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

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For detailed information about 2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase, go to the full flat file.

Reaction

Synonyms

2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate deformylase, ArfB, MJ0116

ECTree

     3 Hydrolases

         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds

             3.5.1 In linear amides

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

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Results	in table
1	Activating Compound
143	AA Sequence
1	Cloned(Commentary)
1	KM Value [mM]
4	Metals/Ions
1	Molecular Weight [Da]
1	Natural Substrates/ Products (Substrates)
1	Organism
5	Pathway
1	pH Optimum
1	pH Range
1	Purification (Commentary)
1	Reaction
1	Reaction Type
1	Reference
1	Specific Activity [micromol/min/mg]
2	Substrates and Products (Substrate)
1	Subunits
3	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
1	Temperature Stability [°C]

Metals Ions

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

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Fe2+

Methanocaldococcus jannaschii

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

696333

Mg2+

Methanocaldococcus jannaschii

Q57580

enzyme contains both 1.4 mol Fe2+ and 6.2 mol Mg2+ per mol of protomer

696333

Mn2+

Methanocaldococcus jannaschii

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

696333

Zn2+

Methanocaldococcus jannaschii

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

696333