Literature summary for 1.3.5.2 extracted from

Kow, R.L.; Whicher, J.R.; McDonald, C.A.; Palfey, B.A.; Fagan, R.L.
Disruption of the proton relay network in the class 2 dihydroorotate dehydrogenase from Escherichia coli (2009), Biochemistry, 48, 9801-9809.

Search for more literature for 1.3.5.2

Protein Variants

Protein Variants	Comment	Organism
F115A	mutation slows the rate of flavin reduction by 3 orders of magnitude	Escherichia coli
S175A	mutation slows the rate of flavin reduction by 3 orders of magnitude. Reduction potential is about 40 mV lower than in wild-type	Escherichia coli
T178A	mutation slows the rate of flavin reduction by 3 orders of magnitude. Reduction potential is about 40 mV lower than in wild-type	Escherichia coli
T178S	reduction potential is about 25 mV lower than in wild-type	Escherichia coli
T178V	reduction potential is about 35 mV lower than in wild-type	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
(S)-dihydroorotate + a quinone = orotate + a quinol	the active base S175 and the hydrogen bonding network including residues T178 and F115 work together for efficient deprotonation of dihydroorotate	Escherichia coli	a

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)