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
Synonyms
More, PsSAR, reductase, salutaridine 7-, SalR, salutaridine 7-reductase, salutaridine reductase
ECTree
Advanced search results
Engineering
Engineering on EC 1.1.1.248 - salutaridine reductase (NADPH)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
F104A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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
N152A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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
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
D107A
the mutant shows altered kinetics compared to the wild-type enzyme
F104A
the mutant shows altered kinetics compared to the wild-type enzyme
shows no substrate inhibition accompanied by a weak affinity for productive salutaridine binding, kcat is almost 2fold higher compared with the wild-type
F104A/I275A
substitution of Phe104 in the substrate-binding pocket, and Ile275 under the flap domain, the mutant shows altered kinetics compared to the wild-type enzyme
increase in Km, shows an increase of velocity by a factor of 2.3
I275A
the mutant shows altered kinetics compared to the wild-type enzyme
moderate effects on substrate affinity, exhibits a turnover number similar to that of the wild-type
K186V
the mutant shows altered kinetics compared to the wild-type enzyme
L185A
the mutant shows altered kinetics compared to the wild-type enzyme
L266A
the mutant shows altered kinetics compared to the wild-type enzyme
M271A
the mutant shows altered kinetics compared to the wild-type enzyme
N272A
the mutant shows altered kinetics compared to the wild-type enzyme
moderate effects on substrate affinity, increase in kcat by 50%
S181A
the mutant shows altered kinetics compared to the wild-type enzyme
T182A
the mutant shows altered kinetics compared to the wild-type enzyme
moderate effects on substrate affinity, increase in kcat by 90%
V106A
the mutant shows altered kinetics compared to the wild-type enzyme