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Literature summary for 4.1.1.71 extracted from

  • Lei, G.; Wang, X.; Lai, C.; Li, Z.M.; Zhang, W.; Xie, C.; Wang, F.; Wu, X.; Li, Z.
    Expression and biochemical characterization of alpha-ketoglutarate decarboxylase from cyanobacterium Synechococcus sp. PCC7002 (2018), Int. J. Biol. Macromol., 114, 188-193 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Synechococcus sp. PCC 7002
expression in Escherichia coli Synechococcus sp. PCC 7002

Inhibitors

Inhibitors Comment Organism Structure
Co2+ 2 mM, 70% residual activity; about 60% residual activity at 2 mM Co2+ Synechococcus sp. PCC 7002
Cu2+ 2 mM, 70% residual activity; about 50% residual activity at 2 mM Co2+ Synechococcus sp. PCC 7002
Zn2+ 2 mM, no residual activity; the activity of the enzyme vanishes at 2 mM Zn2+ Synechococcus sp. PCC 7002

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.19
-
2-oxoglutarate pH 7.0, 25°C Synechococcus sp. PCC 7002
0.19
-
2-oxoglutarate at pH 7.0 and 25°C Synechococcus sp. PCC 7002

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ 2 mM, 1.8fold increase in activity Synechococcus sp. PCC 7002
Ca2+ about 1.8fold increase of activity at 2 mM Synechococcus sp. PCC 7002
Mg2+ 2 mM, 2.3fold increase in activity. Km value 0.059 mM Synechococcus sp. PCC 7002
Mg2+ best stimulant, about 2.3fold increase of activity at 2 mM (used in assay conditions) Synechococcus sp. PCC 7002
Mn2+ 2 mM, 2.2fold increase in activity Synechococcus sp. PCC 7002
Mn2+ about 2.2fold increase of activity at 2 mM Synechococcus sp. PCC 7002

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
247000
-
gel filtration Synechococcus sp. PCC 7002

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-oxoglutarate Synechococcus sp. PCC 7002
-
succinate semialdehyde + CO2
-
?

Organism

Organism UniProt Comment Textmining
Synechococcus sp. PCC 7002
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA resin column chromatography, and Superdex 200 gel filtration Synechococcus sp. PCC 7002

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate
-
Synechococcus sp. PCC 7002 succinate semialdehyde + CO2
-
?
additional information no substrates: pyruvic acid, benzoylformic acid, 2-oxopentanoic acid, 4-methyl-2-oxopentanoic acid and 3-methyl-2-oxobutanoic acid. Enzyme additionally displays low acetolactate synthase activity Synechococcus sp. PCC 7002 ?
-
?
additional information the enzyme has pretty low activity of acetolactate synthase. The enzyme does not catalyze the decarboxylation of any of pyruvic acid, benzoylformic acid, 2-oxopentanoic acid, 4-methyl-2-oxopentanoic acid and 3-methyl-2-oxobutanoic acid to form corresponding aldehyde Synechococcus sp. PCC 7002 ?
-
-

Subunits

Subunits Comment Organism
homotetramer 4 * 60000, SDS-PAGE Synechococcus sp. PCC 7002
tetramer 4 * 60000, SDS-PAGE, * 61667, calcuated from sequence, recombinant protein with His-tag Synechococcus sp. PCC 7002

Synonyms

Synonyms Comment Organism
alpha-ketoglutarate decarboxylase
-
Synechococcus sp. PCC 7002
alpha-KGD
-
Synechococcus sp. PCC 7002

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Synechococcus sp. PCC 7002

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
40 55 the enzyme activity drops by 50% at temperature lower than 40°C, is 70% at 55°C and almost lost at 60°C Synechococcus sp. PCC 7002
40
-
less than 50% of maximum activity below Synechococcus sp. PCC 7002

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2
-
2-oxoglutarate pH 7.0, 25°C Synechococcus sp. PCC 7002
1.2
-
2-oxoglutarate at pH 7.0 and 25°C Synechococcus sp. PCC 7002

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5 7
-
Synechococcus sp. PCC 7002

pH Range

pH Minimum pH Maximum Comment Organism
6
-
34% residual activity Synechococcus sp. PCC 7002
6.5 7 the optimal pH for the enzyme is at the range of 6.5-7.0. The activity of the enzyme is 34% and 17% at pH 6.0 and 8.0, respectively Synechococcus sp. PCC 7002
8
-
17% residual activity Synechococcus sp. PCC 7002

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate required for activity Synechococcus sp. PCC 7002
thiamine diphosphate Km value 0.031 mM Synechococcus sp. PCC 7002

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
6.3
-
2-oxoglutarate pH 7.0, 25°C Synechococcus sp. PCC 7002
6.3
-
2-oxoglutarate at pH 7.0 and 25°C Synechococcus sp. PCC 7002