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Literature summary for 1.1.1.42 extracted from

  • Camacho, M.L.; Brown, R.A.; Bonete, M.J.; Danson, M.J.; Hough, D.W.
    Isocitrate dehydrogenases from Haloferax volcanii and Sulfolobus solfataricus: enzyme purification, characterisation and N-terminal sequence (1995), FEMS Microbiol. Lett., 134, 85-90.
    View publication on PubMed
Search for more literature for 1.1.1.42

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.009
-
 isocitrate pH 8.0, 55°C, cofactor: NADP+ Saccharolobus solfataricus
0.085
-
 NADP+ pH 8.0, 55°C Saccharolobus solfataricus
0.11
-
 NADP+ pH 8.0, 30°C Haloferax volcanii
0.13
-
 isocitrate pH 8.0, 30°C, cofactor: NADP+ Haloferax volcanii
2.9
-
 NAD+ pH 8.0, 55°C Saccharolobus solfataricus

Metals/Ions

Metals/Ions Comment Organism Structure
KCl the activity of the enzyme is markedly dependent on the concentration of NaCl or KC1 in the Tris/EDTA/Mg2+ buffer, being maximal in 0.5 M NaCl or KCl. The stimulatory effect of KCl is greater than that of NaCl Haloferax volcanii
NaCl the activity of the enzyme is markedly dependent on the concentration of NaCl or KC1 in the Tris/EDTA/Mg2+ buffer, being maximal in 0.5 M NaCl or KCl. The stimulatory effect of KCl is greater than that of NaCl Haloferax volcanii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45000
-
 2 * 45000, SDS-PAGE Saccharolobus solfataricus
62000
-
 2 * 62000, SDS-PAGE Haloferax volcanii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
isocitrate + NADP+ Haloferax volcanii
-
 2-oxoglutarate + CO2 + NADPH + H+
-
 ?
isocitrate + NADP+ Saccharolobus solfataricus
-
 2-oxoglutarate + CO2 + NADPH + H+
-
 ?
isocitrate + NADP+ Saccharolobus solfataricus DSM 1616
-
 2-oxoglutarate + CO2 + NADPH + H+
-
 ?
isocitrate + NADP+ Haloferax volcanii DSM 3757
-
 2-oxoglutarate + CO2 + NADPH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Haloferax volcanii
-
-
-
Haloferax volcanii DSM 3757
-
-
-
Saccharolobus solfataricus Q9UWG7
-
-
Saccharolobus solfataricus DSM 1616 Q9UWG7
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Haloferax volcanii
-
 Saccharolobus solfataricus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
40
-
 pH 8.0, 30°C Haloferax volcanii
152
-
 pH 8.0, 55°C Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
isocitrate + NAD+ Km-value for NAD+ is 34fold higher compared to KM-value for NADP+ Saccharolobus solfataricus 2-oxoglutarate + CO2 + NADH + H+
-
 ?
isocitrate + NAD+ Km-value for NAD+ is 34fold higher compared to KM-value for NADP+ Saccharolobus solfataricus DSM 1616 2-oxoglutarate + CO2 + NADH + H+
-
 ?
isocitrate + NADP+
-
 Haloferax volcanii 2-oxoglutarate + CO2 + NADPH + H+
-
 ?
isocitrate + NADP+
-
 Saccharolobus solfataricus 2-oxoglutarate + CO2 + NADPH + H+
-
 ?
isocitrate + NADP+ Km-value for NAD+ is 34fold higher compared to KM-value for NADP+ Saccharolobus solfataricus 2-oxoglutarate + CO2 + NADPH + H+
-
 ?
isocitrate + NADP+
-
 Saccharolobus solfataricus DSM 1616 2-oxoglutarate + CO2 + NADPH + H+
-
 ?
isocitrate + NADP+ Km-value for NAD+ is 34fold higher compared to KM-value for NADP+ Saccharolobus solfataricus DSM 1616 2-oxoglutarate + CO2 + NADPH + H+
-
 ?
isocitrate + NADP+
-
 Haloferax volcanii DSM 3757 2-oxoglutarate + CO2 + NADPH + H+
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 45000, SDS-PAGE Saccharolobus solfataricus
dimer 2 * 62000, SDS-PAGE Haloferax volcanii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Haloferax volcanii
55
-
 assay at Saccharolobus solfataricus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 the enzyme is incubated in Tris/EDTA/Mg2+ buffer containing either 0.5 M or 3 M KCl. The thermal stability of the enzyme is substantially reduced at the lower KCl concentration, with concomitant differences in the activation energies for the thermal inactivation process. Omission of Mg2+ from the incubation buffer greatly accelerates the rate of loss of activity, and its presence plus that of 3 M KCl are recommended for storage of the enzyme Haloferax volcanii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Haloferax volcanii
8
-
 assay at Saccharolobus solfataricus