Literature summary for 3.2.2.4 extracted from

Zhang, Y.; Cottet, S.E.; Ealick, S.E.
Structure of Escherichia coli AMP nucleosidase reveals similarity to nucleoside phosphorylases (2004), Structure, 12, 1383-1394.

Activating Compound

Activating Compound	Comment	Organism	Structure
ATP	-	Escherichia coli

Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli
overexpression of His6-tagged, selenomethionine-labeled enzyme with an inserted thrombin cleavage site in strain B834(DE3)	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant enzyme bound to formycin 5'-phosphate or phosphate, hanging drop vapour diffusion method, 0.002 ml of 15-20 mg/ml protein in 10 mM Tris-HCl, pH 7.6, 0.15 M NaCl, 2 mM MgCl2, and 1 mM DTT, is mixed with an equal amount of reservoir solution containing 1.8-2.0 M ammonium formate, 0.1 M HEPES, pH 6.8-7.2, 0.2 M NaCl, and 1 mm DTT, 1-2 weeks, X-ray diffraction structure determination and analysis at 2.6-3.0 A resolution	Escherichia coli

Crystallization (Comment)

Organism

purified recombinant enzyme bound to formycin 5'-phosphate or phosphate, hanging drop vapour diffusion method, 0.002 ml of 15-20 mg/ml protein in 10 mM Tris-HCl, pH 7.6, 0.15 M NaCl, 2 mM MgCl2, and 1 mM DTT, is mixed with an equal amount of reservoir solution containing 1.8-2.0 M ammonium formate, 0.1 M HEPES, pH 6.8-7.2, 0.2 M NaCl, and 1 mm DTT, 1-2 weeks, X-ray diffraction structure determination and analysis at 2.6-3.0 A resolution

Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
additional information	hanging drop vapor diffusion method, complexed with formycin 5'-monophosphate or inorganic phosphate	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
formycin 5'-phosphate	conformational changes upon inhibitor binding, overview	Escherichia coli
phosphate	conformational changes upon inhibitor binding, additional phosphate binding site, overview	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
AMP + H2O	Escherichia coli	the enzyme is restricted to prokaryotes and is involved in purine nucleoside salvage and intracellular AMP level regulation, enzyme regulation involving the N-terminal regulatory domain of the subunits	D-ribose 5-phosphate + adenine	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli
recombinant His6-tagged, selenomethionine-labeled enzyme from strain B834(DE3) by nickel affinity chromatography, the His-tag is cleaved off by thrombin	Escherichia coli

Reaction

Reaction	Comment	Organism	Reaction ID
AMP + H2O = D-ribose 5-phosphate + adenine	SN1-type catalytic mechanism with formation of an oxocarbenium-like intermediate followed by nucleophilic attack at the anomeric carbon, overview, substrate binding site structure	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
AMP + H2O	-	Escherichia coli	adenine + D-ribose 5-phosphate	-	?
AMP + H2O	-	Escherichia coli	D-ribose 5-phosphate + adenine	-	?
AMP + H2O	the enzyme is restricted to prokaryotes and is involved in purine nucleoside salvage and intracellular AMP level regulation, enzyme regulation involving the N-terminal regulatory domain of the subunits	Escherichia coli	D-ribose 5-phosphate + adenine	-	?

Subunits

Subunits	Comment	Organism
hexamer	-	Escherichia coli
hexamer	homohexamer, crystal structure, each subunit is composed of one catalytic and one regulatory domain, subunit binding site and structure analysis, intersubunit and interdomain interaction, overview	Escherichia coli

Synonyms

Synonyms	Comment	Organism
AMN	-	Escherichia coli
More	the enzyme belongs to the family of nucleoside phosphorylases	Escherichia coli