Literature summary for 5.4.99.27 extracted from

Chan, C.M.; Huang, R.H.
Enzymatic characterization and mutational studies of TruD--the fifth family of pseudouridine synthases (2009), Arch. Biochem. Biophys., 489, 15-19.

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Protein Variants

Protein Variants	Comment	Organism
E31D	27% of wild-type activity	Escherichia coli
E31Q	no activity	Escherichia coli
E31Q/F131Y	no activity	Escherichia coli
F131Y	68% of wild-type activity	Escherichia coli
K79L	no activity	Escherichia coli
K79L	5% of wild-type activity	Escherichia coli
K79L/F131Y	no activity	Escherichia coli
K79L/N129K/F131Y	no activity	Escherichia coli
K79R	10% of wild-type activity	Escherichia coli
N129K	no activity	Escherichia coli
Q87E	29% of wild-type activity	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.00038	-	tRNA uridine13	-	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	Q57261	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
tRNA uridine13 = tRNA pseudouridine13	a strictly conserved glutamate near the active site in TruD is likely to act as a general base for the proton abstraction at C5 of the uridine base	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
tRNA uridine13	-	Escherichia coli	tRNA pseudouridine13	-	?

Synonyms

Synonyms	Comment	Organism
TruD	-	Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.00097	-	tRNA uridine13	-	Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
0.255	-	tRNA uridine13	-	Escherichia coli

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Release 2023.1 (January 2023)