Literature summary for 1.3.1.91 extracted from

Rider, L.W.; Ottosen, M.B.; Gattis, S.G.; Palfey, B.A.
Mechanism of dihydrouridine synthase 2 from yeast and the importance of modifications for efficient tRNA reduction (2009), J. Biol. Chem., 284, 10324-10333.

Search for more literature for 1.3.1.91

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli. There is a higher proportion of tRNAGly in Escherichia coli expressinf DUS2	Saccharomyces cerevisiae

Protein Variants

Protein Variants	Comment	Organism
C117A	rate constant is 1600fold lower than the rate constant of the wild-type enzyme	Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
43000	-	x * 43000, SDS-PAGE	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P53720	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
uracil in tRNA + NAD(P)H + H+	the enzyme is specific for the proR hydrogen of NADPH. Cys117 is very important for the reduction of tRNA	Saccharomyces cerevisiae	5,6-dihydrouracil in tRNA + NAD(P)+	-	r

Subunits

Subunits	Comment	Organism
?	x * 43000, SDS-PAGE	Saccharomyces cerevisiae

Synonyms

Synonyms	Comment	Organism
dihydrouridine synthase 2	-	Saccharomyces cerevisiae
DUS 2	-	Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetics of reductive and oxidative half-reactions	Saccharomyces cerevisiae

Cofactor

Cofactor	Comment	Organism	Structure
FAD	flavin-dependent enzyme	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)