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
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1.3.1.91
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dsrnas
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thermus
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d-loops
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thermophilus
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flavin
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carcinogenesis
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dsrbd
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archaea
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trnaphe
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elbow
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l-shaped
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medicine
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synthase-2
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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
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Subunits
Subunits on EC 1.3.1.91 - tRNA-dihydrouridine20 synthase [NAD(P)+]
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monomer
additional information
the enzyme is composed of two domains: an N-terminal catalytic domain and a C-terminal tRNA-binding domain
additional information
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the enzyme is composed of two domains: an N-terminal catalytic domain and a C-terminal tRNA-binding domain
additional information
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
additional information
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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
additional information
three-dimensional structure analysis of wild-type and selenomethionine-labeled hDus2 catalytic and tRNA-recognition domains, and modeling, overview
additional information
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three-dimensional structure analysis of wild-type and selenomethionine-labeled hDus2 catalytic and tRNA-recognition domains, and modeling, overview