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Literature summary for 1.1.1.41 extracted from

  • Wang, P.; Chen, X.; Yang, J.; Pei, Y.; Bian, M.; Zhu, G.
    Characterization of the nicotinamide adenine dinucleotides (NAD+ and NADP+) binding sites of the monomeric isocitrate dehydrogenases from Campylobacter species (2019), Biochimie, 160, 148-155 .
    View publication on PubMed
Search for more literature for 1.1.1.41

Activating Compound

Activating Compound Comment Organism Structure
citrate 110% activity at 2 mM Campylobacter concisus

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Rosetta(DE3) cells Campylobacter concisus

Protein Variants

Protein Variants Comment Organism
L580H/L591R/A640R the mutant has a 21fold lower Km value for NADP+ when compared to the original enzyme. The turnover rate (kcat) towards isocitrate of the mutant is reduced by more than 50% as compared to the wild type enzyme and even though the mutant is capable of using NADP+ for catalysis, ist catalytic efficiency (kcat/Km) for isocitrate is relatively low, being half of that for the wild type enzyme as using NAD+ Campylobacter concisus

Inhibitors

Inhibitors Comment Organism Structure
2-oxoglutarate complete inhibition at 10 mM Campylobacter concisus
ADP 85% residual activity at 2 mM Campylobacter concisus
AMP 79% residual activity at 2 mM Campylobacter concisus
ATP 68% residual activity at 2 mM Campylobacter concisus
Ca2+ 1.9% residual activity at 2 mM Campylobacter concisus
cis-aconitate 91% residual activity at 2 mM Campylobacter concisus
Co2+ 8.7% residual activity at 2 mM Campylobacter concisus
Cu2+ 1.3% residual activity at 2 mM Campylobacter concisus
fumarate 96% residual activity at 2 mM Campylobacter concisus
K+ 1.7% residual activity at 2 mM Campylobacter concisus
L-glutamate 90% residual activity at 2 mM Campylobacter concisus
L-glutamine 96% residual activity at 2 mM Campylobacter concisus
additional information not influenced by pyruvate and malate Campylobacter concisus
Na+ 3.2% residual activity at 2 mM Campylobacter concisus
Ni2+ 4.4% residual activity at 2 mM Campylobacter concisus
oxaloacetate 98% residual activity at 2 mM Campylobacter concisus
succinate 95% residual activity at 2 mM Campylobacter concisus
Zn2+ 0.4% residual activity at 2 mM Campylobacter concisus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.031
-
 isocitrate mutant enzyme L580H/L591R/A640R, at pH 7.5 and 25°C Campylobacter concisus
0.038
-
 isocitrate wild type enzyme, at pH 7.5 and 25°C Campylobacter concisus
0.088
-
 NAD+ wild type enzyme, at pH 7.5 and 25°C Campylobacter concisus
0.207
-
 NADP+ mutant enzyme L580H/L591R/A640R, at pH 7.5 and 25°C Campylobacter concisus
4.3
-
 NADP+ wild type enzyme, at pH 7.5 and 25°C Campylobacter concisus
4.5
-
 NAD+ mutant enzyme L580H/L591R/A640R, at pH 7.5 and 25°C Campylobacter concisus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ Mg2+ can take the place of Mn2+ with 44.8% eficiency. Mg2+ promotes 94% activity in the presence of Mn2+. 2 mM used in assay conditions Campylobacter concisus
Mn2+ 100% activity, 2 mM used in assay conditions Campylobacter concisus
additional information in the presence of either Mn2+ or Mg2+, neither K+ nor Na+ affects enzyme activity Campylobacter concisus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
isocitrate + NAD+ Campylobacter concisus
-
 2-oxoglutarate + CO2 + NADH + H+
-
 ?
isocitrate + NAD+ Campylobacter concisus DSM9716
-
 2-oxoglutarate + CO2 + NADH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Campylobacter concisus
-
-
-
Campylobacter concisus DSM9716
-
-
-

Purification (Commentary)

Purification (Comment) Organism
TALON metal affinity resin column chromatography Campylobacter concisus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.3
-
 wild type enzyme, with NADP+ as cosubstrate, at pH 7.5 and 25°C Campylobacter concisus
49.3
-
 wild type enzyme, with NAD+ as cosubstrate, at pH 7.5 and 25°C Campylobacter concisus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
isocitrate + NAD+
-
 Campylobacter concisus 2-oxoglutarate + CO2 + NADH + H+
-
 ?
isocitrate + NAD+
-
 Campylobacter concisus DSM9716 2-oxoglutarate + CO2 + NADH + H+
-
 ?
isocitrate + NADP+ the enzyme has weak activity with NADP+ Campylobacter concisus 2-oxoglutarate + CO2 + NADPH + H+
-
 ?
isocitrate + NADP+ the enzyme has weak activity with NADP+ Campylobacter concisus DSM9716 2-oxoglutarate + CO2 + NADPH + H+
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 80000, His6-tagged recombinant enzyme, SDS-PAGE Campylobacter concisus
monomer 1 * 81000, calculated from amino acid sequence Campylobacter concisus

Synonyms

Synonyms Comment Organism
IDH
-
 Campylobacter concisus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
-
 Campylobacter concisus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
45 60 more than 60% activity between 45 and 60°C Campylobacter concisus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45 47 the enzyme is stable below 45°C. The activity of the enzyme drops quickly above 45°C. Incubation at 47°C for 20 min causes 54% and 51% loss of activity with Mn2+ or Mg2+, respectively Campylobacter concisus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
33
-
 NADP+ wild type enzyme, at pH 7.5 and 25°C Campylobacter concisus
37
-
 isocitrate mutant enzyme L580H/L591R/A640R, at pH 7.5 and 25°C Campylobacter concisus
43
-
 NADP+ mutant enzyme L580H/L591R/A640R, at pH 7.5 and 25°C Campylobacter concisus
78
-
 NAD+ wild type enzyme, at pH 7.5 and 25°C Campylobacter concisus
79
-
 NAD+ mutant enzyme L580H/L591R/A640R, at pH 7.5 and 25°C Campylobacter concisus
85
-
 isocitrate wild type enzyme, at pH 7.5 and 25°C Campylobacter concisus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Campylobacter concisus

pH Range

pH Minimum pH Maximum Comment Organism
6.5 8 more than 60% activity between pH 6.5 and 8.0 Campylobacter concisus

Cofactor

Cofactor Comment Organism Structure
NAD+ the recombinant enzyme has a significant high coenzyme preference for NAD+ Campylobacter concisus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
7.7
-
 NADP+ wild type enzyme, at pH 7.5 and 25°C Campylobacter concisus
17.7
-
 NAD+ mutant enzyme L580H/L591R/A640R, at pH 7.5 and 25°C Campylobacter concisus
208
-
 NADP+ mutant enzyme L580H/L591R/A640R, at pH 7.5 and 25°C Campylobacter concisus
886
-
 NAD+ wild type enzyme, at pH 7.5 and 25°C Campylobacter concisus
1200
-
 isocitrate mutant enzyme L580H/L591R/A640R, at pH 7.5 and 25°C Campylobacter concisus
2200
-
 isocitrate wild type enzyme, at pH 7.5 and 25°C Campylobacter concisus