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Literature summary extracted from

  • Bibi, T.; Perveen, S.; Aziz, I.; Bashir, Q.; Rashid, N.; Imanaka, T.; Akhtar, M.
    Pcal_1127, a highly stable and efficient ribose-5-phosphate pyrophosphokinase from Pyrobaculum calidifontis (2016), Extremophiles, 20, 821-830.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.6.1 gene Pcal_1127, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli strain BL21-CodonPlus(DE3)-RIL Pyrobaculum calidifontis

General Stability

EC Number General Stability Organism
2.7.6.1 Pcal_1127 is stable against denaturants, the enzyme activity is not affected by the presence of 8 M urea or 4 M guanidinium chloride Pyrobaculum calidifontis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.6.1 EDTA
-
 Pyrobaculum calidifontis
2.7.6.1 additional information the enzyme activity is not affected by the presence of 8 M urea or 4 M guanidinium chloride Pyrobaculum calidifontis
2.7.6.1 phosphate
-
 Pyrobaculum calidifontis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.6.1 0.06
-
 D-ribose 5-phosphate pH 10.5, 55°C, recombinant enzyme Pyrobaculum calidifontis
2.7.6.1 0.08
-
 ATP pH 10.5, 55°C, recombinant enzyme Pyrobaculum calidifontis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.6.1 Ca2+ activates Pyrobaculum calidifontis
2.7.6.1 Cd2+ activates Pyrobaculum calidifontis
2.7.6.1 Co2+ activates Pyrobaculum calidifontis
2.7.6.1 Cu2+ activates Pyrobaculum calidifontis
2.7.6.1 Hg2+ activates Pyrobaculum calidifontis
2.7.6.1 Mg2+ required, highly activating Pyrobaculum calidifontis
2.7.6.1 Mn2+ activates, best stimulating divalent metal ion Pyrobaculum calidifontis
2.7.6.1 Ni2+ activates Pyrobaculum calidifontis
2.7.6.1 Zn2+ activates, highly activating Pyrobaculum calidifontis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.6.1 32000
-
 recombinant enzyme, gel filtration Pyrobaculum calidifontis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.6.1 ATP + D-ribose 5-phosphate Pyrobaculum calidifontis
-
 AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?
2.7.6.1 ATP + D-ribose 5-phosphate Pyrobaculum calidifontis JCM 11548
-
 AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.6.1 Pyrobaculum calidifontis A3MV85 gene Pcal_1127
-
2.7.6.1 Pyrobaculum calidifontis JCM 11548 A3MV85 gene Pcal_1127
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.6.1 recombinant enzyme 4.6fold from Escherichia coli strain BL21-CodonPlus(DE3)-RIL by heat treatment at 80°C for 25 min, anion exchange chromatography, dialysis, and another step of anion exchange chromatography Pyrobaculum calidifontis

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.6.1 cell culture optimal growth temperature of Pyrobaculum calidifontis is between 90°C and 95°C Pyrobaculum calidifontis
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.6.1 480
-
 pH 10.5, 55°C, purified recombinant enzyme Pyrobaculum calidifontis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.6.1 ATP + D-ribose 5-phosphate
-
 Pyrobaculum calidifontis AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?
2.7.6.1 ATP + D-ribose 5-phosphate
-
 Pyrobaculum calidifontis JCM 11548 AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?
2.7.6.1 CTP + D-ribose 5-phosphate
-
 Pyrobaculum calidifontis CMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?
2.7.6.1 CTP + D-ribose 5-phosphate
-
 Pyrobaculum calidifontis JCM 11548 CMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?
2.7.6.1 dATP + D-ribose 5-phosphate
-
 Pyrobaculum calidifontis dAMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?
2.7.6.1 dATP + D-ribose 5-phosphate
-
 Pyrobaculum calidifontis JCM 11548 dAMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?
2.7.6.1 GTP + D-ribose 5-phosphate
-
 Pyrobaculum calidifontis GMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?
2.7.6.1 GTP + D-ribose 5-phosphate
-
 Pyrobaculum calidifontis JCM 11548 GMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?
2.7.6.1 UTP + D-ribose 5-phosphate
-
 Pyrobaculum calidifontis UMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?
2.7.6.1 UTP + D-ribose 5-phosphate
-
 Pyrobaculum calidifontis JCM 11548 UMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.6.1 monomer 1 * 32741, sequence calculation and SDS-PAGE Pyrobaculum calidifontis

Synonyms

EC Number Synonyms Comment Organism
2.7.6.1 Pcal_1127
-
 Pyrobaculum calidifontis
2.7.6.1 ribose-5-phosphate pyrophosphokinase
-
 Pyrobaculum calidifontis
2.7.6.1 RPPK
-
 Pyrobaculum calidifontis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.6.1 55
-
-
 Pyrobaculum calidifontis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.6.1 90 100 Pcal_1127 is thermo-stable, Pcal_1127 exhibits more than 95% residual activity after heating for 4 h at 90°C and a half-life of 15 min in the boiling water Pyrobaculum calidifontis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.6.1 311
-
 D-ribose 5-phosphate pH 10.5, 55°C, recombinant enzyme Pyrobaculum calidifontis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.6.1 10.5
-
-
 Pyrobaculum calidifontis

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.6.1 ATP best cofactor, Pcal_1127 exhibits slightly higher activity with dATP compared to ATP as diphosphate donor Pyrobaculum calidifontis
2.7.6.1 CTP can partially substitute for ATP Pyrobaculum calidifontis
2.7.6.1 dATP best cofactor, Pcal_1127 exhibits slightly higher activity with dATP compared to ATP as diphosphate donor Pyrobaculum calidifontis
2.7.6.1 GTP can partially substitute for ATP Pyrobaculum calidifontis
2.7.6.1 UTP low activity Pyrobaculum calidifontis

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.7.6.1 Pyrobaculum calidifontis sequence calculation
-
 6.97

General Information

EC Number General Information Comment Organism
2.7.6.1 physiological function ribose-5-phosphate diphosphokinase catalyzes the transfer of pyrophosphoryl group from ATP to C1 hydroxyl group of ribose-5-phosphate resulting in the production of AMP and phosphoribosyl diphosphate, the latter plays a central role in several processes of life, including the synthesis of nucleotides, co-enzyme NAD+, and amino acids histidine and tryptophan Pyrobaculum calidifontis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.7.6.1 5183
-
 D-ribose 5-phosphate pH 10.5, 55°C, recombinant enzyme Pyrobaculum calidifontis