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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.

Word Map on EC 1.1.1.44

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 1, 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, 6PGDH1, 6PGDH2, 6PGDH3, At1G64190, At3g02360, At5g41670, D-gluconate-6-phosphate dehydrogenase, GCG1, gnd, GND1, Gnd1p, Gnd2p, GNTZII, LlPDH, Moth_1283, Os6PGDH1, Os6PGDH2, p6PGDH, peroxisomal 6-phosphogluconate dehydrogenase, Pgd, PGD1, PGD2, PGD3, phosphogluconic acid dehydrogenase, TM0438, YpjI, zwf3

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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A30C/R31I/T32K
A30D/R31I/T32I
A30E/R31I/T32D
R31I/T32G
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
W104L
N32D/R33I/T34I
N32D/R33L/T34S
N32E/R33I/T34I
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