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Literature summary for 2.7.1.30 extracted from

  • Molla, G.; Himmelspach, A.; Wohlgemuth, R.; Haupt, E.; Liese, A.
    Mechanistic and kinetics elucidation of Mg2+/ATP molar ratio effect on glycerol kinase (2018), Mol. Catal., 445, 36-42 .
No PubMed abstract available
Search for more literature for 2.7.1.30

Activating Compound

Activating Compound Comment Organism Structure
Polyphosphate addition of inorganic polyphosphate (PPin) inhibits or activates glycerol kinase due to the complexation of PPin with Mg2+ that shifts Mg2+ to ATP molar ratio below or to the optimum level Cellulomonas sp.

Inhibitors

Inhibitors Comment Organism Structure
ADP competitive inhibition versus ATP Cellulomonas sp.
AMP competitive inhibition versus ATP Cellulomonas sp.
Ca2+ inhibition by Ca2+ due to the formation of enzymatically inactive Ca-ATP complexes. The Ca2+ salt of ATP is not an appropriate substrate for glycerol kinase. Ca2+ must be removed by ion exchange pretreatment from enzyme preparations Cellulomonas sp.
Mg2+ essentially required for activity, maximum activity at the optimum Mg2+ to ATP molar ratio of [0.12-0.3]. Subsequent increase of Mg2+ to ATP molar ratio higher than the values in the optimum region suppresses the enzyme activity to a non-zero asymptotic value Cellulomonas sp.
additional information phosphate (Pi) and sn-glycerol-3-phosphate (sn-G3P) do not inhibit glycerol kinase Cellulomonas sp.
Polyphosphate addition of inorganic polyphosphate (PPin) inhibits or activates glycerol kinase due to the complexation of polyphosphate with Mg2+ that shifts Mg2+ to ATP molar ratio below or to the optimum level Cellulomonas sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information the enzyme exhibits two-step kinetics as a function of ATP at a fixed Mg2+ concentration due to the formation of multiple Mg-ATP complexes at different Mg2+ to ATP molar ratio. The active site of glycerol kinase shows different catalytic property with respect to different Mg-ATP complexes. Glycerol kinase exhibits high affinity (low Km) and less activity (low kcat) for complexes with a stoichiometric or over-stoichiometric constitution like Mg2+-ATP. On the other hand, the enzyme shows less affinity (high Km) and high activity (high kcat) for unsaturated complexes like [Mg(ATP)2]6-. Detailed kinetic analysis of glycerol kinase as a function of Mg2+ to ATP molar ratio, overview. The enzyme exhibits Michaelis-Menten kinetics. The two-step kinetic behavior of glycerol kinase as function of ATP at a fixed Mg2+ concentration can rather be explained due to the various Mg-ATP complexes formed at different Mg2+/ATP molar ratios that bind to the active site. In consequence, different Km and kcat values are determined with respect to the different Mg-ATP complexes Cellulomonas sp.
0.012
-
 glycerol pH 8.5, 30°C Cellulomonas sp.
0.09
-
 ATP ATP at 21 mM Mg2+, pH 8.5, 30°C Cellulomonas sp.
0.12
-
 ATP ATP at 10.5 mM Mg2+, pH 8.5, 30°C Cellulomonas sp.
0.28
-
 ATP ATP at 1.5 mM Mg2+, pH 8.5, 30°C Cellulomonas sp.
1.7
-
 ATP ATP at 10.5 mM Mg2+, pH 8.5, 30°C Cellulomonas sp.
1.7
-
 ATP ATP at 21 mM Mg2+, pH 8.5, 30°C Cellulomonas sp.
2.061
-
 ATP Mg2+/ATP molar ratio constant at 0.3, pH 8.5, 30°C Cellulomonas sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ essentially required for activity, maximum activity at the optimum Mg2+ to ATP molar ratio of [0.12-0.3]. Subsequent increase of Mg2+ to ATP molar ratio higher than the values in the optimum region suppresses the enzyme activity to a non-zero asymptotic value. The enzyme exhibits two-step kinetics as a function of ATP at a fixed Mg2+ concentration due to the formation of multiple Mg-ATP complexes at different Mg2+ to ATP molar ratio. The interaction of Mg2+ and ATP generates Mg-ATP complexes of various physical and chemical features in which the product composition depends on Mg2+ to ATP molar ratio among other factors such as pH, temperature, availability of other polyvalent chelating anions as well as cations and their concentration Cellulomonas sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + glycerol Cellulomonas sp.
-
 ADP + sn-glycerol 3-phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Cellulomonas sp.
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Cellulomonas sp.
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + glycerol
-
 Cellulomonas sp. ADP + sn-glycerol 3-phosphate
-
 ?
additional information the enzyme exhibits two-step kinetics as a function of ATP at a fixed Mg2+ concentration due to the formation of multiple Mg-ATP complexes at different Mg2+ to ATP molar ratio. The interaction of Mg2+ and ATP generates Mg-ATP complexes of various physical and chemical features in which the product composition depends on Mg2+ to ATP molar ratio among other factors such as pH, temperature, availability of other polyvalent chelating anions, as well as cations and their concentration. The Ca2+ salt of ATP is not an appropriate substrate for glycerol kinase Cellulomonas sp. ?
-
-

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Cellulomonas sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
 assay at Cellulomonas sp.

General Information

General Information Comment Organism
additional information detailed kinetic analysis of glycerol kinase as a function of Mg2+ to ATP molar ratio, and multinuclear NMR study of the Mg-ATP complex formation is described in order to elucidate the effect of Mg2+ in modifying the physical and chemical features of ATP, and mechanistic elucidation of the effect of Mg-ATP interaction on the catalytic properties of glycerol kinase, overview Cellulomonas sp.