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.

Reaction

salutaridinol
+
NADP+
=
salutaridine
+
NADPH
+
H+

Synonyms

More, 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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ENGINEERING
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
F104A/I275A
I275V
the mutant shows altered kinetics compared to the wild-type enzyme
L185S
the mutant shows altered kinetics compared to the wild-type enzyme
L185V
the mutant shows altered kinetics compared to the wild-type enzyme
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