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1.1.1.343: phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating)

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

Word Map on EC 1.1.1.343

Reaction

6-phospho-D-gluconate
+
NAD+
=
D-ribulose 5-phosphate
 +
CO2
 +
NADH
 +
H+

Synonyms

6-PGDH, 6-phospho-gluconate dehydrogenase, 6-phosphogluconate dehydrogenase, 6PGDH, EC 1.1.1.44, GND1, gndA, GNDl, gntZ, Gox1705, HVO_1830, NAD+-dependent 6-P gluconate dehydrogenase, NAD+-dependent 6-P-gluconate dehydrogenase, NAD+-dependent 6-phosphogluconate dehydrogenase, NAD+-dependent 6-phosphogluconate dehydrogenase (decarboxylating), NAD-dependent 6-phosphogluconate dehydrogenase (decarboxylating), NAD-dependent PGDH, NAD-specific 6-PGDH, NAD-specific 6-phosphogluconate dehydrogenase, phosphogluconate dehydrogenase

ECTree

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

Engineering

Engineering on EC 1.1.1.343 - phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A30C/R31I/T32K
the catalytic efficiency of the mutant for NAD+ is increased by about 1.6fold compared to the wild type enzyme
A30D/R31I/T32I
the catalytic efficiency of the mutant for NAD+ is increased by 54fold, with a 4278fold reversal of coenzyme selectivity from NADP+ to NAD+
A30E/R31I/T32D
the catalytic efficiency of the mutant for NAD+ is increased by about 9.5fold compared to the wild type enzyme
R31I
the catalytic efficiency of the mutant for NAD+ is increased by about 4.7fold compared to the wild type enzyme
R31I/T32G
the catalytic efficiency of the mutant for NAD+ is increased by about 4fold compared to the wild type enzyme
R31T
the catalytic efficiency of the mutant for NAD+ is increased by about 1.7fold compared to the wild type enzyme
N32D
the mutant exhibits an about 1.3fold increase of catalytic efficiency with NAD+ as cofactor compared to the wild type enzyme
N32D/R33I/T34I
the mutant exhibits an about 1.5fold increase of catalytic efficiency with NAD+ as cofactor compared to the wild type enzyme
N32D/R33L/T34S
the mutant exhibits an about 0.6fold decrease of catalytic efficiency with NAD+ as cofactor compared to the wild type enzyme
N32E/R33I/T34I
the mutant exhibits an about 3.5fold increase of catalytic efficiency with NAD+ as cofactor, with about 64000fold reversal of the coenzyme selectivity from NADP+ to NAD+ compared to the wild type enzyme