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1.1.1.184: carbonyl reductase (NADPH)

This is an abbreviated version!
For detailed information about carbonyl reductase (NADPH), go to the full flat file.

Word Map on EC 1.1.1.184

Reaction

R-CHOH-R'
+
NADP+
=
R-CO-R'
+
NADPH
+
H+

Synonyms

(R) specific carbonyl reductase, (S)-specific carbonyl reductase, 15-hydroxyprostaglandin dehydrogenase [NADP+], 2,5-diketo-D-gluconic acid reductase, Adipocyte P27 protein, aldehyde reductase 1, aldehyde reductase I, aldo-keto reductase, ALR3, AP27, carbonyl reductase, carbonyl reductase (NADPH), carbonyl reductase 1, carbonyl reductase 3, carbonyl reductase S1, CBR, CBR 1, CBR 3, CBR1, CBR3, CHCR, CHCR1, CHCR2, CHCR3, CR, CR125, crc1, CSCR1, Gox0644, Gox1615, hCBR1, ketoreductase, KLCR1, KR, LCR, LOC415661, LOC610164, microsomal carbonyl reductase, More, NADP+-dependent ADH, NADPH-carbonyl reductase, NADPH-dependent carbonyl reductase, NADPH-dependent carbonyl reductase S1, NCCR, nonspecific NADPH-dependent carbonyl reductase, peroxisomal-type carbonyl reductase, PHCR, prostaglandin 9-ketoreductase, Prostaglandin-E2 9-reductase, PTCR, R-specific carbonyl reductase, reductase S1, reductase, carbonyl, RLCR, SCR, SCR9, SDR21C1, secondary-alcohol: NADP+-oxidoreductase, short-chain (S)-1-phenyl-1,2-ethanediol dehydrogenase, short-chain carbonyl reductase, sniffer, SRED, SSCR, SyS1, tetrameric carbonyl reductase, Tm1743, Tm_1743, xenobiotic carbonyl reductase, xenobiotic ketone reductase, YGL039w1, YGL039w2, YtbE, YueD

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.184 carbonyl reductase (NADPH)

Engineering

Engineering on EC 1.1.1.184 - carbonyl reductase (NADPH)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G135A
-
the mutant shows decreased activity with 3-bromoacetophenone as compared to the wild type enzyme
G180A
-
the mutant shows slightly increased activity with 3-bromoacetophenone as compared to the wild type enzyme
I190A
-
the mutant shows decreased activity with 3-bromoacetophenone as compared to the wild type enzyme
M186A
-
the mutant shows increased activity with 3-bromoacetophenone as compared to the wild type enzyme
Q187A
-
the mutant shows increased activity with 3-bromoacetophenone as compared to the wild type enzyme
V181A
-
the mutant shows strongly increased activity with 3-bromoacetophenone as compared to the wild type enzyme
W144A
-
the mutant shows slightly increased activity with 3-bromoacetophenone as compared to the wild type enzyme
Y141A
-
the mutant shows slightly increased activity with 3-bromoacetophenone as compared to the wild type enzyme
G135A
-
the mutant shows decreased activity with 3-bromoacetophenone as compared to the wild type enzyme
-
G180A
-
the mutant shows slightly increased activity with 3-bromoacetophenone as compared to the wild type enzyme
-
Q187A
-
the mutant shows increased activity with 3-bromoacetophenone as compared to the wild type enzyme
-
V181A
-
the mutant shows strongly increased activity with 3-bromoacetophenone as compared to the wild type enzyme
-
W144A
-
the mutant shows slightly increased activity with 3-bromoacetophenone as compared to the wild type enzyme
-
DELTA31
deletion of the N-terminal 31 residues, kinetic parameters KM and kcat are essentially the same as those of the wild-type. It forms a tetramer in solution, which is similar to the wild-type but is less stable. Melting temperature is 48°C, which is lower than that of the wild-type (52°C)
H68D
produces (R)-enantiomer with low optical purity and yield
H68D/P69D
produces (R)-enantiomer with low optical purity and yield
P69D
produces (R)-enantiomer with low optical purity and yield
S172A
S172T
S67D
produces (R)-enantiomer with low optical purity and yield
S67D/H68D
S67D/P69D
produces (R)-enantiomer with low optical purity and yield
V270D
Y187A
Y187F
D218V
J9P7P2
single nucleotide polymorphism
W230P
-
exhibits properties similar to the parent enzyme with regard to steroid specificities and kinetics toward substrates
Y172A
Km value for 9,10-phenanthrenequinone (model substrate) is 12.5 times higher than that for the wild-type enzyme
C227S
displays a similar kcat, but a 30fold higher Km value for S-nitrosoglutathione, and does not show substrate inhibition
D236A/K238P/D239K/S240A/I241T/R242K/T243S/V244P
mutations introduce activity towards S-nitrosoglutathione
P230W
P230W/D236A/K238P/D239K/S240A/I241T/R242K/T243S/V244P
mutations introduce activity towards S-nitrosoglutathione
Q142M/C143S/P230W/D236A/K238P/D239K/S240A/I241T/R242K/T243S/V244P/H270S
mutations introduce activity towards S-nitrosoglutathione
V244M
V88I
-
functional genetic polymorphism. Mutation results in CBR1 isoforms with different binding affinities for cofactor NADPH and inhibitor rutin as well as different maximal velocities for reaction with daunorubicin and prostaglandin E2
V166A
-
the mutant has increased activity with 2,2,2-trifluoroacetophenone compared to the wild type enzyme
W230P
exhibits properties similar to the parent enzyme with regard to steroid specificities and kinetics toward substrates
A89N/F154Y
-
Vmax and kcat values of the mutant enzyme are enhanced by 2.08 and 3.86fold, respectively, while the Km value decreases by 2.36fold compared to the wild type enzyme
Q245H
-
inversion of enantioselectivity from (R)- to (S)-configuration of reduced acetophenone product, with enhanced enantioselectivity
Q245L
-
inversion of enantioselectivity from (R)- to (S)-configuration of reduced acetophenone product, with enhanced enantioselectivity
Q245P
-
inversion of enantioselectivity from (R)- to (S)-configuration of reduced acetophenone product, with enhanced enantioselectivity
S41A/S42A/S43Q/W63I/Y64D/N65I/S66N
-
site-sirected mutagenesis, mutant S1M1 shows reduced activity and inverted cofactor specificity, using exclusively NADH, compared to the wild-type enzyme
S41A/S42A/S43R/W63I/Y64D/N65I/S66N
-
site-sirected mutagenesis, mutant S1M4 shows reduced activity and inverted cofactor specificity, using exclusively NADH, compared to the wild-type enzyme
S41A/S42A/S43Q/W63I/Y64D/N65I/S66N
-
site-sirected mutagenesis, mutant S1M1 shows reduced activity and inverted cofactor specificity, using exclusively NADH, compared to the wild-type enzyme
-
S41A/S42A/S43R/W63I/Y64D/N65I/S66N
-
site-sirected mutagenesis, mutant S1M4 shows reduced activity and inverted cofactor specificity, using exclusively NADH, compared to the wild-type enzyme
-
E142M
increase in reaction velocity
E142V
increase in reaction velocity
additional information