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Literature summary for 2.7.6.1 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
Search for more literature for 2.7.6.1

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
E206A KM-value for ATP is 2.5fold higher than wild-type value Bacillus subtilis
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
M208A KM-value for ATP is 1.2fold higher than wild-type value Bacillus subtilis
N203A KM-value for ATP is 5.6fold higher than wild-type value Bacillus subtilis
P200A KM-value for ATP is 1.5fold lower than wild-type value Bacillus subtilis
P202A KM-value for ATP is 1.5fold higher than wild-type value Bacillus subtilis
R198A KM-value for ATP is nearly identical to wild-type value Bacillus subtilis
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
R201A KM-value for ATP is 2.9fold higher than wild-type value Bacillus subtilis
V204A KM-value for ATP is nearly identical to wild-type value Bacillus subtilis
V207A KM-value for ATP is 1.2fold lower than wild-type value Bacillus subtilis

General Stability

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

Inhibitors

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant Bacillus subtilis

Substrates and Products (Substrate)

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
61
-
 transition temperature of mutant enzyme K197A is 61.2°C Bacillus subtilis
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]

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