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Literature summary for 2.4.2.7 extracted from

  • Harris, L.D.; Harijan, R.K.; Ducati, R.G.; Evans, G.B.; Hirsch, B.M.; Schramm, V.L.
    Synthesis of bis-phosphate iminoaltritol enantiomers and structural characterization with adenine phosphoribosyltransferase (2018), ACS Chem. Biol., 13, 152-160 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.2.7

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of N-terminally His6-tagged enzyme Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment) Organism
purified His-tagged recombinant enzyme in complex with inhibitors D-DIAB and L-DIAB, and also with adenine, X-ray diffraction structure determination and analysis of enzyme-inhibitor complexes at 1.78 A and 1.98 A resolution, respectively, modeling, structure comparisons Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
E106L site-directed mutagenesis, the mutant shows highly reduced kcat compared to wild-type Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
D-2,5-dideoxy-2,5-imino-altritol 1,6-bisphosphate D-DIAB, a iminoaltritol bis-phosphate, transition-state analogue inhibitor, enzyme interactions and binding structure analysis Saccharomyces cerevisiae
L-2,5-dideoxy-2,5-imino-altritol 1,6-bisphosphate L-DIAB, a iminoaltritol bis-phosphate, enzyme binding structure analysis Saccharomyces cerevisiae
additional information an enantiomeric pair of iminoaltritol bis-phosphates (L-DIAB and D-DIAB) is synthesized and shown to display inhibition of Saccharomyces cerevisiae adenine phosphoribosyltransferase (ScAPRT). Synthesis pathway, detailed overview. Crystallographic inhibitor binding analysis of L- and D-DIAB bound to the catalytic sites of ScAPRT demonstrates accommodation of both enantiomers by altered ring geometry and bis-phosphate catalytic site contacts Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
AMP + diphosphate Saccharomyces cerevisiae
-
 adenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?
AMP + diphosphate Saccharomyces cerevisiae ATCC 204508
-
 adenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P49435
-
-
Saccharomyces cerevisiae ATCC 204508 P49435
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally His6-tagged enzyme by nickel affinity chromatography Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,6-diaminopurine 5-phosphoribosyl nucleotide + diphosphate
-
 Saccharomyces cerevisiae 2,6-diaminopurine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?
2,6-diaminopurine 5-phosphoribosyl nucleotide + diphosphate
-
 Saccharomyces cerevisiae ATCC 204508 2,6-diaminopurine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?
AMP + diphosphate
-
 Saccharomyces cerevisiae adenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?
AMP + diphosphate adenine binds to only one of the two subunits, leaving the adjacent adenine-free binding pockets occupied by a symmetry-related Tyr107 side chain, suggesting subunit-sequential catalytic site activity Saccharomyces cerevisiae adenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?
AMP + diphosphate
-
 Saccharomyces cerevisiae ATCC 204508 adenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?
AMP + diphosphate adenine binds to only one of the two subunits, leaving the adjacent adenine-free binding pockets occupied by a symmetry-related Tyr107 side chain, suggesting subunit-sequential catalytic site activity Saccharomyces cerevisiae ATCC 204508 adenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?

Synonyms

Synonyms Comment Organism
APRT1
-
 Saccharomyces cerevisiae
ScAPRT
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Saccharomyces cerevisiae

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0087
-
 D-2,5-dideoxy-2,5-imino-altritol 1,6-bisphosphate pH 7.5, 25°C, recombinant enzyme Saccharomyces cerevisiae
0.0149
-
 L-2,5-dideoxy-2,5-imino-altritol 1,6-bisphosphate pH 7.5, 25°C, recombinant enzyme Saccharomyces cerevisiae