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Literature summary extracted from

  • Hove-Jensen, B.; Bentsen, A.K.; Harlow, K.W.
    Catalytic residues Lys197 and Arg199 of Bacillus subtilis phosphoribosyl diphosphate synthase. Alanine-scanning mutagenesis of the flexible catalytic loop (2005), FEBS J., 272, 3631-3639.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.6.1 produced in an Escherichia coli strain lacking endogenous phosphoribosyl diphosphate synthase activity Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
2.7.6.1 E206A KM-value for ATP is 2.5fold higher than wild-type value Bacillus subtilis
2.7.6.1 K197A maximal velocity is reduced more than 30000fold compared to wild-type enzyme. The KM-values for ATP and ribose 5-phosphate are unchanged Bacillus subtilis
2.7.6.1 M208A KM-value for ATP is 1.2fold higher than wild-type value Bacillus subtilis
2.7.6.1 N203A KM-value for ATP is 5.6fold higher than wild-type value Bacillus subtilis
2.7.6.1 P200A KM-value for ATP is 1.5fold lower than wild-type value Bacillus subtilis
2.7.6.1 P202A KM-value for ATP is 1.5fold higher than wild-type value Bacillus subtilis
2.7.6.1 R198A KM-value for ATP is nearly identical to wild-type value Bacillus subtilis
2.7.6.1 R199A maximal velocity is reduced more than 24000fold compared to wild-type enzyme. The KM-values for ATP and ribose 5-phosphate are unchanged Bacillus subtilis
2.7.6.1 R201A KM-value for ATP is 2.9fold higher than wild-type value Bacillus subtilis
2.7.6.1 V204A KM-value for ATP is nearly identical to wild-type value Bacillus subtilis
2.7.6.1 V207A KM-value for ATP is 1.2fold lower than wild-type value Bacillus subtilis

General Stability

EC Number General Stability Organism
2.7.6.1 Lys197 and Arg199 are important in stabilization of the transition state Bacillus subtilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.6.1 5-phospho-alpha-D-ribose 1-diphosphate competitive with respect to ATP and noncompetitive with respect to D-ribose 5-phosphate Bacillus subtilis
2.7.6.1 AMP noncompetitive with respect to D-ribose 5-phosphate and competitive with respect to ATP Bacillus subtilis
2.7.6.1 ATP
-
 Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.6.1 0.057
-
 ATP mutant enzyme K199A Bacillus subtilis
2.7.6.1 0.107
-
 D-ribose 5-phosphate mutant enzyme K199A Bacillus subtilis
2.7.6.1 0.12
-
 ATP mutant enzyme K197A Bacillus subtilis
2.7.6.1 0.13
-
 ATP mutant enzyme P200A Bacillus subtilis
2.7.6.1 0.16
-
 ATP mutant enzyme V207A Bacillus subtilis
2.7.6.1 0.19
-
 ATP mutant enzyme R198A Bacillus subtilis
2.7.6.1 0.19
-
 ATP mutant enzyme V204A Bacillus subtilis
2.7.6.1 0.191
-
 ATP wild-type enzyme Bacillus subtilis
2.7.6.1 0.217
-
 D-ribose 5-phosphate mutant enzyme K197A Bacillus subtilis
2.7.6.1 0.23
-
 D-ribose 5-phosphate wild-type enzyme Bacillus subtilis
2.7.6.1 0.23
-
 ATP mutant enzyme M208A Bacillus subtilis
2.7.6.1 0.29
-
 ATP mutant enzyme P202A Bacillus subtilis
2.7.6.1 0.48
-
 ATP mutant enzyme E206A Bacillus subtilis
2.7.6.1 0.56
-
 ATP mutant enzyme R201A Bacillus subtilis
2.7.6.1 0.87
-
 ATP mutant enzyme N203A Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
2.7.6.1 Bacillus subtilis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.6.1 recombinant Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.6.1 ATP + D-ribose 5-phosphate
-
 Bacillus subtilis AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.6.1 61
-
 transition temperature of mutant enzyme K197A is 61.2°C Bacillus subtilis
2.7.6.1 63
-
 transition temperature of wild-type enzyme is 62.8°C, transition temperature of mutant enzyme R199A is 62.6°C Bacillus subtilis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.6.1 additional information
-
 additional information
-
 Bacillus subtilis
2.7.6.1 0.167
-
 ATP mutant enzyme K197A Bacillus subtilis
2.7.6.1 0.323
-
 ATP mutant enzyme K199A Bacillus subtilis
2.7.6.1 1.089
-
 ATP wild-type enzyme Bacillus subtilis