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
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
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
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate deformylase
Q57580
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MJ0116
Q57580
gene name
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
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-
-
?
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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?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
LITERATURE
Fe2+
Q57580
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+
Q57580
enzyme contains both 1.4 mol Fe2+ and 6.2 mol Mg2+ per mol of protomer
Mn2+
Q57580
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+
Q57580
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
LITERATURE
IMAGE
dithiothreitol
Q57580
ArfB is not active in the absence of 2 mM dithiothreitol
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate
Q57580
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
LITERATURE
6
Q57580
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
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8.5
Q57580
pH 6.5: about 80% of maximal activity, pH 8.5: about 40% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
Q57580
2 * 25000
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
Q57580
stable at
696333
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified by anion-exchange chromatography
Q57580
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in Escherichia coli
Q57580