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Literature summary for 1.1.1.41 extracted from

  • Wang, P.; Song, P.; Jin, M.; Zhu, G.
    Isocitrate dehydrogenase from Streptococcus mutans: biochemical properties and evaluation of a putative phosphorylation site at Ser102 (2013), PLoS ONE, 8, e58918.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene idh, expression of wild-type and mutant enzymes in Escherichia coli glutamate auxotrophic strain Dicd::kanr fused to gene icd, the endogenous icd gene is replaced by the kanamycin resistance gene, the wild-type phenotype of the icd defective strain on minimal medium without glutamate is restored Streptococcus mutans

Protein Variants

Protein Variants Comment Organism
S102A site-directed mutagenesis, the mutant shows decreased affinity for isocitrate and 3.3% of wild-type activity Streptococcus mutans
S102G site-directed mutagenesis, the mutant shows decreased affinity for isocitrate and 2.8% of wild-type activity Streptococcus mutans
S102T site-directed mutagenesis, the mutant shows decreased affinity for isocitrate and 16% of wild-type activity Streptococcus mutans
S102Y site-directed mutagenesis, the mutant shows decreased affinity for isocitrate and 1.1% of wild-type activity Streptococcus mutans

Inhibitors

Inhibitors Comment Organism Structure
Ca2+
-
Streptococcus mutans
Co2+
-
Streptococcus mutans
Cu2+
-
Streptococcus mutans
Ni2+
-
Streptococcus mutans
Zn2+
-
Streptococcus mutans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.075
-
DL-isocitrate pH 7.5, 37°C, recombinant wild-type enzyme Streptococcus mutans
0.143
-
DL-isocitrate pH 7.5, 37°C, recombinant enzyme mutant S102G Streptococcus mutans
0.148
-
DL-isocitrate pH 7.5, 37°C, recombinant enzyme mutant S102A Streptococcus mutans
0.15
-
DL-isocitrate pH 7.5, 37°C, recombinant enzyme mutant S102T Streptococcus mutans
0.154
-
NAD+ pH 7.5, 37°C, recombinant enzyme Streptococcus mutans
0.246
-
NAD+ pH 7.5, 37°C, recombinant enzyme mutant S102A Streptococcus mutans
0.295
-
NAD+ pH 7.5, 37°C, recombinant enzyme mutant S102G Streptococcus mutans
0.35
-
NAD+ pH 7.5, 37°C, recombinant enzyme mutant S102T Streptococcus mutans
0.385
-
DL-isocitrate pH 7.5, 37°C, recombinant enzyme mutant S102Y Streptococcus mutans
1.56
-
NAD+ pH 7.5, 37°C, recombinant enzyme mutant S102Y Streptococcus mutans

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ best divalent cation Streptococcus mutans
additional information the enzyme is dependent on divalent cations Streptococcus mutans

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
70000
-
recombinant enzyme, gel filtration Streptococcus mutans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
DL-isocitrate + NAD+ Streptococcus mutans
-
2-oxoglutarate + CO2 + NADH
-
r

Organism

Organism UniProt Comment Textmining
Streptococcus mutans
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein catalytically important phosphorylation site at Ser102 Streptococcus mutans

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli Streptococcus mutans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DL-isocitrate + NAD+
-
Streptococcus mutans 2-oxoglutarate + CO2 + NADH
-
r
additional information the enzyme is also active with NADP+ and NADPH, cf. EC 1.1.1.42 Streptococcus mutans ?
-
?

Subunits

Subunits Comment Organism
homodimer
-
Streptococcus mutans

Synonyms

Synonyms Comment Organism
IDH
-
Streptococcus mutans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
Streptococcus mutans

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 55 activity range, profile overview Streptococcus mutans

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
purified recombinant enzyme, stable up to, rapid inactivation above Streptococcus mutans
50
-
purified recombinant enzyme, inactivation Streptococcus mutans

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.5
-
DL-isocitrate pH 7.5, 37°C, recombinant enzyme mutant S102Y Streptococcus mutans
3
-
NAD+ pH 7.5, 37°C, recombinant enzyme mutant S102A Streptococcus mutans
3.3
-
DL-isocitrate pH 7.5, 37°C, recombinant enzyme mutant S102A Streptococcus mutans
3.5
-
NAD+ pH 7.5, 37°C, recombinant enzyme mutant S102Y Streptococcus mutans
4
-
DL-isocitrate pH 7.5, 37°C, recombinant enzyme mutant S102G Streptococcus mutans
9.1
-
NAD+ pH 7.5, 37°C, recombinant enzyme mutant S102G Streptococcus mutans
25
-
DL-isocitrate pH 7.5, 37°C, recombinant enzyme mutant S102T Streptococcus mutans
56
-
NAD+ pH 7.5, 37°C, recombinant wild-type enzyme Streptococcus mutans
59
-
NAD+ pH 7.5, 37°C, recombinant enzyme mutant S102T Streptococcus mutans
124
-
DL-isocitrate pH 7.5, 37°C, recombinant wild-type enzyme Streptococcus mutans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
-
Streptococcus mutans

pH Range

pH Minimum pH Maximum Comment Organism
7.2 9.2 activity range, profile overview Streptococcus mutans

Cofactor

Cofactor Comment Organism Structure
additional information the enzyme is also active with NADP+ and NADPH, cf. EC 1.1.1.42 Streptococcus mutans
NAD+
-
Streptococcus mutans
NADH
-
Streptococcus mutans

General Information

General Information Comment Organism
evolution the ancient NAD-dependent IDHs might be the underlying origin of phosphorylation mechanism used by their bacterial NADP-dependent homologues Streptococcus mutans
additional information Ser102 plays an important role in substrate binding and is required for the enzyme function Streptococcus mutans

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.000002
-
NAD+ pH 7.5, 37°C, recombinant enzyme mutant S102Y Streptococcus mutans
0.000004
-
DL-isocitrate pH 7.5, 37°C, recombinant enzyme mutant S102Y Streptococcus mutans
0.00001
-
NAD+ pH 7.5, 37°C, recombinant enzyme mutant S102A Streptococcus mutans
0.000022
-
DL-isocitrate pH 7.5, 37°C, recombinant enzyme mutant S102A Streptococcus mutans
0.000028
-
DL-isocitrate pH 7.5, 37°C, recombinant enzyme mutant S102G Streptococcus mutans
0.00003
-
NAD+ pH 7.5, 37°C, recombinant enzyme mutant S102G Streptococcus mutans
0.00017
-
NAD+ pH 7.5, 37°C, recombinant enzyme mutant S102T Streptococcus mutans
0.00017
-
DL-isocitrate pH 7.5, 37°C, recombinant enzyme mutant S102T Streptococcus mutans
0.00036
-
NAD+ pH 7.5, 37°C, recombinant enzyme Streptococcus mutans
0.00165
-
DL-isocitrate pH 7.5, 37°C, recombinant wild-type enzyme Streptococcus mutans