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Literature summary for 1.3.5.1 extracted from

  • Maklashina, E.; Iverson, T.M.; Sher, Y.; Kotlyar, V.; Andrell, J.; Mirza, O.; Hudson, J.M.; Armstrong, F.A.; Rothery, R.A.; Weiner, J.H.; Cecchini, G.
    Fumarate reductase and succinate oxidase activity of Escherichia coli complex II homologs are perturbed differently by mutation of the flavin binding domain (2006), J. Biol. Chem., 281, 11357-11365.
    View publication on PubMed
Search for more literature for 1.3.5.1

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, x-ray structure of mutant E49Q Escherichia coli

Protein Variants

Protein Variants Comment Organism
E49A decrease in catalytic efficiency of both fumarate reduction and succinate oxidation Escherichia coli
E49Q decrease in catalytic efficiency of both fumarate reduction and succinate oxidation Escherichia coli
additional information investigation on the role of the amino acid side chain in enzymes with Glu/Gln/Ala substitutions at fumarate reductase FrdA Glu49 and succinate dehydrogenase SdhA, EC 1.5.3.1, Gln50. The mutant enzymes with Ala substitutions in either Frd or Sdh remain functionally similar to their wild type counterparts. There are, however, dramatic changes in the catalytic properties when Glu and Gln are exchanged for each other in Frd and Sdh. Both enzymes are more efficient succinate oxidases when Gln is in the target position and a better fumarate reductase when Glu is present. Structural and catalytic analyses of the FrdA E49Q and SdhA Q50E mutants suggest that coulombic effects and the electronic state of the FAD are critical in dictating the preferred directionality of the succinate/fumarate interconversions Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
malonate
-
 Escherichia coli
oxaloacetate
-
 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.02
-
 fumarate wild-type, pH 7.0, 30°C Escherichia coli
0.03
-
 fumarate mutant E49A, pH 7.0, 30°C Escherichia coli
0.11
-
 succinate mutant E49A, pH 7.0, 30°C Escherichia coli
0.22
-
 succinate mutant E49A, pH 7.0, 30°C Escherichia coli
0.55
-
 succinate wild-type, pH 7.0, 30°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P00363
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
fumarate + menaquinol
-
 Escherichia coli succinate + menaquinone
-
 r
succinate + menaquinone
-
 Escherichia coli fumarate + menaquinol
-
 r

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1
-
 fumarate mutant E49A, pH 7.0, 30°C Escherichia coli
2.4
-
 succinate mutant E49A, pH 7.0, 30°C Escherichia coli
4
-
 succinate mutant E49A, pH 7.0, 30°C Escherichia coli
30
-
 succinate wild-type, pH 7.0, 30°C Escherichia coli
32
-
 fumarate mutant E49A, pH 7.0, 30°C Escherichia coli
250
-
 fumarate wild-type, pH 7.0, 30°C Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00006
-
 oxaloacetate mutant E49A, pH 7.0, 30°C Escherichia coli
0.0001
-
 oxaloacetate mutant E49A, pH 7.0, 30°C Escherichia coli
0.0003
-
 oxaloacetate wild-type, pH 7.0, 30°C Escherichia coli
0.005
-
 malonate mutant E49A, pH 7.0, 30°C Escherichia coli
0.01
-
 malonate mutant E49A, pH 7.0, 30°C Escherichia coli
0.025
-
 malonate wild-type, pH 7.0, 30°C Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
11
-
 succinate mutant E49A, pH 7.0, 30°C Escherichia coli
36
-
 succinate mutant E49A, pH 7.0, 30°C Escherichia coli
54
-
 succinate wild-type, pH 7.0, 30°C Escherichia coli
97
-
 fumarate mutant E49A, pH 7.0, 30°C Escherichia coli
232
-
 fumarate wild-type, pH 7.0, 30°C Escherichia coli