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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)

Application

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

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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
-
when temperature-stable forms of of the enzyme (PGD1 and PGD2) are expressed in maize endosperm plastids, this increases enzyme activity and mitigates the reduction in grain yield that occurred in control plants exposed to elevated temperatures at night. This genetic improvement could be included as part of integrated approaches to mitigate yield losses due to climate change
biotechnology
-
immobilization of 6PDGH on ASMNPs can be an effective way for its biotechnological and biosensor applications
medicine
pharmacology
the enzyme is a target for inhibitor development for usage as drugs against African Trypanosomiasis
synthesis
additional information
the enzyme can be used for power production in biobatteries. Mutant N32E/R33I/T34I versus the wild-type 6PGDH are evaluated electrochemically in an anodic reaction system containing two enzymes: 6PGDH and diaphorase, a coenzyme (NADP+ or NAD+), an electron mediator AQDS, and a 6-phosphogluconate substrate. Cyclic voltammetry results clearly show that both enzymes produce significant oxidation current peaks at -0.3 V versus Ag/AgCl. The mutant N32E/R33I/T34I exhibits a current density 25% higher than that generated by the wild-type