Information on EC 5.4.99.28 - tRNA pseudouridine32 synthase

Word Map on EC 5.4.99.28
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
5.4.99.28
-
RECOMMENDED NAME
GeneOntology No.
tRNA pseudouridine32 synthase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
tRNA uridine32 = tRNA pseudouridine32
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
tRNA-uridine32 uracil mutase
The dual-specificity enzyme from Escherichia coli also catalyses the formation of pseudouridine746 in 23S rRNA [5]. cf. EC 5.4.99.29 (23S rRNA pseudouridine746 synthase).
CAS REGISTRY NUMBER
COMMENTARY hide
430429-15-5
-
61506-89-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
tRNA uridine32
tRNA pseudouridine32
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
tRNA uridine32
tRNA pseudouridine32
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000108 - 0.000455
tRNA uridine32
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.051 - 0.15
tRNA uridine32
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
112.1 - 937.5
tRNA uridine32
4180
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24432
-
x * 24432, calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 24432, calculated from sequence
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
vapor diffusion method. 2.05 A resolution structure of RluA bound to a substrate RNA comprising the anticodon stem loop of tRNAPhe reveals that enzyme binding induces a dramatic reorganization of the RNA
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
Tm-value for mutant enzyme P29L
38
-
Tm-value for mutant enzyme P29G is 37.9C
45
-
Tm-value for wild-type enzyme is 44.9C
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli; overexpression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C117A
-
kcat is 1.4fold lower than wild-type value, KM is 3.9fold higher than wild-type value
C117A/A128A
-
kcat is 1.3fold lower than wild-type value, KM is 1.5fold higher than wild-type value
C128A
-
kcat is 1.5fold higher than wild-type value, KM is 1.5fold higher than wild-type value
P29G
-
kcat-value is 1.6fold lower than wild-type value. KM-value is 2.9fold higher than wild-type value
P29L
-
kcat-value is 1.9fold lower than wild-type value. KM-value is 4.2fold higher than wild-type value
D112A
mutant does not pseudouridine32 in formation in cytoplasmic tRNAGly of the DELTArib2/pus8/DELTApus9 strain
additional information
Show AA Sequence (559 entries)
Please use the Sequence Search for a specific query.