1.1.1.44: phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating)

This is an abbreviated version, for detailed information about phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating), go to the full flat file.

Reaction

6-phospho-D-gluconate
+
NADP+
=
D-ribulose 5-phosphate
+
CO2
+
NADPH
+
H+

Synonyms

6-GPD, 6-P-gluconate dehydrogenase, 6-Pgd, 6-PGDH, 6-PGDHase, 6-phospho-D-gluconate dehydrogenase, 6-phospho-D-gluconate-NADP+ oxidoreductase, decarboxylating, 6-phosphogluconate dehydrogenase, 6-phosphogluconate dehydrogenase (decarboxylating), 6-phosphogluconate dehydrogenase Gnd1, 6-phosphogluconate dehydrogenase, decarboxylating, 6-phosphogluconate-dehydrogenase, 6-phosphogluconate:NADP oxidoreductase, 6-phosphogluconic carboxylase, 6-phosphogluconic dehydrogenase, 6-phosphonogluconate dehydrogenase, 6PDH, 6PG DH, 6PGD, 6PGDH, 6PGDH/Gnd1, D-gluconate-6-phosphate dehydrogenase, gnd, GND1, GNTZII, LlPDH, Os6PGDH2, p6PGDH, peroxisomal 6-phosphogluconate dehydrogenase, PGD1, PGD2, PGD3, phosphogluconic acid dehydrogenase, YpjI

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.44 phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating)

Engineering

Engineering on EC 1.1.1.44 - phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating)

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A30C/R31I/T32K
the mutant exhibits a 118.5fold reversal of coenzyme selectivity from NADP+ to NAD+
A30D/R31I/T32I
the mutant exhibits a 4278fold reversal of coenzyme selectivity from NADP+ to NAD+
A30E/R31I/T32D
the mutant exhibits a 1293fold reversal of coenzyme selectivity from NADP+ to NAD+
R31I
the mutant exhibits a 6.9fold reversal of coenzyme selectivity from NADP+ to NAD+
R31I/T32G
the mutant exhibits a 22.1fold reversal of coenzyme selectivity from NADP+ to NAD+
R31T
the mutant exhibits a 3.5fold reversal of coenzyme selectivity from NADP+ to NAD+
E131A
-
the mutant shows a 2.3fold decrease in turnover number compared to the wild type enzyme
H186A
-
reduced activity compared to the wild type enzyme
H187A
-
reduced activity compared to the wild type enzyme
K260A
-
reduced activity compared to the wild type enzyme
M13F
-
mutant showing decrease in affinity for NADP+, but not NADPH
M13I
-
mutant showing decrease in affinity for NADP+, but not NADPH
R287A
-
reduced activity compared to the wild type enzyme
R446A
-
reduced activity compared to the wild type enzyme
S128A
-
reduced activity compared to the wild type enzyme
T262A
-
activity similar to the wild type enzyme
Y191A
-
reduced activity compared to the wild type enzyme
N32D
the mutant exhibits an 460times higher Km value on NADP+ and a slightly decreased Km value of 4.0 mM on NAD+ compared with the wild type enzyme
N32D/R33I/T34I
the mutant exhibits a far higher Km value of on NADP+ and a slightly decreased Km value on NAD+ compared with the wild type enzyme
N32D/R33L/T34S
the mutant has an increased Km value on NADP+ and NAD+ compared to the wild type enzyme
N32E/R33I/T34I
the mutant exhibits an about 6400fold reversal of the coenzyme selectivity from NADP+ to NAD+ compared to the wild type enzyme
V244D/C257R
site-directed mutagenesis, unaltered reaction kinetics and increased stability, due introduction of 2 salt bridges by the double-mutation, compared to the wild-type enzyme
additional information