Information on EC 1.3.1.91 - tRNA-dihydrouridine20 synthase [NAD(P)+]

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.3.1.91
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RECOMMENDED NAME
GeneOntology No.
tRNA-dihydrouridine20 synthase [NAD(P)+]
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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
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SYSTEMATIC NAME
IUBMB Comments
tRNA-5,6-dihydrouracil20:NAD(P)+ oxidoreductase
A flavoenzyme [3]. The enzyme specifically modifies uracil20 in tRNA.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
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LITERATURE
malfunction
physiological function
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formation of dihydrouridine in yeast cytoplasmic tRNAs is carried out by a family of four dihydrouridine synthases (Dus1p, Dus2p, Dus3p, and Dus4p), each acting at specific positions in tRNAs. Dus1p modifies U16 and U17, Dus2p modifies U20, Dus3p modifies U47, and Dus4p modifies U20a and U20b. These four proteins are responsible for all dihydrouridine modification of cytoplasmic tRNAs in yeast
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
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LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
uracil in pre-tRNALeu + NAD(P)H + H+
5,6-dihydrouracil in pre-tRNALeu + NAD(P)+
show the reaction diagram
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uracil in pre-tRNATyr + NAD(P)H + H+
5,6-dihydrouracil in pre-tRNATyr + NAD(P)+
show the reaction diagram
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uracil in tRNA + NAD(P)H + H+
5,6-dihydrouracil in tRNA + NAD(P)+
show the reaction diagram
uracil20 in tRNA + NAD(P)H + H+
5,6-dihydrouracil20 in tRNA + NAD(P)+
show the reaction diagram
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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
uracil in tRNA + NAD(P)H + H+
5,6-dihydrouracil in tRNA + NAD(P)+
show the reaction diagram
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uracil20 in tRNA + NAD(P)H + H+
5,6-dihydrouracil20 in tRNA + NAD(P)+
show the reaction diagram
P53720
the enzyme specifically modifies uracil20 in tRNA, e.g. tRNALeu(CAA) and tRNATyr
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COFACTOR
ORGANISM
UNIPROT
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LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
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LITERATURE
IMAGE
additional information
additional information
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kinetics of reductive and oxidative half-reactions
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
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LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
overexpression of hDUS2 in non–small cell lung carcinomas is identified by analysis of the gene-expression profiles
Manually annotated by BRENDA team
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
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x * 43000, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 43000, SDS-PAGE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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expression in Escherichia coli. There is a higher proportion of tRNAGly in Escherichia coli expressinf DUS2
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
upregulation of hDUS2 is a relatively common feature of pulmonary carcinogenesis
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ENGINEERING
ORGANISM
UNIPROT
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LITERATURE
C117A
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rate constant is 1600fold lower than the rate constant of the wild-type enzyme
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
upregulation of hDUS2 is a relatively common feature of pulmonary carcinogenesis. Selective suppression of hDUS2 enzyme activity and/or inhibition of formation of the hDUS2-tRNA synthetase complex could be a promising therapeutic strategy for treatment of many lung cancers. Significant association between higher levels of hDUS2 in tumors and poorer prognosis of lung cancer patients
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LINKS TO OTHER DATABASES (specific for EC-Number 1.3.1.91)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)