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.

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

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Release 2026.1 (March 2026)