1.1.1.236: tropinone reductase II

This is an abbreviated version, for detailed information about tropinone reductase II, go to the full flat file.

Reaction

pseudotropine
+
NADP+
=
tropinone
+
NADPH
+
H+

Synonyms

DnTR2, More, pseudotropine forming tropinone reductase, pseudotropine-forming tropinone reductase, pseudotropinone forming tropinone reductase, TR-II, TR2, TRII, tropinone (psi-tropine-forming) reductase, tropinone reductase, tropinone reductase I, tropinone reductase II, tropinone reductase-II

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.236 tropinone reductase II

General Information

General Information on EC 1.1.1.236 - tropinone reductase II

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
DnTR2 amino acid sequence contains a conserved Rossmann folding structure, which includes a conserved NAD(P)H binding motif (Gly-X3-Gly-X-Gly) and catalytic residues Ser-Asn-Lys, suggesting that DnTR2 is a member of the SDR superfamily
malfunction
DnTR2 residue Tyr201 is located at the opposite side of Arg110 in the inner substrate binding surface. These structural characters suggest that the disabled tropinone reduction activity of DnTR2 may be caused by the replacement of an uncharged amino acid at position 201
metabolism
physiological function
-
pseudotropine forming tropinone reductase (TRII) catalyzes a tropinone reduction competing with TRI, EC 1.1.1.206. StTRII is the main enzyme catalyzing the synthesis of pseudotropine from tropinone. StTRII plays a role in calystegine formation in potato sprouts
additional information
three-dimensional structure modeling of DnTR2, catalytic triad Ser-Asn-Lys, role of Tyr201 in substrate binding, structure comparisons, overview