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Literature summary extracted from

  • Nguyen, Q.T.; Trinco, G.; Binda, C.; Mattevi, A.; Fraaije, M.W.
    Discovery and characterization of an F420-dependent glucose-6-phosphate dehydrogenase (Rh-FGD1) from Rhodococcus jostii RHA1 (2016), Appl. Microbiol. Biotechnol., 101, 2831-2842.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.98.2 expressed in Escherichia coli C41(DE3) cells Rhodococcus jostii

Protein Variants

EC Number Protein Variants Comment Organism
1.1.98.2 K197N the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme Rhodococcus jostii
1.1.98.2 K258N the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme Rhodococcus jostii
1.1.98.2 R282Q the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme Rhodococcus jostii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.98.2 0.31
-
 D-glucose 6-phosphate wild type enzyme, at pH 7.5 and 25°C Rhodococcus jostii
1.1.98.2 61
-
 D-glucose 6-phosphate mutant enzyme K258N, at pH 7.5 and 25°C Rhodococcus jostii
1.1.98.2 95
-
 D-glucose 6-phosphate mutant enzyme K197N, at pH 7.5 and 25°C Rhodococcus jostii
1.1.98.2 100
-
 D-glucose 6-phosphate Km above 100 mM, mutant enzyme R282Q, at pH 7.5 and 25°C Rhodococcus jostii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.98.2 D-glucose 6-phosphate + oxidized coenzyme F420 Rhodococcus jostii
-
 6-phospho-D-glucono-1,5-lactone + reduced coenzyme F420
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.98.2 Rhodococcus jostii
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.98.2 HisTrap column chromatography and Superdex 200 gel filtration Rhodococcus jostii

Storage Stability

EC Number Storage Stability Organism
1.1.98.2 -80°C, phosphate-based buffer with both NaCl and glycerol as additives, 1 year, less than 10% loss of activity Rhodococcus jostii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.98.2 D-fructose 6-phosphate + oxidized coenzyme F420 4.8% activity compared to D-glucose 6-phosphate Rhodococcus jostii ? + reduced coenzyme F420
-
 ?
1.1.98.2 D-glucosamine 6-phosphate + oxidized coenzyme F420 2.8% activity compared to D-glucose 6-phosphate Rhodococcus jostii ?
-
 ?
1.1.98.2 D-glucose 6-phosphate + oxidized coenzyme F420
-
 Rhodococcus jostii 6-phospho-D-glucono-1,5-lactone + reduced coenzyme F420
-
 ?
1.1.98.2 D-glucose 6-phosphate + oxidized coenzyme F420 100% activity Rhodococcus jostii 6-phospho-D-glucono-1,5-lactone + reduced coenzyme F420
-
 ?
1.1.98.2 D-mannose 6-phosphate + oxidized coenzyme F420 1.1% activity compared to D-glucose 6-phosphate Rhodococcus jostii 6-phospho-D-mannono-1,5-lactone + reduced coenzyme F420
-
 ?
1.1.98.2 additional information there is no detectable enzyme activity with alpha-Dglucose 1-phosphate and alpha-D-galactose 1-phosphate. The enzyme also accepts D-glucose as substrate, although with very low catalytic activity Rhodococcus jostii ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.98.2 F420-dependent glucose-6-phosphate dehydrogenase
-
 Rhodococcus jostii
1.1.98.2 FGD1
-
 Rhodococcus jostii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.98.2 35
-
 the enzyme exhibits melting temperature values above 35°C in most common buffer systems like HEPES, citrate, and phosphate Rhodococcus jostii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.98.2 0.047
-
 D-glucose 6-phosphate kcat above 0.047 s-1, mutant enzyme R282Q, at pH 7.5 and 25°C Rhodococcus jostii
1.1.98.2 0.57
-
 D-glucose 6-phosphate mutant enzyme K258N, at pH 7.5 and 25°C Rhodococcus jostii
1.1.98.2 3.8
-
 D-glucose 6-phosphate mutant enzyme K197N, at pH 7.5 and 25°C Rhodococcus jostii
1.1.98.2 17
-
 D-glucose 6-phosphate wild type enzyme, at pH 7.5 and 25°C Rhodococcus jostii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.98.2 7.5 8
-
 Rhodococcus jostii

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.98.2 coenzyme F420 the enzyme is strictly dependent on F420 as coenzyme Rhodococcus jostii
1.1.98.2 additional information the enzyme shows no significant activity when NAD+, NADP+, FAD, or FMN is used as alternative electron acceptor Rhodococcus jostii

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.98.2 0.00067
-
 D-glucose 6-phosphate mutant enzyme R282Q, at pH 7.5 and 25°C Rhodococcus jostii
1.1.98.2 0.0094
-
 D-glucose 6-phosphate mutant enzyme K258N, at pH 7.5 and 25°C Rhodococcus jostii
1.1.98.2 0.04
-
 D-glucose 6-phosphate mutant enzyme K197N, at pH 7.5 and 25°C Rhodococcus jostii
1.1.98.2 57
-
 D-glucose 6-phosphate wild type enzyme, at pH 7.5 and 25°C Rhodococcus jostii