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1.1.1.248: salutaridine reductase (NADPH)

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

Word Map on EC 1.1.1.248

Reaction

salutaridinol
+
NADP+
=
salutaridine
+
NADPH
+
H+

Synonyms

More, PsSAR, reductase, salutaridine 7-, SalR, salutaridine 7-reductase, salutaridine reductase

ECTree

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

Engineering

Engineering on EC 1.1.1.248 - salutaridine reductase (NADPH)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F104A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K240E
site-directed mutagenesis, inactive mutant
L266A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L266S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L266V
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
M271T
site-directed mutagenesis, inactive mutant
N152A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N272T
site-directed mutagenesis, inactive mutant
R44E
site-directed mutagenesis, the mutant enzyme shows altered cofactor specificity and utilizes also NADH in contrast to the wild-type enzyme
R48E
site-directed mutagenesis, the mutant enzyme shows altered cofactor specificity and utilizes also NADH in contrast to the wild-type enzyme
S180A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
V106A
site-directed mutagenesis, the mutant shows about 2fold increased activity compared to the wild-type enzyme
Y236F
site-directed mutagenesis, inactive mutant
D107A
F104A
F104A/I275A
I275A
I275V
the mutant shows altered kinetics compared to the wild-type enzyme
K186V
L185A
L185S
the mutant shows altered kinetics compared to the wild-type enzyme
L185V
the mutant shows altered kinetics compared to the wild-type enzyme
L266A
M271A
N272A
S181A
T182A
V106A
additional information
-
specific virus-induced gene silencing as a functional genomics tool to investigate the regulation of morphine biosynthesis via a systematic reduction in enzyme levels responsible for the final six steps in the pathway, overview. Reduced SalR protein levels correlate with lower morphine levels and a substantial increase in the accumulation of salutaridine