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Literature summary for 1.2.4.2 extracted from

  • Chakraborty, J.; Nemeria, N.; Zhang, X.; Nareddy, P.; Szostak, M.; Farinas, E.; Jordan, F.
    Engineering 2-oxoglutarate dehydrogenase to a 2-oxo aliphatic dehydrogenase complex by optimizing consecutive components (2020), AIChE J., 66, e16769 .
No PubMed abstract available
Search for more literature for 1.2.4.2

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli JW0715 cells Escherichia coli

Protein Variants

Protein Variants Comment Organism
H298D mutation in subunit E1o, active for 2-oxovalerate in an E1o-specific assay Escherichia coli
H298D the mutant enzyme shows 4.4fold increased activity toward 2-oxovalerate and 1200fold decreased activity toward 2-oxoglutarate compared to the wild type enzyme Escherichia coli
H348F mutation in subunit Eo, leads to activity for 2-oxovalerate in the reconstituted complex with E1o-H298D Escherichia coli
H348Q mutation in subunit Eo, leads to activity for 2-oxovalerate in the reconstituted complex with E1o-H298D Escherichia coli
H348Y mutation in subunit Eo, leads to activity for 2-oxovalerate in the reconstituted complex with E1o-H298D Escherichia coli
additional information conversion of enzyme from a 2-oxoglutarate dehydrogenase to a 2-oxo aliphatic dehydrogenase complex by evolving the E1o and E2o components. Mutants E2o-S333M, E2o-H348F, E2o-H348Q, and E2o-H348Y show activity for 2-oxovalerate in the reconstituted complex with E1o-H298D Escherichia coli
S333M mutation in subunit Eo, leads to activity for 2-oxovalerate in the reconstituted complex with E1o-H298D Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.006
-
 2-oxoglutarate wild type enzyme, at pH 8.0 and 30°C Escherichia coli
0.01
-
 2-oxovalerate mutant E1o-H298D/E2o-H348F, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.01
-
 2-oxovalerate mutant E1o-H298D/E2o-H348Y, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.02
-
 2-oxoglutarate mutant E1o-H298D/E2o-H348Y, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.03
-
 2-oxoglutarate mutant E1o-H298D, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.03
-
 2-oxoglutarate mutant E1o-H298D/E2o-H348F, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.04
-
 2-oxoglutarate wild-type, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.04
-
 2-oxoglutarate mutant E1o-H298D/E2o-S333M, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.05
-
 2-oxovalerate mutant E1o-H298D/E2o-H348Q, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.07
-
 2-oxoglutarate mutant E1o-H298D/E2o-H348Q, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.08
-
 2-oxovalerate mutant E1o-H298D/E2o-S333M, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.11
-
 2-oxo-5-hexenoic acid mutant E1o-H298D/E2o-S333M, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.5
-
 2-oxo-5-hexenoic acid mutant E1o-H298D/E2o-H348F, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.73
-
 2-oxo-5-hexenoic acid mutant E1o-H298D/E2o-H348Y, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.1
-
 2-oxo-5-hexenoic acid mutant E1o-H298D/E2o-H348Q, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.87
-
 2-oxoglutarate mutant enzyme H298D, at pH 8.0 and 30°C Escherichia coli
6.62
-
 2-oxovalerate mutant enzyme H298D, at pH 8.0 and 30°C Escherichia coli
8.01
-
 2-oxo-5-hexenoic acid wild type enzyme, at pH 8.0 and 30°C Escherichia coli
8.18
-
 2-oxovalerate wild type enzyme, at pH 8.0 and 30°C Escherichia coli
11.1
-
 2-oxo-5-hexenoic acid mutant enzyme H298D, at pH 8.0 and 30°C Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ 1 mM used in assay conditions Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine Escherichia coli
-
 [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0168
-
 wild type enzyme, with 2-oxo-5-hexenoate as substrate, at pH 8.0 and 30°C Escherichia coli
0.042
-
 mutant enzyme H298D, with 2-oxo-5-hexenoate as substrate, at pH 8.0 and 30°C Escherichia coli
0.0429
-
 wild type enzyme, with 2-oxovalerate as substrate, at pH 8.0 and 30°C Escherichia coli
0.135
-
 mutant enzyme H298D, with 2-oxovalerate as substrate, at pH 8.0 and 30°C Escherichia coli
0.206
-
 mutant enzyme H298D, with 2-oxoglutarate as substrate, at pH 8.0 and 30°C Escherichia coli
0.775
-
 wild type enzyme, with 2-oxoglutarate as substrate, at pH 8.0 and 30°C Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxo-5-hexenoic acid + 2,6-dichlorophenolindophenol
-
 Escherichia coli ?
-
 ?
2-oxo-5-hexenoic acid + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine 2-oxo-5-hexenoic acid is not a substrate for wild-type Escherichia coli [dihydrolipoyllysine-residue succinyltransferase] S-pent-4-enoyldihydrolipoyllysine + CO2
-
 ?
2-oxoglutarate + 2,6-dichlorophenolindophenol
-
 Escherichia coli ?
-
 ?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
-
 Escherichia coli [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
 ?
2-oxovalerate + 2,6-dichlorophenolindophenol
-
 Escherichia coli ?
-
 ?
2-oxovalerate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine 2-oxovalerate is not a substrate for wild-type Escherichia coli [dihydrolipoyllysine-residue succinyltransferase] S-butanoyldihydrolipoyllysine + CO2
-
 ?

Subunits

Subunits Comment Organism
? x * 105000, calculated from amino acid sequence Escherichia coli

Synonyms

Synonyms Comment Organism
2-oxoglutarate dehydrogenase complex
-
 Escherichia coli
E1o 2-oxoglutarate dehydrogenase subunit of the 2-oxoglutarate dehydrogenase complex Escherichia coli
OGDHC
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0595
-
 2-oxo-5-hexenoic acid wild type enzyme, at pH 8.0 and 30°C Escherichia coli
0.148
-
 2-oxo-5-hexenoic acid mutant enzyme H298D, at pH 8.0 and 30°C Escherichia coli
0.152
-
 2-oxovalerate wild type enzyme, at pH 8.0 and 30°C Escherichia coli
0.34
-
 2-oxovalerate mutant E1o-H298D/E2o-H348Q, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.38
-
 2-oxovalerate mutant E1o-H298D/E2o-S333M, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.48
-
 2-oxovalerate mutant enzyme H298D, at pH 8.0 and 30°C Escherichia coli
0.57
-
 2-oxovalerate mutant E1o-H298D/E2o-H348Y, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.65
-
 2-oxo-5-hexenoic acid mutant E1o-H298D/E2o-H348Q, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.73
-
 2-oxoglutarate mutant enzyme H298D, at pH 8.0 and 30°C Escherichia coli
0.81
-
 2-oxovalerate mutant E1o-H298D/E2o-H348F, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.86
-
 2-oxo-5-hexenoic acid mutant E1o-H298D/E2o-H348Y, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.99
-
 2-oxo-5-hexenoic acid mutant E1o-H298D/E2o-H348F, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.68
-
 2-oxo-5-hexenoic acid mutant E1o-H298D/E2o-S333M, pH not specified in the publication, temperature not specified in the publication Escherichia coli
2.7
-
 2-oxoglutarate wild type enzyme, at pH 8.0 and 30°C Escherichia coli
6.8
-
 2-oxoglutarate mutant E1o-H298D/E2o-H348Y, pH not specified in the publication, temperature not specified in the publication Escherichia coli
7.3
-
 2-oxoglutarate mutant E1o-H298D/E2o-H348F, pH not specified in the publication, temperature not specified in the publication Escherichia coli
8.4
-
 2-oxoglutarate mutant E1o-H298D/E2o-S333M, pH not specified in the publication, temperature not specified in the publication Escherichia coli
10.5
-
 2-oxoglutarate mutant E1o-H298D/E2o-H348Q, pH not specified in the publication, temperature not specified in the publication Escherichia coli
21.1
-
 2-oxoglutarate mutant E1o-H298D, pH not specified in the publication, temperature not specified in the publication Escherichia coli
35
-
 2-oxoglutarate wild-type, pH not specified in the publication, temperature not specified in the publication Escherichia coli

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate
-
 Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.0074
-
 2-oxo-5-hexenoate wild type enzyme, at pH 8.0 and 30°C Escherichia coli
0.0134
-
 2-oxo-5-hexenoate mutant enzyme H298D, at pH 8.0 and 30°C Escherichia coli
0.0165
-
 2-oxovalerate wild type enzyme, at pH 8.0 and 30°C Escherichia coli
0.0725
-
 2-oxovalerate mutant enzyme H298D, at pH 8.0 and 30°C Escherichia coli
0.39
-
 2-oxoglutarate mutant enzyme H298D, at pH 8.0 and 30°C Escherichia coli
0.59
-
 2-oxo-5-hexenoic acid mutant E1o-H298D/E2o-H348Q, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.17
-
 2-oxo-5-hexenoic acid mutant E1o-H298D/E2o-H348Y, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.98
-
 2-oxo-5-hexenoic acid mutant E1o-H298D/E2o-H348F, pH not specified in the publication, temperature not specified in the publication Escherichia coli
4.7
-
 2-oxovalerate mutant E1o-H298D/E2o-S333M, pH not specified in the publication, temperature not specified in the publication Escherichia coli
6.8
-
 2-oxovalerate mutant E1o-H298D/E2o-H348Q, pH not specified in the publication, temperature not specified in the publication Escherichia coli
15.3
-
 2-oxo-5-hexenoic acid mutant E1o-H298D/E2o-S333M, pH not specified in the publication, temperature not specified in the publication Escherichia coli
57
-
 2-oxovalerate mutant E1o-H298D/E2o-H348Y, pH not specified in the publication, temperature not specified in the publication Escherichia coli
81
-
 2-oxovalerate mutant E1o-H298D/E2o-H348F, pH not specified in the publication, temperature not specified in the publication Escherichia coli
149
-
 2-oxoglutarate mutant E1o-H298D/E2o-H348Q, pH not specified in the publication, temperature not specified in the publication Escherichia coli
210
-
 2-oxoglutarate mutant E1o-H298D/E2o-S333M, pH not specified in the publication, temperature not specified in the publication Escherichia coli
244
-
 2-oxoglutarate mutant E1o-H298D/E2o-H348F, pH not specified in the publication, temperature not specified in the publication Escherichia coli
338
-
 2-oxoglutarate mutant E1o-H298D/E2o-H348Y, pH not specified in the publication, temperature not specified in the publication Escherichia coli
456.6
-
 2-oxoglutarate wild type enzyme, at pH 8.0 and 30°C Escherichia coli
703
-
 2-oxoglutarate mutant E1o-H298D, pH not specified in the publication, temperature not specified in the publication Escherichia coli
875
-
 2-oxoglutarate wild-type, pH not specified in the publication, temperature not specified in the publication Escherichia coli