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Literature summary 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

Protein Variants

EC Number Protein Variants Comment Organism
1.2.1.105 H260A mutation drastically reduces catalytic activity Escherichia coli
1.2.1.105 H260E mutation drastically reduces catalytic activity Escherichia coli
1.2.1.105 H260E/H298N almost 20fold decrease in kcat/Km vlaue Escherichia coli
1.2.1.105 H298A mutation drastically reduces catalytic activity Escherichia coli
1.2.1.105 H298D mutant accepts unnatural substrate 2-oxovalerate Escherichia coli
1.2.1.105 H298L mutant accepts unnatural substrate 2-oxovalerate Escherichia coli
1.2.1.105 H298T mutant accepts unnatural substrate 2-oxovalerate Escherichia coli
1.2.1.105 H298V mutant accepts unnatural substrate 2-oxovalerate Escherichia coli
1.2.1.105 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.105 0.0025
-
2-oxoglutarate mutant H298T, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 0.00261
-
2-oxoglutarate wild-type, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 0.00273
-
2-oxoglutarate mutant H260E/H298N, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 0.00341
-
2-oxoglutarate mutant H298L, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 0.0063
-
2-oxovalerate mutant H298L, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 0.00702
-
2-oxovalerate mutant H298D, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 0.00896
-
2-oxovalerate mutant H298V, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 0.0153
-
2-oxovalerate mutant H298T, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 0.0163
-
2-oxovalerate wild-type, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 0.165
-
2-oxoglutarate mutant H298V, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 0.383
-
2-oxoglutarate mutant H260E, pH not specified in the publication, temperature not specified in the publication Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.105 2-oxoglutarate + CoA + NAD+ Escherichia coli
-
succinyl-CoA + CO2 + NADH
-
?

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.105 2-oxoglutarate + CoA + NAD+
-
Escherichia coli succinyl-CoA + CO2 + NADH
-
?
1.2.1.105 2-oxovalerate + CoA + NAD+ unnatural substrate, very poor substrate of wild-type Escherichia coli ? + CO2 + NADH
-
?

Synonyms

EC Number Synonyms Comment Organism
1.2.1.105 SucA
-
Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.1.105 0.0064
-
2-oxoglutarate mutant H298T, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 0.03
-
2-oxovalerate mutant H298T, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 0.032
-
2-oxoglutarate mutant H260E, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 0.076
-
2-oxovalerate wild-type, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 0.094
-
2-oxovalerate mutant H298L, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 0.099
-
2-oxoglutarate mutant H298V, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 0.134
-
2-oxoglutarate mutant H260E/H298N, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 0.415
-
2-oxoglutarate mutant H298L, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 0.556
-
2-oxovalerate mutant H298V, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 1.24
-
2-oxovalerate mutant H298D, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 2.15
-
2-oxoglutarate wild-type, pH not specified in the publication, temperature not specified in the publication Escherichia coli

General Information

EC Number General Information Comment Organism
1.2.1.105 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]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.2.1.105 0.002
-
2-oxovalerate mutant H298T, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 0.0047
-
2-oxovalerate wild-type, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 0.0084
-
2-oxoglutarate mutant H260E, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 0.015
-
2-oxovalerate mutant H298L, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 0.062
-
2-oxovalerate mutant H298V, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 0.18
-
2-oxovalerate mutant H298D, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 0.6
-
2-oxoglutarate mutant H298V, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 1.5
-
2-oxoglutarate mutant H298T, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 49.1
-
2-oxoglutarate mutant H260E/H298N, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 122
-
2-oxoglutarate mutant H298L, pH not specified in the publication, temperature not specified in the publication Escherichia coli
1.2.1.105 824
-
2-oxoglutarate wild-type, pH not specified in the publication, temperature not specified in the publication Escherichia coli