Literature summary for 2.4.2.7 extracted from

Rehse, P.H.; Tahirov, T.H.
Crystal structure of a purine/pyrimidine phosphoribosyltransferase-related protein from Thermus thermophilus HB8 (2005), Proteins, 61, 658-665.

Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type enzyme in Escherichia coli strain BL21(DE3) and of the selenomethionine-labeled enzyme in Escherichia coli strain B834	Thermus thermophilus

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant native and selenomethionine-labeled enzymes, sitting drop vapour diffusion method, 0.001 ml of 20 mg/ml native protein in 20 mM Tris-HCl, 50 mM NaCl, pH 8.0, is mixed with an equal volume of reservoir solution containing 100 mM MES, pH 5.5, 100 mM calcium acetate, 3% w/v PEG 10000, and 3% v/v MeOH, 1 week, for the selenomethionine-labeled protein 40 mM calcium acetate, 1.5% w/v PEG 10000, and 3% v/v MeOH is used at a protein concentration of 29.4 mg/ml, X-ray diffraction structure determination and analysis at 1.9-2.6 A resolution, multiple wavelength anomalous dispersion method, asymmetric unit of two pairs of identical dimers, each related by noncrystallographic two-fold symmetry, a fifth monomer forms a similar dimer across a crystallographic two-fold axis, modeling	Thermus thermophilus

Crystallization (Comment)

Organism

purified recombinant native and selenomethionine-labeled enzymes, sitting drop vapour diffusion method, 0.001 ml of 20 mg/ml native protein in 20 mM Tris-HCl, 50 mM NaCl, pH 8.0, is mixed with an equal volume of reservoir solution containing 100 mM MES, pH 5.5, 100 mM calcium acetate, 3% w/v PEG 10000, and 3% v/v MeOH, 1 week, for the selenomethionine-labeled protein 40 mM calcium acetate, 1.5% w/v PEG 10000, and 3% v/v MeOH is used at a protein concentration of 29.4 mg/ml, X-ray diffraction structure determination and analysis at 1.9-2.6 A resolution, multiple wavelength anomalous dispersion method, asymmetric unit of two pairs of identical dimers, each related by noncrystallographic two-fold symmetry, a fifth monomer forms a similar dimer across a crystallographic two-fold axis, modeling

Thermus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
5-phospho-alpha-D-ribosyl-1-diphosphate + adenine	Thermus thermophilus	the enzyme is involved in the salvage of adenosine, overview	AMP + diphosphate	-	?
5-phospho-alpha-D-ribosyl-1-diphosphate + adenine	Thermus thermophilus HB8 / ATCC 27634 / DSM 579	the enzyme is involved in the salvage of adenosine, overview	AMP + diphosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus	-	-	-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant wild-type enzyme from Escherichia coli strain BL21(DE3) and recombinant selenomethionine-labeled enzyme from Escherichia coli strain B834 by two steps of anion exchange chromatography, and gel filtration	Thermus thermophilus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
5-phospho-alpha-D-ribosyl-1-diphosphate + adenine	-	Thermus thermophilus	AMP + diphosphate	-	?
5-phospho-alpha-D-ribosyl-1-diphosphate + adenine	the enzyme is involved in the salvage of adenosine, overview	Thermus thermophilus	AMP + diphosphate	-	?
5-phospho-alpha-D-ribosyl-1-diphosphate + adenine	-	Thermus thermophilus HB8 / ATCC 27634 / DSM 579	AMP + diphosphate	-	?
5-phospho-alpha-D-ribosyl-1-diphosphate + adenine	the enzyme is involved in the salvage of adenosine, overview	Thermus thermophilus HB8 / ATCC 27634 / DSM 579	AMP + diphosphate	-	?

Synonyms

Synonyms	Comment	Organism
adenine phosphoribosyltransferase	-	Thermus thermophilus
APRTase	-	Thermus thermophilus