Literature summary extracted from
Kamitori, S.; Iguchi, A.; Ohtaki, A.; Yamada, M.; Kita, K.
X-ray structures of NADPH-dependent carbonyl reductase from Sporobolomyces salmonicolor provide insights into stereoselective reductions of carbonyl compounds (2005), J. Mol. Biol., 352, 551-558.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
1.1.1.184 |
expression of wild-type enzyme in Escherichia coli strain JM109, and of selenomethionine-CR in Escherichia coli strain B834 |
Sporidiobolus salmonicolor |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
1.1.1.184 |
purified recombinant free wild-type or selenomethionine-labeled enzyme and in complex with NADPH, vapour disffusion method, 30 mg/ml protein in 20 mM Tris-HCl, pH 8.0, against a reservoir solution containing 32% w/v PEG 2000 monomethyl ether, 100 mM ammonium sulfate, and 0.2 M sodium acetate, pH 5.0, with or without 4 mM NADPH, X-ray diffraction structure determination and analysis at 1.8 A and 1.6 A resolution, respectively, structure modeling |
Sporidiobolus salmonicolor |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.1.1.184 |
Sporidiobolus salmonicolor |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
1.1.1.184 |
recombinant wild-type enzyme from Escherichia coli strain JM109 and recombinant selenomethionine-CR from Escherichia coli strain B834, by ammonium sulfate fractionation, hydrophobic interaction and anion exchange chromatography, and gel filtration |
Sporidiobolus salmonicolor |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
1.1.1.184 |
R-CHOH-R' + NADP+ = R-CO-R' + NADPH + H+ |
stereoselective enzyme, reaction mechanism and substrate binding model, formation of a hydrophobic channel induced by NADPH binding |
Sporidiobolus salmonicolor |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.1.1.184 |
benzaldehyde + NADPH + H+ |
- |
Sporidiobolus salmonicolor |
benzylalcohol + NADP+ |
- |
? |
|
1.1.1.184 |
camphorquinone + NADPH + H+ |
- |
Sporidiobolus salmonicolor |
? |
- |
? |
|
1.1.1.184 |
ethyl 4-chloro-3-oxobutanoate + NAD(P)H + H+ |
stereospecific reaction, formation of a hydrophobic channel induced by NADPH binding, structure overview |
Sporidiobolus salmonicolor |
ethyl (S)-4-chloro-3-hydroxybutanoate + NAD(P)+ |
optically pure (S)-enantiomer |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
1.1.1.184 |
More |
SSCR has two domains, an NADPH-binding domain and a substrate-binding domain, structure overview |
Sporidiobolus salmonicolor |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.1.1.184 |
More |
the enzyme belongs to the short-chain dehydrogenases/reductases family |
Sporidiobolus salmonicolor |
1.1.1.184 |
SSCR |
- |
Sporidiobolus salmonicolor |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.1.1.184 |
NADPH |
dependent on, structure of the NADPH-binding domain and interaction between the enzyme and NADPH, overview |
Sporidiobolus salmonicolor |
|