1.1.1.153: sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming)

This is an abbreviated version, for detailed information about sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming), go to the full flat file.

Reaction

L-erythro-7,8-dihydrobiopterin
+
NADP+
=
sepiapterin
+
NADPH
+
H+

Synonyms

AKR1B1, reductase, sepiapterin, sepiapterin reductase, SPR, SR

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.153 sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming)

Engineering

Engineering on EC 1.1.1.153 - sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming)

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F99A
-
the mutant shows 3.9fold higher Km and lower Vmax (8.95%) than the wild type enzyme
W196A
-
the mutant shows 8.7fold higher Km and lower Vmax (5.64%) than the wild type enzyme
D257H
-
mutant shows completely inhibited sepiapterin reduction. Mutation has only minimal effects on redox cycling
DELTA257-261
-
deletion of the C-terminal 5 amino acids almost completely eliminates enzyme activity. For redox cycling, the catalytic efficacy decreases to less than 1% of the wild type enzyme
G14S
-
mutations in Gly14 and Gly18 in the NADPH binding motif of sepiapterin reductase results in almost complete loss of the ability to reduce sepiapterin, and a 65-75% decrease in redox cycling. For both of these mutations, the catalytic efficiencies for redox cycling decreases to 0.2% of wild type sepiapterin reductase
G18D
-
mutations in Gly14 and Gly18 in the NADPH binding motif of sepiapterin reductase results in almost complete loss of the ability to reduce sepiapterin, and a 65-75% decrease in redox cycling. For both of these mutations, the catalytic efficiencies for redox cycling decreases to 0.2% of wild type sepiapterin reductase
K174L
-
catalytic efficiencies (Kcat/Km) for sepiapterin reduction of S157A mutant and K174L mutant decreases to 1.8% and 0.8% of wild type sepiapterin reductase, respectively, and for redox cycling to 6.8% and 1.4%, respectively
K251X
-
naturally occurring mutation in gene SPR, exon 3, causing enzyme deficiency
M205G
-
mutation leads to marked reductions in the activities of both sepiapterin reduction and redox cycling. The catalytic efficiency of N99A and M205G for sepiapterin reduction decreases to approximately 1% and 5%, respectively, and for redox cycling, 5% and 25%, respectively, when compared to the wild type enzyme
N99A
-
mutation leads to marked reductions in the activities of both sepiapterin reduction and redox cycling. The catalytic efficiency of N99A and M205G for sepiapterin reduction decreases to approximately 1% and 5%, respectively, and for redox cycling, 5% and 25%, respectively, when compared to the wild type enzyme
P163L
-
naturally occurring mutation in gene SPR, exon 2, causing enzyme deficiency
Q119X
-
naturally occurring mutation in gene SPR, exon 2, causing enzyme deficiency
R150fs
-
naturally occurring mutation in gene SPR, exon 2, causing enzyme deficiency
R150G
-
naturally occurring mutation in gene SPR, exon 2, causing enzyme deficiency
R42G
-
mutation leads to a 90% reduction in sepiapterin reduction activity and a 50% reduction in redox cycling activity. The catalytic efficiencies for this mutant decreases to 2% and 7% of wild type sepiapterin reductase for sepiapterin reduction and redox cycling, respectively
S157A
-
catalytic efficiencies (Kcat/Km) for sepiapterin reduction of S157A mutant and K174L mutant decreases to 1.8% and 0.8% of wild type sepiapterin reductase, respectively, and for redox cycling to 6.8% and 1.4%, respectively
Y259A
-
mutation of Tyr259, a unique potential phosphorylation site in the C-terminal substrate transfer motif, has no major effects on sepiapterin reduction and redox cycling activity
K175I
-
decreased activity against a pteridine substrate and exogenous carbonyl compound
S158D
-
decreased activity against a pteridine substrate and exogenous carbonyl compound
S158D/Y171V
-
double-point mutant does not show any activity towards any substrate
Y171V
-
decreased activity against a pteridine substrate and exogenous carbonyl compound
additional information