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Literature summary extracted from

  • Chen, H.; Zhu, Z.; Huang, R.; Zhang, Y.P.
    Coenzyme engineering of a hyperthermophilic 6-phosphogluconate dehydrogenase from NADP(+) to NAD(+) with its application to biobatteries (2016), Sci. Rep., 6, 36311 .
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
1.1.1.44 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 Thermotoga maritima

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.44 gene 6pgdh, recombinant overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Thermotoga maritima

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.44 additional information construction and evaluation of enzyme mutants with increased activity for NAD* compared to the wild-type enzyme Thermotoga maritima
1.1.1.44 N32D site-directed mutagenesis, mutant N32D has a 460times higher Km value for NADP+ and a slightly decreased Km value for NAD+, but no significant difference of kcat for NADP+, compared to the wild-type enzyme Thermotoga maritima
1.1.1.44 N32D/R33I/T34I site-directed mutagenesis, the triple mutant exhibits a far higher Km value for NADP+ and a slightly decreased Km value for NAD+, but no significant difference of kcat for NADP+, compared to the wild-type enzyme Thermotoga maritima
1.1.1.44 N32D/R33L/T34S site-directed mutagenesis, the triple mutant has a increased Km value for NADP+ and NAD+, but no significant difference of kcat for NADP+, compared to the wild-type enzyme Thermotoga maritima
1.1.1.44 N32E/R33I/T34I site-directed mutagenesis, the mutant shows almost 2fold declined Km and a 2fold increased kcat for NAD+ compared to wild-type, the catalytic efficiency kcat/Km towards NADP+ decreases, while the catalytic efficiency towards NAD+ increases Thermotoga maritima

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.44 6-phospho-D-gluconate + NADP+ Thermotoga maritima
-
 D-ribulose 5-phosphate + CO2 + NADPH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.44 Thermotoga maritima Q9WYR9
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.44 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to homogeneity Thermotoga maritima

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.44 6-phospho-D-gluconate + NAD+
-
 Thermotoga maritima D-ribulose 5-phosphate + CO2 + NADH + H+
-
 ?
1.1.1.44 6-phospho-D-gluconate + NADP+
-
 Thermotoga maritima D-ribulose 5-phosphate + CO2 + NADPH + H+
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.44 NAD+ active with enzyme mutants, not with the wild-type enzyme Thermotoga maritima
1.1.1.44 NADP+ specific for, natural coenzyme is NADP+ Thermotoga maritima