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Literature summary extracted from

  • Kita, A.; Kishimoto, A.; Shimosaka, T.; Tomita, H.; Yokooji, Y.; Imanaka, T.; Atomi, H.; Miki, K.
    Crystal structure of pantoate kinase from Thermococcus kodakarensis (2020), Proteins, 88, 718-724 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.169 purified recombinant enzyme in apoform or in complex with ATP and a magnesium ion, mixing of 5-10 mg/ml protein in 50 mM Tris-HCl, pH 7.5, with 18%-20% PEG 8000 solutions containing 200 mM calcium acetate and 100 mM MES, pH 6.0, as a precipitant, 1-2 weeks, 20°C, X-ray diffraction structure determination and analysis at 2.5-2.7 A resolution, single isomorphous replacement (SIR) method using derivative data of K2Pt (NO2)4 collected at 3.0 A resolution, modeling. In TkPoK/ATP, the adenine ring of the ATP is not included in the crystal structure, because its electron density is very poor Thermococcus kodakarensis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.169 Mg2+ required Thermococcus kodakarensis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.169 ATP + (R)-pantoate Thermococcus kodakarensis
-
ADP + (R)-4-phosphopantoate
-
?
2.7.1.169 ATP + (R)-pantoate Thermococcus kodakarensis JCM 12380
-
ADP + (R)-4-phosphopantoate
-
?
2.7.1.169 ATP + (R)-pantoate Thermococcus kodakarensis ATCC BAA-918
-
ADP + (R)-4-phosphopantoate
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.169 Thermococcus kodakarensis Q5JHF1 Pyrococcus kodakaraensis strain KOD1
-
2.7.1.169 Thermococcus kodakarensis ATCC BAA-918 Q5JHF1 Pyrococcus kodakaraensis strain KOD1
-
2.7.1.169 Thermococcus kodakarensis JCM 12380 Q5JHF1 Pyrococcus kodakaraensis strain KOD1
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.169 ATP + (R)-pantoate
-
Thermococcus kodakarensis ADP + (R)-4-phosphopantoate
-
?
2.7.1.169 ATP + (R)-pantoate
-
Thermococcus kodakarensis JCM 12380 ADP + (R)-4-phosphopantoate
-
?
2.7.1.169 ATP + (R)-pantoate
-
Thermococcus kodakarensis ATCC BAA-918 ADP + (R)-4-phosphopantoate
-
?
2.7.1.169 additional information the enzyme shows broad nucleotide specificity Thermococcus kodakarensis ?
-
-
2.7.1.169 additional information the enzyme shows broad nucleotide specificity Thermococcus kodakarensis JCM 12380 ?
-
-
2.7.1.169 additional information the enzyme shows broad nucleotide specificity Thermococcus kodakarensis ATCC BAA-918 ?
-
-

Subunits

EC Number Subunits Comment Organism
2.7.1.169 dimer 2 * 33000, about, sequence calculation and crystal structure analysis Thermococcus kodakarensis

Synonyms

EC Number Synonyms Comment Organism
2.7.1.169 PoK
-
Thermococcus kodakarensis
2.7.1.169 TK2141
-
Thermococcus kodakarensis
2.7.1.169 TkPoK
-
Thermococcus kodakarensis

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.169 ATP the electron density for the adenosine moiety of ATP is very weak, which most likely relates to its broad nucleotide specificity. The triphosphate moiety of ATP is surrounded by the lycine-rich loop of motif II (P96NGYGFGNSAG106). The magnesium ion can interact with oxygen atoms of beta- and gamma-phosphates, and with the O5' atom of ATP which bridges the adenosine and the triphosphate groups Thermococcus kodakarensis

General Information

EC Number General Information Comment Organism
2.7.1.169 metabolism the CoA biosynthesis pathway involves reactions that convert pantoate to 4'-phosphopantothenate. For this conversion, bacteria/eukaryotes commonly use two enzymes, pantothenate synthetase (PS) and pantothenate kinase (PanK). In the PS/PanK pathway, pantoate and beta-alanine are first condensed to form pantothenate by the reaction of PS, and then pantothenate is phosphorylated to generate 40-phosphopantothenate by the reaction of PanK Thermococcus kodakarensis