Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.3.1.91 extracted from

  • 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 (2015), Nucleic Acids Res., 43, 9446-9456 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.3.1.91

Cloned(Commentary)

Cloned (Comment) Organism
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 Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
uracil20 in tRNA + NAD(P)H + H+ Homo sapiens
-
 5,6-dihydrouracil20 in tRNA + NAD(P)+
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9NX74
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme by nickel affinity chromatography and gel filtration Homo sapiens

Reaction

Reaction Comment Organism Reaction ID
5,6-dihydrouracil20 in tRNA + NAD(P)+ = uracil20 in tRNA + NAD(P)H + H+ dsRNA binding mode, modeling Homo sapiens
a

Source Tissue

Source Tissue Comment Organism Textmining
lung cancer cell isozyme Dus2 is upregulated Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information no enzymatic activity ith tRNAAsp substrate Homo sapiens ?
-
 ?
uracil20 in tRNA + NAD(P)H + H+
-
 Homo sapiens 5,6-dihydrouracil20 in tRNA + NAD(P)+
-
 ?

Subunits

Subunits Comment Organism
? x * 55000, about, recombinant enzyme, SDS-PAGE Homo sapiens
More the N-terminal catalytic domain contains the flavin cofactor involved in the reduction of uridine. The second module is the conserved alpha-helical domain known as the tRNA binding domain in HsDus2 homologues. It is connected via a flexible linker to an unusual extended version of a dsRNA binding domain (dsRBD). The catalytic domain binds selectively NADPH but cannot reduce uridine in the absence of the dsRBD. Domain architecture of HsDus2, enzyme MALDI peptide mass finger printing analysis, overview Homo sapiens

Synonyms

Synonyms Comment Organism
dihydrouridine synthase 2
-
 Homo sapiens
DUS2
-
 Homo sapiens
HsDus2
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FMN the flavin cofactor is involved in the reduction of uridine, FMN binding site structure, overview. HsDus2dusD binds the FMN cofactor non-covalently at the C-terminal end of the beta-barrel, above beta-strands 1 and 8 Homo sapiens
NAD(P)H binds to the catalytic domain Homo sapiens

General Information

General Information Comment Organism
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) Homo sapiens
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 Homo sapiens
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 Homo sapiens