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Literature summary for 2.7.1.165 extracted from

  • Kouril, T.; Wieloch, P.; Reimann, J.; Wagner, M.; Zaparty, M.; Albers, S.V.; Schomburg, D.; Ruoff, P.; Siebers, B.
    Unraveling the function of the two Entner-Doudoroff branches in the thermoacidophilic crenarchaeon Sulfolobus solfataricus P2 (2013), FEBS J., 280, 1126-1138.
    View publication on PubMed
Search for more literature for 2.7.1.165

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3)-RIL cells Saccharolobus solfataricus
expression in Escherichia coli Saccharolobus solfataricus

Inhibitors

Inhibitors Comment Organism Structure
ATP weak substrate inhibition Saccharolobus solfataricus
D-glycerate substrate inhibition; substrate inhibition at glycerate concentrations higher than 2 mM at 80°C, above 2 mM at 70°C and 5 mM at 65°C Saccharolobus solfataricus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ dependent on Saccharolobus solfataricus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
44400
-
 2 * 44400, calculated from amino acid sequence Saccharolobus solfataricus
44400
-
 2 * 44400, calculated from sequence Saccharolobus solfataricus
49000
-
 2 * 49000, SDS-PAGE Saccharolobus solfataricus
90000
-
 gel filtration Saccharolobus solfataricus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + D-glycerate Saccharolobus solfataricus a key enzyme in the nonphosphorylative Entner-Doudoroff pathway in archaea. The glycerate kinase, with its unusual regulatory properties, seems to play a major role in controlling the flux between the glycolytic nonphosphorylative Entner-Doudoroff and the glycolytic/gluconeogenetic semiphosphorylative Entner-Doudoroff pathway ADP + 2-phospho-D-glycerate
-
 ?
ATP + D-glycerate Saccharolobus solfataricus P2 a key enzyme in the nonphosphorylative Entner-Doudoroff pathway in archaea. The glycerate kinase, with its unusual regulatory properties, seems to play a major role in controlling the flux between the glycolytic nonphosphorylative Entner-Doudoroff and the glycolytic/gluconeogenetic semiphosphorylative Entner-Doudoroff pathway ADP + 2-phospho-D-glycerate
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus Q7LXP1
-
-
Saccharolobus solfataricus P2 Q7LXP1
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharolobus solfataricus
UNO Q-12 column chromatography and Superdex 200 gel filtration Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + D-glycerate specific substrate Saccharolobus solfataricus ADP + 2-phospho-D-glycerate
-
 ?
ATP + D-glycerate a key enzyme in the nonphosphorylative Entner-Doudoroff pathway in archaea. The glycerate kinase, with its unusual regulatory properties, seems to play a major role in controlling the flux between the glycolytic nonphosphorylative Entner-Doudoroff and the glycolytic/gluconeogenetic semiphosphorylative Entner-Doudoroff pathway Saccharolobus solfataricus ADP + 2-phospho-D-glycerate
-
 ?
ATP + D-glycerate the enzyme is specific for D-glycerate. The enzyme shows cooperativity by D-glycerate and ATP. A good fit achieved from the kinetic model to the experimental data suggests a mechanism where two glycerate molecules bind to glycerate kinase and are converted to product, while a third binding site appears to be inhibitory. The model suggests that the inhibition appears to be due to the formation of an additional complex with very low activity at 80°C Saccharolobus solfataricus ADP + 2-phospho-D-glycerate
-
 ?
ATP + D-glycerate specific substrate Saccharolobus solfataricus P2 ADP + 2-phospho-D-glycerate
-
 ?
ATP + D-glycerate a key enzyme in the nonphosphorylative Entner-Doudoroff pathway in archaea. The glycerate kinase, with its unusual regulatory properties, seems to play a major role in controlling the flux between the glycolytic nonphosphorylative Entner-Doudoroff and the glycolytic/gluconeogenetic semiphosphorylative Entner-Doudoroff pathway Saccharolobus solfataricus P2 ADP + 2-phospho-D-glycerate
-
 ?
ATP + D-glycerate the enzyme is specific for D-glycerate. The enzyme shows cooperativity by D-glycerate and ATP. A good fit achieved from the kinetic model to the experimental data suggests a mechanism where two glycerate molecules bind to glycerate kinase and are converted to product, while a third binding site appears to be inhibitory. The model suggests that the inhibition appears to be due to the formation of an additional complex with very low activity at 80°C Saccharolobus solfataricus P2 ADP + 2-phospho-D-glycerate
-
 ?

Subunits

Subunits Comment Organism
homodimer 2 * 49000, SDS-PAGE Saccharolobus solfataricus
homodimer 2 * 44400, calculated from amino acid sequence Saccharolobus solfataricus
homodimer 2 * 44400, calculated from sequence Saccharolobus solfataricus

Synonyms

Synonyms Comment Organism
class II glycerate kinase
-
 Saccharolobus solfataricus
glycerate kinase
-
 Saccharolobus solfataricus
Sso-GK
-
 Saccharolobus solfataricus
SSO0666
-
 Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
80
-
-
 Saccharolobus solfataricus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
24.5
-
 D-glycerate in 100 mM HEPES/KOH, pH 7.0, at 37°C Saccharolobus solfataricus
24.5
-
 D-glycerate pH 6.5, 80°C, Hill equation Saccharolobus solfataricus
28.8
-
 ATP in 100 mM HEPES/KOH, pH 7.0, at 37°C Saccharolobus solfataricus
28.8
-
 ATP pH 6.5, 80°C, Michaelis–Menten equation Saccharolobus solfataricus
35.1
-
 ATP pH 6.5, 80°C, substrate-inhibition model Saccharolobus solfataricus
533.3
-
 D-glycerate pH 6.5, 80°C, kinetic model Saccharolobus solfataricus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.1
-
 D-glycerate in 100 mM HEPES/KOH, pH 7.0, at 37°C Saccharolobus solfataricus
0.1
-
 D-glycerate pH 6.5, 80°C Saccharolobus solfataricus
61
-
 ATP in 100 mM HEPES/KOH, pH 7.0, at 37°C Saccharolobus solfataricus
61
-
 ATP pH 6.5, 80°C Saccharolobus solfataricus

General Information

General Information Comment Organism
metabolism the enzyme plays a major role in controlling the flux between the glycolytic non-phosphorylative-Entner-Doudoroff and the glycolytic/gluconeogenetic semiphosphorylative Entner-Doudoroff pathway Saccharolobus solfataricus