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Literature summary for 1.1.1.41 extracted from

  • Wang, P.; Jin, M.; Zhu, G.
    Biochemical and molecular characterization of NAD(+)-dependent isocitrate dehydrogenase from the ethanologenic bacterium Zymomonas mobilis (2012), FEMS Microbiol. Lett., 327, 134-141.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene idh, DNA and amino acid sequence determination and analysis, sequence comparisons, expression of His6-tagged enzyme in Escherichia coli strain BL21 (DE3) Zymomonas mobilis

Inhibitors

Inhibitors Comment Organism Structure
Ca2+
-
Zymomonas mobilis
Co2+
-
Zymomonas mobilis
Cu2+ complete inhibition Zymomonas mobilis
Ni2+
-
Zymomonas mobilis
Zn2+ complete inhibition Zymomonas mobilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.245
-
NAD+ pH 7.5, 37°C, with Mn2+, recombinant enzyme Zymomonas mobilis
0.312
-
NAD+ pH 7.5, 37°C, with Mg2+, recombinant enzyme Zymomonas mobilis
7.7
-
NADP+ pH 7.5, 37°C, with Mn2+, recombinant enzyme Zymomonas mobilis
8.2
-
NADP+ pH 7.5, 37°C, with Mg2+, recombinant enzyme Zymomonas mobilis

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ activates, 42.5% activity compared to Mn2+ Zymomonas mobilis
Mg2+ activates, 78% activity compared to Mn2+ Zymomonas mobilis
Mn2+ activates, best cation Zymomonas mobilis
additional information the recombinant ZmIDH activity is completely dependent on the divalent cation and Mn2+ is the most effective cation Zymomonas mobilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
46000
-
2 * 46000, recombinant His6-tagged enzyme, SDS-PAGE Zymomonas mobilis
74000
-
recombinant His6-tagged enzyme, gel filtration Zymomonas mobilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
isocitrate + NAD+ Zymomonas mobilis
-
2-oxoglutarate + CO2 + NADH + H+
-
?
isocitrate + NAD+ Zymomonas mobilis ATCC 10988
-
2-oxoglutarate + CO2 + NADH + H+
-
?

Organism

Organism UniProt Comment Textmining
Zymomonas mobilis
-
ssp. mobiliss
-
Zymomonas mobilis ATCC 10988
-
ssp. mobiliss
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21 (DE3) Zymomonas mobilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
isocitrate + NAD+
-
Zymomonas mobilis 2-oxoglutarate + CO2 + NADH + H+
-
?
isocitrate + NAD+ poor performance of the recombinant ZmIDH in decarboxylation Zymomonas mobilis 2-oxoglutarate + CO2 + NADH + H+
-
?
isocitrate + NAD+
-
Zymomonas mobilis ATCC 10988 2-oxoglutarate + CO2 + NADH + H+
-
?
isocitrate + NAD+ poor performance of the recombinant ZmIDH in decarboxylation Zymomonas mobilis ATCC 10988 2-oxoglutarate + CO2 + NADH + H+
-
?
isocitrate + NADP+ poor performance of the recombinant ZmIDH in decarboxylation Zymomonas mobilis 2-oxoglutarate + CO2 + NADPH + H+
-
?
isocitrate + NADP+ poor performance of the recombinant ZmIDH in decarboxylation Zymomonas mobilis ATCC 10988 2-oxoglutarate + CO2 + NADPH + H+
-
?

Subunits

Subunits Comment Organism
dimer 2 * 46000, recombinant His6-tagged enzyme, SDS-PAGE Zymomonas mobilis

Synonyms

Synonyms Comment Organism
IDH
-
Zymomonas mobilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
-
Zymomonas mobilis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 60 and above, activity range, profile overview Zymomonas mobilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
purified recombinant His-tagged enzyme, rapid inactivation above Zymomonas mobilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
14
-
NADP+ pH 7.5, 37°C, with Mg2+, recombinant enzyme Zymomonas mobilis
25
-
NADP+ pH 7.5, 37°C, with Mn2+, recombinant enzyme Zymomonas mobilis
88
-
NAD+ pH 7.5, 37°C, with Mg2+, recombinant enzyme Zymomonas mobilis
112
-
NAD+ pH 7.5, 37°C, with Mn2+, recombinant enzyme Zymomonas mobilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
with Mn2+ Zymomonas mobilis
8.5
-
with Mg2+ Zymomonas mobilis

pH Range

pH Minimum pH Maximum Comment Organism
6.5 10 activity range, profile overview Zymomonas mobilis

Cofactor

Cofactor Comment Organism Structure
NAD+ ZmIDH displays a 165fold (kcat/Km) preference for NAD+ over NADP+ with Mg2+, and 142fold with Mn2+ Zymomonas mobilis
NADP+ ZmIDH displays a 165fold (kcat/Km) preference for NAD+ over NADP+ with Mg2+, and 142fold with Mn2+ Zymomonas mobilis

General Information

General Information Comment Organism
evolution the recombinant ZmIDH is mainly NAD+-dependent and its catalytic efficiency (kcat/Km) is relative low when compared to the prokaryotic NADP+-IDHs Zymomonas mobilis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.000002
-
NADP+ pH 7.5, 37°C, with Mg2+, recombinant enzyme Zymomonas mobilis
0.000003
-
NADP+ pH 7.5, 37°C, with Mn2+, recombinant enzyme Zymomonas mobilis
0.0003
-
NAD+ pH 7.5, 37°C, with Mg2+, recombinant enzyme Zymomonas mobilis
0.0005
-
NAD+ pH 7.5, 37°C, with Mn2+, recombinant enzyme Zymomonas mobilis