Identification and properties of an inducible and highly specific fructokinase from Streptomyces violaceoruber

Sabater, Bartolomé; Sebastián, Jesús; Asensio, Carlos

doi:10.1016/0005-2744(72)90137-4

Cited by 31 publications

(17 citation statements)

References 7 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Therefore, these organisms employ a single kinase to integrate two different hexoses into the same catabolic route. The enzyme purified from a crude extract of Streptomyces violaceoruber constitutes the only example until now of a bacterial fructokinase that is highly specific for D-fructose (39). Consequently, this work presents the first characterization at the molecular and biochemical level of a fructokinase from a gram-positive bacterium that is highly specific for D-fructose.…”

Section: Discussionmentioning

confidence: 99%

“…For example, prior to being catabolized by the bacterial cell, fructose needs to be phosphorylated either by specific fructose phosphoenolpyruvate (PEP)-phosphotransferase (PTS) enzymes or by a nucleotidedependent fructokinase (EC 2.7.1.4). The phosphotransferase system involves two classes of proteins, sugar-specific (EII) and general (EI and HPr) enzymes, which supply the cell with fructose-1-P (16,32,35), whereas fructokinases (Frk or ScrK; ATP:␤-D-fructose 6-phosphotransferases) catalyze the transfer of ␥-phosphate from ATP to an intracellular molecule of fructose, leading to fructose-6-P (F6P) (3,39,40,66). For the majority of bacteria, genes encoding fructokinases are either isolated on the chromosome (frk) (17,64,65,66) or members of a sucrose utilization gene cluster (scrK, sacK, or cscK) (3,5,6,28,38,53).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Bifidobacterium longum Requires a Fructokinase (Frk; ATP: d -Fructose 6-Phosphotransferase, EC 2.7.1.4) for Fructose Catabolism

et al. 2004

View full text Add to dashboard Cite

Although the ability of Bifidobacterium spp. to grow on fructose as a unique carbon source has been demonstrated, the enzyme(s) needed to incorporate fructose into a catabolic pathway has hitherto not been defined. This work demonstrates that intracellular fructose is metabolized via the fructose-6-P phosphoketolase pathway and suggests that a fructokinase (Frk; EC 2.7.1.4) is the enzyme that is necessary and sufficient for the assimilation of fructose into this catabolic route in Bifidobacterium longum. The B. longum A10C fructokinase-encoding gene (frk) was expressed in Escherichia coli from a pET28 vector with an attached N-terminal histidine tag. The expressed enzyme was purified by affinity chromatography on a Co 2؉ -based column, and the pH and temperature optima were determined. A biochemical analysis revealed that Frk displays the same affinity for fructose and ATP (K m fructose ‫؍‬ 0.739 ؎ 0.18 mM and K m ATP ‫؍‬ 0.756 ؎ 0.08 mM), is highly specific for D-fructose, and is inhibited by an excess of ATP (>12 mM). It was also found that frk is inducible by fructose and is subject to glucose-mediated repression. Consequently, this work presents the first characterization at the molecular and biochemical level of a fructokinase from a gram-positive bacterium that is highly specific for D-fructose.

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Bifidobacterium longum Requires a Fructokinase (Frk; ATP: d -Fructose 6-Phosphotransferase, EC 2.7.1.4) for Fructose Catabolism

et al. 2004

View full text Add to dashboard Cite

show abstract

“…However, in their strain glucose did not inhibit fructose uptake nor did inhibitors of respiration and glycolysis. It should be noted that the cells were also dealt with less speedily and it is perhaps as a consequence of this that they failed to see a second period of fructose uptake in glucose-grown cells even though they had shown previously (Sabater et al, 1972) that a fructose kinase was inducible.…”

Section: Galactose and Fructose Uptakementioning

confidence: 99%

Glucose Repression of Carbon Source Uptake and Metabolism in Streptomyces coelicolor A3(2) and its Perturbation in Mutants Resistant to 2-Deoxyglucose

Hodgson

1982

Microbiology

110

View full text Add to dashboard Cite

A newly devised method to obtain diffuse growth of Streptomyces coelicolor A3(2) in liquid minimal medium was used to study glucose repression. Although diauxic growth was not obtained, glucose repression of uptake of 14C-labelled carbon sources was demonstrated. Active, arabinose-induced, arabinose transport was repressed at the level of transcription by glucose. Of two glycerol-inducible glycerol transport systems, one was glucose-inhibited but not repressed (and operated by facilitated diffusion), whilst the other (an active transport system) was glucose-repressed. Active transport systems for galactose and fructose which did not require induction by their respective sugars were both inhibited by glucose. Galactose-and fructosemetabolizing enzymes were inducible by the respective sugars, but only in the absence of glucose. This was because glucose both inhibited galactose and fructose transport and repressed the metabolic enzymes concerned. Constitutive active glucose uptake was also demonstrated in arabinose-grown cells. Mutants that grew on arabinose or glycerol in the presence of 2-deoxyglucose were glucose-derepressed for both soluble carbon source utilization and extracellular agarose.*Three glucose-derepressed mutants were studied in detail. One of these could not utilize glucose (and probably lacks glucose kinase), whilst the other two could utilize glucose to differing degrees.

show abstract

“…Fructokinases (EC 2.7.1.4) have been found in various microorganisms, including Streptomyces violaceoruber, 1) Leuconostoc mesenteroides,2) Streptococcus faecalis, 3) Echinococcus granulosus, 4) and Tritrichomonas foetus. 5) These enzymes, however, has broad substrate specificities; i.e., glucose and/or mannose were phosphorylated by these enzymes.…”

mentioning

confidence: 99%

Isolation and Characterization of Fructokinase fromPseudomonassp. KN-21

Murao¹,

Nakatani²,

Kaneda³

1995

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

Identification and properties of an inducible and highly specific fructokinase from Streptomyces violaceoruber

Cited by 31 publications

References 7 publications

Bifidobacterium longum Requires a Fructokinase (Frk; ATP: d -Fructose 6-Phosphotransferase, EC 2.7.1.4) for Fructose Catabolism

Bifidobacterium longum Requires a Fructokinase (Frk; ATP: d -Fructose 6-Phosphotransferase, EC 2.7.1.4) for Fructose Catabolism

Glucose Repression of Carbon Source Uptake and Metabolism in Streptomyces coelicolor A3(2) and its Perturbation in Mutants Resistant to 2-Deoxyglucose

Isolation and Characterization of Fructokinase fromPseudomonassp. KN-21

Contact Info

Product

Resources

About