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Literature summary for 1.1.1.184 extracted from

  • Sgraja, T.; Ulschmid, J.; Becker, K.; Schneuwly, S.; Klebe, G.; Reuter, K.; Heine, A.
    Structural insights into the neuroprotective-acting carbonyl reductase Sniffer of Drosophila melanogaster (2004), J. Mol. Biol., 342, 1613-1624.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
sniffer gene, expression as His-tagged enzyme from Escherichia coli strain M15 Drosophila melanogaster

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme, hanging drop vapour diffusion method, 0.001 ml water with 0.003 ml protein solution and 0.003 ml reservoir solution giving 18% w/v PEG 4000, 0.15 M sodium acetate, 75 mM Tris, pH 8.5, severeal days at 4°C, X-ray diffraction structure determination and analysis at 1.75 A resolution, molecular modeling Drosophila melanogaster

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme by nickel affinity chromatography Drosophila melanogaster

Reaction

Reaction Comment Organism Reaction ID
R-CHOH-R' + NADP+ = R-CO-R' + NADPH + H+ stereospecifc reaction mechanism Drosophila melanogaster

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrobenzaldehyde + NADPH artificial substrate Drosophila melanogaster 4-nitrobenzyl alcohol + NADP+
-
?
9,10-phenanthrenequinone + NADPH artificial substrate Drosophila melanogaster ? + NADP+
-
?
menadione + NADPH artificial substrate Drosophila melanogaster ? + NADP+
-
?
additional information stereospecific enzyme, substrate binding mechanism, active site cleft Drosophila melanogaster ?
-
?
pyridin-4-carboxyaldehyde + NADPH artificial substrate Drosophila melanogaster pyridin-4-ylmethanol + NADP+
-
?

Subunits

Subunits Comment Organism
dimer
-
Drosophila melanogaster

Synonyms

Synonyms Comment Organism
carbonyl reductase
-
Drosophila melanogaster
More enzyme belongs to the short-chain dehydrogenase/reductase family of enzymes Drosophila melanogaster

Cofactor

Cofactor Comment Organism Structure
NADPH beta-form, cofactor binding site structure Drosophila melanogaster