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Literature summary extracted from

  • Mukhopadhyay, B.; Concar, E.M.; Wolfe, R.S.
    A GTP-dependent vertebrate-type phosphoenolpyruvate carboxykinase from Mycobacterium smegmatis (2001), J. Biol. Chem., 276, 16137-16145.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.1.1.32 2-mercaptoethanol maximum stimulation at 75 mM Mycolicibacterium smegmatis
4.1.1.32 dithiothreitol maximum at 10-40 mM, 30% stimulation Mycolicibacterium smegmatis
4.1.1.32 reduced glutathione maximum stimulation at 20 mM Mycolicibacterium smegmatis
4.1.1.32 thiol-containing reducing agent activates Mycolicibacterium smegmatis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.32 pck gene, overexpression in Escherichia coli C41(DE3), sequencing Mycolicibacterium smegmatis

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.32 alpha-ketoglutarate inhibits oxaloacetate formation, mixed-type inhibition Mycolicibacterium smegmatis
4.1.1.32 KCl 0.5 M, 50% inhibition Mycolicibacterium smegmatis
4.1.1.32 Na2SO4
-
Mycolicibacterium smegmatis
4.1.1.32 NaCl 0.5 M, 50% inhibition Mycolicibacterium smegmatis
4.1.1.32 oxalate potent inhibitor of oxaloacetate formation, mixed-type inhibition Mycolicibacterium smegmatis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.32 additional information
-
additional information Km-values for several divalent cations, the presence of 2 mM Mg2+ greatly lowers the Km-values for Mn2+, 144fold in the presence of dithiothreitol and 9.4fold in the absence of dithiothreitol, and for Co2+ by 230fold, influence of divalent cations on the Km-value for phosphoenolpyruvate Mycolicibacterium smegmatis
4.1.1.32 0.012
-
oxaloacetate pH 7.2, 37°C Mycolicibacterium smegmatis
4.1.1.32 0.013
-
GTP pH 7.2, 37°C Mycolicibacterium smegmatis
4.1.1.32 0.066
-
GDP pH 7.2, 37°C Mycolicibacterium smegmatis
4.1.1.32 0.1
-
phosphoenolpyruvate pH 7.2, 37°C Mycolicibacterium smegmatis
4.1.1.32 0.29
-
IDP pH 7.2, 37°C Mycolicibacterium smegmatis
4.1.1.32 8.3
-
CO2 pH 7.2, 37°C, bicarbonate Mycolicibacterium smegmatis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.1.1.32 soluble recombinant enzyme Mycolicibacterium smegmatis
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.32 Co2+ requirement for a divalent cation, best fulfilled by Mn2+ and Co2+, kinetics, acts as phosphoenolpyruvate activator Mycolicibacterium smegmatis
4.1.1.32 Mg2+ requirement for a divalent cation, poor activator, kinetics, Mg2+ is superior in complexing the nucleotide substrate compared with Mn2+ or Co2+ Mycolicibacterium smegmatis
4.1.1.32 Mn2+ requirement for a divalent cation, best fulfilled by Mn2+ and Co2+, kinetics, acts as phosphoenolpyruvate activator Mycolicibacterium smegmatis
4.1.1.32 additional information not activated by Ca2+, Zn2+, Cu2+ or Ni2+ Mycolicibacterium smegmatis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.32 71200
-
1 * 72000-74000, SDS-PAGE, 1 * 71200, mass spectrometry Mycolicibacterium smegmatis
4.1.1.32 83200
-
gel filtration Mycolicibacterium smegmatis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.32 GTP + oxaloacetate Mycolicibacterium smegmatis catalyzes the first committed step in gluconeogenesis, in vivo enzyme prefers the gluconeogenesis/glycerogenesis direction, i.e phosphoenolpyruvate formation, GDP is the more physiologically relevant nucleotide substrate than IDP GDP + phosphoenolpyruvate + CO2
-
r
4.1.1.32 GTP + oxaloacetate Mycolicibacterium smegmatis mc(2)155 catalyzes the first committed step in gluconeogenesis, in vivo enzyme prefers the gluconeogenesis/glycerogenesis direction, i.e phosphoenolpyruvate formation, GDP is the more physiologically relevant nucleotide substrate than IDP GDP + phosphoenolpyruvate + CO2
-
r

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.32 Mycolicibacterium smegmatis Q9AGJ6
-
-
4.1.1.32 Mycolicibacterium smegmatis mc(2)155 Q9AGJ6
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.32 recombinant enzyme Mycolicibacterium smegmatis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.1.32 additional information
-
-
Mycolicibacterium smegmatis

Storage Stability

EC Number Storage Stability Organism
4.1.1.32 4°C, purified recombinant enzyme, 100 mM sodium phosphate buffer, pH 7, 100 mM NaCl, 1 month, 24% loss of activity Mycolicibacterium smegmatis
4.1.1.32 4°C, purified recombinant His-tagged enzyme, 100 mM sodium phosphate buffer, pH 7, 100 mM NaCl, 2 months, 25% loss of activity Mycolicibacterium smegmatis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.32 GTP + oxaloacetate GTP-dependent, enzyme prefers the phosphoenolpyruvate synthesis direction Mycolicibacterium smegmatis GDP + phosphoenolpyruvate + CO2
-
r
4.1.1.32 GTP + oxaloacetate catalyzes the first committed step in gluconeogenesis, in vivo enzyme prefers the gluconeogenesis/glycerogenesis direction, i.e phosphoenolpyruvate formation, GDP is the more physiologically relevant nucleotide substrate than IDP Mycolicibacterium smegmatis GDP + phosphoenolpyruvate + CO2
-
r
4.1.1.32 GTP + oxaloacetate GTP-dependent, enzyme prefers the phosphoenolpyruvate synthesis direction Mycolicibacterium smegmatis mc(2)155 GDP + phosphoenolpyruvate + CO2
-
r
4.1.1.32 GTP + oxaloacetate catalyzes the first committed step in gluconeogenesis, in vivo enzyme prefers the gluconeogenesis/glycerogenesis direction, i.e phosphoenolpyruvate formation, GDP is the more physiologically relevant nucleotide substrate than IDP Mycolicibacterium smegmatis mc(2)155 GDP + phosphoenolpyruvate + CO2
-
r
4.1.1.32 ITP + oxaloacetate
-
Mycolicibacterium smegmatis IDP + phosphoenolpyruvate + CO2
-
r
4.1.1.32 ITP + oxaloacetate
-
Mycolicibacterium smegmatis mc(2)155 IDP + phosphoenolpyruvate + CO2
-
r
4.1.1.32 additional information ADP is a very poor substrate in the reverse reaction Mycolicibacterium smegmatis ?
-
?
4.1.1.32 additional information ADP is a very poor substrate in the reverse reaction Mycolicibacterium smegmatis mc(2)155 ?
-
?

Subunits

EC Number Subunits Comment Organism
4.1.1.32 monomer 1 * 72000-74000, SDS-PAGE, 1 * 71200, mass spectrometry Mycolicibacterium smegmatis

Synonyms

EC Number Synonyms Comment Organism
4.1.1.32 GTP/ITP:oxaloacetate carboxylyase (transphosphorylating)
-
Mycolicibacterium smegmatis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.32 70
-
at pH 7.2 Mycolicibacterium smegmatis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.32 7 7.4 at 37°C Mycolicibacterium smegmatis