Literature summary for 1.3.5.1 extracted from

Yang, X.; Yu, L.; He, D.; Yu, C.A.
The quinone-binding site in succinate-ubiquinone reductase from Escherichia coli. Quinone-binding domain and amino acid residues involved in quinone binding (1998), J. Biol. Chem., 273, 31916-31923.

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Protein Variants

Protein Variants	Comment	Organism
F20L	growth on succinate is essentially the same as the wild-type, electron transfer activity, the apparent Km value for Q2 and the amount of azido-Q incorporated into the succinate dehydrogenase C subunit are comparable with those of the complement reductase, Phe-20 is not involved in the Q binding	Escherichia coli
H30A	growth on succinate is essentially the same as the wild-type, electron transfer activity, the apparent Km value for Q2 and the amount of azido-Q incorporated into the succinate dehydrogenase C subunit are comparable with those of the complement reductase, His-30 is not involved in the Q binding	Escherichia coli
R19A	growth on succinate is essentially the same as the wild-type, electron transfer activity, the apparent Km value for Q2 and the amount of azido-Q incorporated into the succinate dehydrogenase C subunit are comparable with those of the complement reductase, Arg-19 is not involved in the Q binding	Escherichia coli
R31A	the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, Arg-31 is a critical residue for succinate-Q-reductase	Escherichia coli
R31H	the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, the guanidino group of arginine is critical for succinate-Q reductase activity	Escherichia coli
R31K	the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, the guanidino group of arginine is critical for succinate-Q reductase activity, it occupies a much larger space than the primary amine of lysine, extends a longer distance, and may provide more chance for hydrogen bond formation, it may stabilize Q binding through pi-pi interactions between the guanidino group and the benzoquinone ring	Escherichia coli
S27A	the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, Ser-27 is a critical residue for succinate-Q-reductase, it participates in a hydrogen bond at the Q-binding site of the C subunit	Escherichia coli
S27C	the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, the size of the amino acid side chain at position 27 of C subunit is critical for Q binding	Escherichia coli
S27T	the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, the size of the amino acid side chain at position 27 of C subunit is critical for Q binding	Escherichia coli
S33A	the mutant has retarded aerobic growth rate in succinate/M9 medium and it has 35% of the succinate-Q-reducase activity of complement enzyme, the apparent Km value of this mutant for Q2 is about the same as wild-type, the purified mutant protein has azido-Q uptake comparable with that of complement reductase, the mutation of Ser-33 to alanine may greatly reduce enzyme turnover without affecting the affinity for Q	Escherichia coli
S33C	the mutant has retarded aerobic growth rate in succinate/M9 medium and it has 44% of the succinate-Q-reducase activity of complement enzyme, the apparent Km value of this mutant for Q2 is about the same as wild-type, the purified mutant protein has azido-Q uptake comparable with that of complement reductase	Escherichia coli
S33T	the mutant has retarded aerobic growth rate in succinate/M9 medium and it has 88% of the succinate-Q-reducase activity of complement enzyme, the apparent Km value of this mutant for Q2 is about the same as wild-type, the purified mutant protein has azido-Q uptake comparable with that of complement reductase	Escherichia coli
T17A	growth on succinate is essentially the same as the wild-type, electron transfer activity, the apparent Km value for Q2 and the amount of azido-Q incorporated into the succinate dehydrogenase C subunit are comparable with those of the complement reductase, Thr-17 is not involved in the Q binding	Escherichia coli
T23A	the mutation yields cells capable of aerobic growth on M9/succinate medium at a rate slightly slower than that of complement strain, 40% decrease in the specific activity of the mutant to catalyze electron transfer from succinate to Q, apparent Km for Q2 is the same as that of complement reductase, Thr-23 may not be involved in Q binding	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0089	-	ubiquinone-2	S33C mutant	Escherichia coli
0.009	-	ubiquinone-2	R19A and F20L mutants	Escherichia coli
0.01	-	ubiquinone-2	S33T mutant	Escherichia coli
0.0102	-	ubiquinone-2	T17A mutant	Escherichia coli
0.0106	-	ubiquinone-2	H30A mutant	Escherichia coli
0.0108	-	ubiquinone-2	wild-type and T23A mutant	Escherichia coli
0.0114	-	ubiquinone-2	S33A mutant	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	succinate dehydrogenase	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	activities of wild-type and mutants, expressed in micromol of succinate oxidized/min/nmol of cytochrome b556	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
succinate + 3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinone	the succinate dehydrogenase C subunit is responsible for ubiquinone binding	Escherichia coli	fumarate + 3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinol	-	?
succinate + ubiquinone	-	Escherichia coli	fumarate + ubiquinol	-	?
succinate + ubiquinone-2	-	Escherichia coli	fumarate + ubiquinol	-	r

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Release 2023.1 (January 2023)