino-6-(D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + H2O
2,5-diamino-6-(D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + formate
show the reaction diagram
Q57580
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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
Mg2+
enzyme contains both 1.4 mol Fe2+ and 6.2 mol Mg2+ per mol of protomer
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
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
ArfB is not active in the absence of 2 mM dithiothreitol
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
Vmax at a concentration of 2 mM Fe2+, 5 mM MgCl2, 10 mM dithiothreitol and 25 mM TES, pH 7.2
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
pH 6.5: about 80% of maximal activity, pH 8.5: about 40% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified by anion-exchange chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE