Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.98.2 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
Search for more literature for 1.1.98.2

Cloned(Commentary)

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

Protein Variants

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

KM Value [mM]

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

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

Organism

Organism UniProt Comment Textmining
Rhodococcus jostii
-
-
-

Purification (Commentary)

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

Storage Stability

Storage Stability Organism
-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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 6-phosphate + oxidized coenzyme F420 4.8% activity compared to D-glucose 6-phosphate Rhodococcus jostii ? + reduced coenzyme F420
-
 ?
D-glucosamine 6-phosphate + oxidized coenzyme F420 2.8% activity compared to D-glucose 6-phosphate Rhodococcus jostii ?
-
 ?
D-glucose 6-phosphate + oxidized coenzyme F420
-
 Rhodococcus jostii 6-phospho-D-glucono-1,5-lactone + reduced coenzyme F420
-
 ?
D-glucose 6-phosphate + oxidized coenzyme F420 100% activity Rhodococcus jostii 6-phospho-D-glucono-1,5-lactone + reduced coenzyme F420
-
 ?
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
-
 ?
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

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8
-
 Rhodococcus jostii

Cofactor

Cofactor Comment Organism Structure
coenzyme F420 the enzyme is strictly dependent on F420 as coenzyme Rhodococcus jostii
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]

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