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1.1.98.3: decaprenylphospho-beta-D-ribofuranose 2-dehydrogenase

This is an abbreviated version!
For detailed information about decaprenylphospho-beta-D-ribofuranose 2-dehydrogenase, go to the full flat file.

Word Map on EC 1.1.98.3

Reaction

trans,octacis-decaprenylphospho-beta-D-ribofuranose
+
FAD
=
trans,octacis-decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose
+
FADH2

Synonyms

decaprenylphospho-beta-D-ribofuranose 2-oxidase, decaprenylphosphoryl-beta-D-ribofuranose 2'-epimerase, decaprenylphosphoryl-beta-D-ribofuranose 2'-oxidase, decaprenylphosphoryl-beta-D-ribose 2'-epimerase, decaprenylphosphoryl-beta-D-ribose 2'-oxidase, decaprenylphosphoryl-beta-D-ribose 2-epimerase, decaprenylphosphoryl-beta-D-ribose oxidase, decaprenylphosphoryl-beta-D-ribose-2'-epimerase, decaprenylphosphoryl-D-ribose oxidase, DprE1, DprE2, MSMEG_6382, Rv3790

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.98 With other, known, physiological acceptors
                1.1.98.3 decaprenylphospho-beta-D-ribofuranose 2-dehydrogenase

Crystallization

Crystallization on EC 1.1.98.3 - decaprenylphospho-beta-D-ribofuranose 2-dehydrogenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals are grown from a mixture of ethyl acetate/heptane by slow evaporation
different crystal forms of ligand-free enzyme reveal considerable levels of structural flexibility of two surface loops that seem to govern accessibility of the active site. Structures of complexes with the benzothiazinone-derived nitroso derivative 3-nitroso-N-[(1R)-1-phenylethyl]-5-(trifluoromethyl)benzamide reveal that inhibitor binding includes a covalent link to conserved Cys387, and reveal a trifluoromethyl group as a second key determinant of interaction with the enzyme. A noncovalent complex is formed between the enzyme and 3-nitro-N-[(1R)-1-phenylethyl]-5-(trifluoromethyl)benzamide, which is structurally identical to 3-nitroso-N-[(1R)-1-phenylethyl]-5-(trifluoromethyl)benzamide except for an inert nitro group replacing the reactive nitroso group. Binding of benzothiazinone-class inhibitors to the enzyme is not strictly dependent on formation of the covalent link to Cys387
sitting drop vapor diffusion method, using 15-20% (v/v) isopropanol, 0.2 M sodium citrate pH 6.8, and 0.5% (w/v) N,N-dimethyldodecylamine-N-oxide