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Information on EC 1.3.1.91 - tRNA-dihydrouridine20 synthase [NAD(P)+] and Organism(s) Homo sapiens and UniProt Accession Q9NX74

for references in articles please use BRENDA:EC1.3.1.91
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IUBMB Comments
A flavoenzyme . The enzyme specifically modifies uracil20 in tRNA.
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q9NX74
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
5,6-dihydrouracil20 in tRNA
+
=
uracil20 in tRNA
+
+
Synonyms
hdus2, dihydrouridine synthase, hsdus2, dihydrouridine synthase 2, dus 2, dus2p, ecodusc, trna-dihydrouridine synthases, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dihydrouridine synthase
-
dihydrouridine synthase 2
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5,6-dihydrouracil20 in tRNA + NAD(P)+ = uracil20 in tRNA + NAD(P)H + H+
show the reaction diagram
dsRNA binding mode, modeling
SYSTEMATIC NAME
IUBMB Comments
tRNA-5,6-dihydrouracil20:NAD(P)+ oxidoreductase
A flavoenzyme [3]. The enzyme specifically modifies uracil20 in tRNA.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
uracil20 in tRNA + NAD(P)H + H+
5,6-dihydrouracil20 in tRNA + NAD(P)+
show the reaction diagram
uracil20 in tRNA + NADPH + H+
5,6-dihydrouracil20 in tRNA + NADP+
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
uracil20 in tRNA + NAD(P)H + H+
5,6-dihydrouracil20 in tRNA + NAD(P)+
show the reaction diagram
uracil20 in tRNA + NADPH + H+
5,6-dihydrouracil20 in tRNA + NADP+
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)H
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
isozyme Dus2 is upregulated
Manually annotated by BRENDA team
overexpression of hDUS2 in non–small cell lung carcinomas is identified by analysis of the gene-expression profiles
Manually annotated by BRENDA team
elevated hDus2 mRNA and protein levels
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DUS2L_HUMAN
493
0
55050
Swiss-Prot
other Location (Reliability: 5)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 55000, about, recombinant enzyme, SDS-PAGE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant enzyme E294K, vapor diffusion method, using 30% (w/v) PEG 2000 MME, 200 mM ammonium sulfate, and 50 mM sodium acetate pH 5.5. Mutant enzyme E294K/Q305K, vapor diffusion method, using 30% (w/v) PEG 2000 MME, 200 mM ammonium sulfate, and 50 mM sodium acetate pH 5.0. Mutant enzyme Q305K, vapor diffusion method, using 2.2 M ammonium sulfate
purified recombinant catalytic HsDus2dusD domain and tRNA binding domain HsDus2dsRBD (Glu347-Lys451), by hanging drop vapor diffusion method, at 19°C, X-ray diffraction structure determination and crystal structure analysis, PDB IDs 4WFS and 4WFT
purified recombinant hDus2 catalytic and tRNA-recognition domains (residues 1-340), sitting drop vapour diffusion method, 300 nl of 10 mg/ml protein in 20 mM Tris, pH 8.0, 100 mM NaCl, 5 mM imidazole, and 5 mM DTT, are mixed with 0. 54 ml of reservoir solution containing 0.1 M MES-malic acid-Tris, pH 4.0, and 25% w/v PEG 1500, 2 days, 19°C, X-ray diffraction structure determination and analysis by single-wavelength anomalous diffraction at 1.9 A resolution, automated molecular replacement with different search models, and modeling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E294K
the mutation increases the tRNA binding affinity and dihydrouridine activity compared to the wild type enzyme
E294K/Q305K
the mutation increases the tRNA binding affinity and dihydrouridine activity compared to the wild type enzyme
Q305K
the mutation increases the tRNA binding affinity and dihydrouridine activity compared to the wild type enzyme
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Superdex S200 gel filtration
recombinant His-tagged enzyme by nickel affinity chromatography and gel filtration
recombinant wild-type and selenomethionine-labeled hDus2 1-340 fragment, comprising the hDus2 catalytic and tRNA-recognition domains, from Escherichia coli strains BL21(DE3) and B834(DE3), respectively
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
recombinant expression of His-tagged enzyme, functional complementation of an enzyme-deficient Saccharomyces cerevisiae mutant by expression of enzyme domains HsDus2dusD and HsDus2dsRBD, both domains are required for activity
recombinant expression of wild-type and selenomethionine-labeled hDus2 1-340 fragment, comprising the hDus2 catalytic and tRNA-recognition domains, in Escherichia coli strains BL21(DE3) and B834(DE3), respectively
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
upregulation of hDUS2 is a relatively common feature of pulmonary carcinogenesis
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
the enzyme defined as an independent prognostic factor for the development of non-small cell lung cancer cells
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kato, T.; Daigo, Y.; Hayama, S.; Ishikawa, N.; Yamabuki, T.; Ito, T.; Miyamoto, M.; Kondo, S.; Nakamura, Y.
A novel human tRNA-dihydrouridine synthase involved in pulmonary carcinogenesis
Cancer Res.
65
5638-5646
2005
Homo sapiens (Q9NX74), Homo sapiens
Manually annotated by BRENDA team
Whelan, F.; Jenkins, H.T.; Griffiths, S.C.; Byrne, R.T.; Dodson, E.J.; Antson, A.A.
From bacterial to human dihydrouridine synthase automated structure determination
Acta Crystallogr. Sect. D
71
1564-1571
2015
Homo sapiens (Q9NX74), Homo sapiens
Manually annotated by BRENDA team
Bou-Nader, C.; Pecqueur, L.; Bregeon, D.; Kamah, A.; Guerineau, V.; Golinelli-Pimpaneau, B.; Guimaraes, B.G.; Fontecave, M.; Hamdane, D.
An extended dsRBD is required for post-transcriptional modification in human tRNAs
Nucleic Acids Res.
43
9446-9456
2015
Homo sapiens (Q9NX74), Homo sapiens
Manually annotated by BRENDA team
Bou-Nader, C.; Bregeon, D.; Pecqueur, L.; Fontecave, M.; Hamdane, D.
Electrostatic potential in the tRNA binding evolution of dihydrouridine synthases
Biochemistry
57
5407-5414
2018
Saccharomyces cerevisiae, Homo sapiens (Q9NX74)
Manually annotated by BRENDA team