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Literature summary for 1.2.1.105 extracted from

  • Shim, d.a. .J.; Nemeria, N.S.; Balakrishnan, A.; Patel, H.; Song, J.; Wang, J.; Jordan, F.; Farinas, E.T.
    Assignment of function to histidines 260 and 298 by engineering the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase complex; substitutions that lead to acceptance of substrates lacking the 5-carboxyl group (2011), Biochemistry, 50, 7705-7709 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.2.1.105

Protein Variants

Protein Variants Comment Organism
H260A mutation drastically reduces catalytic activity Escherichia coli
H260E mutation drastically reduces catalytic activity Escherichia coli
H260E/H298N almost 20fold decrease in kcat/Km vlaue Escherichia coli
H298A mutation drastically reduces catalytic activity Escherichia coli
H298D mutant accepts unnatural substrate 2-oxovalerate Escherichia coli
H298L mutant accepts unnatural substrate 2-oxovalerate Escherichia coli
H298T mutant accepts unnatural substrate 2-oxovalerate Escherichia coli
H298V mutant accepts unnatural substrate 2-oxovalerate Escherichia coli
additional information engineering of the E1 component to accept substrates lacking the 5-carboxylate group. Residue H260 is required for substrate recognition, but H298 can be replaced by hydrophobic residues of similar molecular volume Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0025
-
 2-oxoglutarate mutant H298T, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.00261
-
 2-oxoglutarate wild-type, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.00273
-
 2-oxoglutarate mutant H260E/H298N, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.00341
-
 2-oxoglutarate mutant H298L, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.0063
-
 2-oxovalerate mutant H298L, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.00702
-
 2-oxovalerate mutant H298D, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.00896
-
 2-oxovalerate mutant H298V, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.0153
-
 2-oxovalerate mutant H298T, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.0163
-
 2-oxovalerate wild-type, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.165
-
 2-oxoglutarate mutant H298V, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.383
-
 2-oxoglutarate mutant H260E, pH not specified in the publication, temperature not specified in the publication Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-oxoglutarate + CoA + NAD+ Escherichia coli
-
 succinyl-CoA + CO2 + NADH
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AFG3 i.e. 2-oxoglutarate dehydrogenase E1 component SucA, cf. EC 1.2.4.2
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate + CoA + NAD+
-
 Escherichia coli succinyl-CoA + CO2 + NADH
-
 ?
2-oxovalerate + CoA + NAD+ unnatural substrate, very poor substrate of wild-type Escherichia coli ? + CO2 + NADH
-
 ?

Synonyms

Synonyms Comment Organism
SucA
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0064
-
 2-oxoglutarate mutant H298T, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.03
-
 2-oxovalerate mutant H298T, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.032
-
 2-oxoglutarate mutant H260E, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.076
-
 2-oxovalerate wild-type, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.094
-
 2-oxovalerate mutant H298L, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.099
-
 2-oxoglutarate mutant H298V, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.134
-
 2-oxoglutarate mutant H260E/H298N, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.415
-
 2-oxoglutarate mutant H298L, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.556
-
 2-oxovalerate mutant H298V, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.24
-
 2-oxovalerate mutant H298D, pH not specified in the publication, temperature not specified in the publication Escherichia coli
2.15
-
 2-oxoglutarate wild-type, pH not specified in the publication, temperature not specified in the publication Escherichia coli

General Information

General Information Comment Organism
physiological function hybrid complexes consisting of recombinant components of OGDHc and pyruvate dehydrogenase enzymes suggest that a different component is the gatekeeper for specificity for the two multienzyme complexes in bacteria, the E1 component for pyruvate, but the E2 component for 2-oxoglutarate Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.002
-
 2-oxovalerate mutant H298T, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.0047
-
 2-oxovalerate wild-type, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.0084
-
 2-oxoglutarate mutant H260E, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.015
-
 2-oxovalerate mutant H298L, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.062
-
 2-oxovalerate mutant H298V, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.18
-
 2-oxovalerate mutant H298D, pH not specified in the publication, temperature not specified in the publication Escherichia coli
0.6
-
 2-oxoglutarate mutant H298V, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.5
-
 2-oxoglutarate mutant H298T, pH not specified in the publication, temperature not specified in the publication Escherichia coli
49.1
-
 2-oxoglutarate mutant H260E/H298N, pH not specified in the publication, temperature not specified in the publication Escherichia coli
122
-
 2-oxoglutarate mutant H298L, pH not specified in the publication, temperature not specified in the publication Escherichia coli
824
-
 2-oxoglutarate wild-type, pH not specified in the publication, temperature not specified in the publication Escherichia coli