1.3.1.91: tRNA-dihydrouridine20 synthase [NAD(P)+]
This is an abbreviated version!
For detailed information about tRNA-dihydrouridine20 synthase [NAD(P)+], go to the full flat file.
Word Map on EC 1.3.1.91
-
1.3.1.91
-
dsrnas
-
thermus
-
d-loops
-
thermophilus
-
flavin
-
carcinogenesis
-
dsrbd
-
archaea
-
trnaphe
-
elbow
-
l-shaped
-
medicine
-
synthase-2
-
diagnostics
- 1.3.1.91
- dsrnas
-
thermus
-
d-loops
- thermophilus
- flavin
- carcinogenesis
-
dsrbd
- archaea
- trnaphe
-
elbow
-
l-shaped
- medicine
- synthase-2
- diagnostics
Reaction
Synonyms
dihydrouridine synthase, dihydrouridine synthase 2, dihydrouridine synthase C, Dus, DUS 2, DUS2, Dus2p, DusA, DusB, DusC, EcoDusC, hDUS2, HsDus2, SMM1, tRNA-dihydrouridine synthase 2, tRNA-dihydrouridine synthases
ECTree
Advanced search results
General Information
General Information on EC 1.3.1.91 - tRNA-dihydrouridine20 synthase [NAD(P)+]
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
evolution
malfunction
physiological function
additional information
comparison of structure and substrate recognition mechanisms of Thermus thermophilus Dus and Escherichia coli Dus enzymes, overview
evolution
In humans, there are four Dus enzymes. The hDus2 subfamily is proposed to specifically modify U20. The overall fold of the human Dus2 is similar to that of bacterial enzymes, but has a larger recognition domain and a unique three-stranded antiparallel beta-sheet insertion into the catalytic domain that packs next to the recognition domain, contributing to domain-domain interactions
evolution
while in Dus enzymes from bacteria, plants and fungi, tRNA binding is essentially achieved by the alpha-helical domain, in HsDus2 this function is carried out by the dsRNA binding domain (dsRBD)
a small interfering RNA against hDUS2 transfected into NSCLC cells suppresses expression of the gene, reduces the amount of dihydrouridine in tRNA molecules, and suppresses growth
malfunction
yeast extract from a dus1-DELTA strain is completely defective in modification of yeast pre-tRNAPhe
malfunction
increased expression of human dihydrouridine synthase 2 (hDus2) is linked to pulmonary carcinogenesis, while its knockdown decreases cancer cell line viability
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
physiological function
dihydrouridine is produced by dihydrouridine synthase (Dus) by enzymatic reduction of the C5-C6 bond in uridine
physiological function
in tRNA, dihydrouridine is a conserved modified base generated by the post-transcriptional reduction of uridine. Formation of dihydrouridine 20, located in the D-loop, is catalyzed by dihydrouridine synthase 2 (Dus2). Full-length HsDus2 but not its Dus domain complements a DELTAdus2 yeast strain by catalyzing formation of dihydrouridine20
residues that participate in binding to the adapter molecule in EcoDusC are Asn95, Lys139, Arg141, His168 and Arg170. The catalytic cysteine residue is Cys98
additional information
-
residues that participate in binding to the adapter molecule in EcoDusC are Asn95, Lys139, Arg141, His168 and Arg170. The catalytic cysteine residue is Cys98
additional information
the catalytic domain binds selectively NADPH but cannot reduce uridine in the absence of the dsRNA binding domain (dsRBD). HsDus2 catalytic domain structure, overview
additional information
-
the catalytic domain binds selectively NADPH but cannot reduce uridine in the absence of the dsRNA binding domain (dsRBD). HsDus2 catalytic domain structure, overview
additional information
tRNA binding and the active site structure, overview