Information on EC 4.2.1.70 - pseudouridylate synthase

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

EC NUMBER
COMMENTARY hide
4.2.1.70
-
RECOMMENDED NAME
GeneOntology No.
pseudouridylate synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
uracil + D-ribose 5-phosphate = pseudouridine 5'-phosphate + H2O
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
addition
elimination
-
of H2O, C-O bond cleavage
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
pseudouridine degradation
-
-
Pyrimidine metabolism
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-
SYSTEMATIC NAME
IUBMB Comments
uracil hydro-lyase (adding D-ribose 5-phosphate; pseudouridine-5'-phosphate-forming)
The reaction it readily reversible. While the enzymes from Tetrahymena pyriformis and Agrobacterium tumefaciens produce pseudouridine 5'-phosphate the enzyme from Escherichia coli functions as a pseudouridine-5'-phosphate glycosidase in vivo [5].
CAS REGISTRY NUMBER
COMMENTARY hide
9023-35-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
15955 (ATCC)
-
-
Manually annotated by BRENDA team
B6-6 (ATCC)
-
-
Manually annotated by BRENDA team
calf
-
-
Manually annotated by BRENDA team
var. italica
-
-
Manually annotated by BRENDA team
strain N1, pseudouridine synthase 1
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-
Manually annotated by BRENDA team
strain N1, pseudouridine synthase 1
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-
Manually annotated by BRENDA team
EB146 (leuK16)
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-
Manually annotated by BRENDA team
strain K12, TruD
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-
Manually annotated by BRENDA team
RsuA
-
-
Manually annotated by BRENDA team
rye grass
-
-
Manually annotated by BRENDA team
normal and with Agrobacterium tumefaciens transformed tissue
-
-
Manually annotated by BRENDA team
FL100 (ATCC)
-
-
Manually annotated by BRENDA team
spinach
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-thiouracil + D-ribose 5-phosphate
?
show the reaction diagram
-
-
-
-
-
isocytosine + D-ribose 5-phosphate
?
show the reaction diagram
-
-
-
-
-
pseudouridine 5' phosphate + H2O
?
show the reaction diagram
pseudouridine 5'-phosphate + H2O
uracil + D-ribose 5-phosphate
show the reaction diagram
tRNAIle
?
show the reaction diagram
-
-
-
-
-
tRNAVal
?
show the reaction diagram
-
-
-
-
-
uracil + D-ribose 5-phosphate
?
show the reaction diagram
-
biosynthetic pathway for pseudouridylic acid and pseudouridine
-
-
-
uracil + D-ribose 5-phosphate
pseudouridine 5'-phosphate + H2O
show the reaction diagram
uracil + deoxyribose 5-phosphate
deoxypseudouridine 5'-phosphate + H2O
show the reaction diagram
uracil + ribose 5-phosphate
5-ribosyluracil 5'-monophosphate + H2O
show the reaction diagram
-
r
-
-
uridinyl-tRNA
pseudouridinyl-tRNA
show the reaction diagram
additional information
?
-
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
pseudouridine 5' phosphate + H2O
?
show the reaction diagram
uracil + D-ribose 5-phosphate
?
show the reaction diagram
-
biosynthetic pathway for pseudouridylic acid and pseudouridine
-
-
-
uracil + D-ribose 5-phosphate
pseudouridine 5'-phosphate + H2O
show the reaction diagram
uridinyl-tRNA
pseudouridinyl-tRNA
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
high activity
Fe2+
high activity
Mg2+
-
required, broad maximal activity between 0.01 M and 0.05 M
Mn2+
high activity
Zn2+
-
essential for its native conformation and tRNA recognition
additional information
YeiN is dependent on divalent cations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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loss of activity within 5 min in the presence of 40 mM pseudouridine synthetase Pus1
1-(Tetrahydro-2-furanyl)-5-fluorouracil
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i.e. ftorafur
5-fluorouracil
-
-
iodoacetamide
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150 mM, in about 5 min all activity is lost
p-chloromercuribenzoate
thiol reagents
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-
tRNA
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wild-type RNA, 50% inhibition at a concentration of 0.005 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06
pseudouridine 5'-phosphate
pH 7.1, 30°C
0.024 - 0.84
ribose 5-phosphate
0.00074
tRNAIle
-
Pus1, intronless yeast tRNAIle
0.00042 - 0.0015
tRNAVal
0.071 - 0.67
Uracil
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00833
tRNAIle
Saccharomyces cerevisiae
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substrate from yeast, intronless, limiting
0.00667 - 0.00833
tRNAVal
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9.5
-
pH 7.0 about 50% of maximal activity, pH 9.5 about 80% of maximal activity
7.5 - 10
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pH 7.5 about 40% of maximal activity, pH 10 about 20% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 50
-
about 40% of maximal activity at 10°C and about 10% of maximal activity at 50°C
24 - 37
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about 50% of maximal activity at 25°C and about 30% of maximal activity at 37°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
-
pseudouridine synthase I, calculation from genomic sequence
46610
-
pus1p, calculation from sequence of cDNA
50000
-
2 * 50000, glycerol gradient sedimentation, tRNA induced dimerization
62100
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Pus1p, calculation from genomic sequence
63200
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1 * 63200, MALDI mass spectrometry
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 50000, glycerol gradient sedimentation, tRNA induced dimerization
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pseudouridine synthase RluC fragment
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TruB, two substrate-free forms, sitting-drop vapor-diffusion method
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
no activity at or below
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity retained after freezing and thawing
-
buffers containing 20% glycerol stabilize the enzyme
-
enzyme retains its activity during dialysis
-
mercaptoethanol is very effective in restoring the original activity of aged enzyme preparations
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for 1 year without loss of activity
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4°C, storage for 40 days, preincubation with 15 mM mercaptoethanol restores the original activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni2+ Sepharose column chromatography and Superdex 75 gel filtration
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partial
pseudouridylate synthetase I, partial
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recombinant His-tagged enzyme from Escherichia coli by affinity chromatography
recombinant TruB
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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expression as His-tagged enzyme in Escherichia coli
Pus1p, expression in Escherichia coli
RluC, expression in Escherichia coli
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Rv2793c gene, expression in Escherichia coli
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