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Literature summary extracted from

  • Pickl, A.; Johnsen, U.; Schoenheit, P.
    Fructose degradation in the haloarchaeon Haloferax volcanii involves a bacterial type phosphoenolpyruvate-dependent phosphotransferase system, fructose-1-phosphate kinase, and class II fructose-1,6-bisphosphate aldolase (2012), J. Bacteriol., 194, 3088-3097.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.1.2.13 cysteine highest activity at 1 mM cysteine Haloferax volcanii

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.2.13 EDTA 2 mM, complete inhibition of activity, which could be reversed by the addition of Mn2+ (3 mM) Haloferax volcanii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.56 0.08
-
 ATP in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C Haloferax volcanii
2.7.1.56 0.31
-
 D-Fructose 1-phosphate in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C Haloferax volcanii
2.7.1.56 1.12
-
 D-fructose 6-phosphate in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C Haloferax volcanii
4.1.2.13 0.24
-
 D-fructose 1,6-bisphosphate pH 7.5, 42°C Haloferax volcanii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.56 K+ the enzyme shows the highest activity at about 0.5M KCl Haloferax volcanii
4.1.2.13 FeSO4 the enzyme requires divalent cation for activity. The highest activity is obtained with MnCl2 (100%, 50 U/mg), which can be partially replaced by FeSO4 (40% residual activity) Haloferax volcanii
4.1.2.13 KCl highest activity at 1 mM KCl Haloferax volcanii
4.1.2.13 MnCl2 the enzyme requires divalent cation for activity. The highest activity is obtained with MnCl2 (100%, 50 U/mg), which can be partially replaced by FeSO4 (40% residual activity) Haloferax volcanii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.1.56 38000
-
 2 * 38000, SDS-PAGE Haloferax volcanii
2.7.1.56 70000
-
 gel filtration Haloferax volcanii
4.1.2.13 42000
-
 2 * 42000, SDS-PAGE Haloferax volcanii
4.1.2.13 80000
-
-
 Haloferax volcanii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.56 ATP + D-fructose 1-phosphate Haloferax volcanii physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate ADP + D-fructose 1,6-bisphosphate
-
 ?
2.7.1.56 ATP + D-fructose 1-phosphate Haloferax volcanii H1209 physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate ADP + D-fructose 1,6-bisphosphate
-
 ?
2.7.1.56 ATP + D-fructose 6-phosphate Haloferax volcanii physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate ADP + ?
-
 ?
2.7.1.56 ATP + D-fructose 6-phosphate Haloferax volcanii H1209 physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate ADP + ?
-
 ?
4.1.2.13 D-fructose 1,6-bisphosphate Haloferax volcanii the enzyme has an anabolic function catalyzing fructose-1,6-bisphosphate formation in the course of gluconeogenesis glycerone phosphate + D-glyceraldehyde 3-phosphate
-
 r
4.1.2.13 D-fructose 1,6-bisphosphate Haloferax volcanii DSM 3757 the enzyme has an anabolic function catalyzing fructose-1,6-bisphosphate formation in the course of gluconeogenesis glycerone phosphate + D-glyceraldehyde 3-phosphate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.56 Haloferax volcanii D4GYE6
-
-
2.7.1.56 Haloferax volcanii H1209 D4GYE6
-
-
2.7.3.9 Haloferax volcanii
-
-
-
2.7.3.9 Haloferax volcanii H26
-
-
-
4.1.2.13 Haloferax volcanii D4GYE0
-
-
4.1.2.13 Haloferax volcanii DSM 3757 D4GYE0
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.56 Ni-NTA column chromatography and Superdex 200 gel filtration Haloferax volcanii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.56 ATP + D-fructose 1-phosphate physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate Haloferax volcanii ADP + D-fructose 1,6-bisphosphate
-
 ?
2.7.1.56 ATP + D-fructose 1-phosphate physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate Haloferax volcanii H1209 ADP + D-fructose 1,6-bisphosphate
-
 ?
2.7.1.56 ATP + D-fructose 6-phosphate physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate Haloferax volcanii ADP + ?
-
 ?
2.7.1.56 ATP + D-fructose 6-phosphate physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate Haloferax volcanii H1209 ADP + ?
-
 ?
4.1.2.13 D-fructose 1,6-bisphosphate
-
 Haloferax volcanii glycerone phosphate + D-glyceraldehyde 3-phosphate
-
 r
4.1.2.13 D-fructose 1,6-bisphosphate the enzyme has an anabolic function catalyzing fructose-1,6-bisphosphate formation in the course of gluconeogenesis Haloferax volcanii glycerone phosphate + D-glyceraldehyde 3-phosphate
-
 r
4.1.2.13 D-fructose 1,6-bisphosphate
-
 Haloferax volcanii DSM 3757 glycerone phosphate + D-glyceraldehyde 3-phosphate
-
 r
4.1.2.13 D-fructose 1,6-bisphosphate the enzyme has an anabolic function catalyzing fructose-1,6-bisphosphate formation in the course of gluconeogenesis Haloferax volcanii DSM 3757 glycerone phosphate + D-glyceraldehyde 3-phosphate
-
 r

Subunits

EC Number Subunits Comment Organism
2.7.1.56 homodimer 2 * 38000, SDS-PAGE Haloferax volcanii
4.1.2.13 homodimer 2 * 42000, SDS-PAGE Haloferax volcanii

Synonyms

EC Number Synonyms Comment Organism
2.7.1.56 1-PFK
-
 Haloferax volcanii
2.7.1.56 fructose-1-phosphate kinase
-
 Haloferax volcanii
2.7.1.56 pfkB
-
 Haloferax volcanii
2.7.3.9 phosphotransferase system component enzyme I
-
 Haloferax volcanii
2.7.3.9 protein kinase enzyme I
-
 Haloferax volcanii
2.7.3.9 ptsI
-
 Haloferax volcanii
4.1.2.13 FBA
-
 Haloferax volcanii
4.1.2.13 fructose-1,6-bisphosphate aldolase
-
 Haloferax volcanii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.2.13 42
-
 assay at Haloferax volcanii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.56 7.5 9
-
 Haloferax volcanii
4.1.2.13 7.5
-
-
 Haloferax volcanii

Expression

EC Number Organism Comment Expression
2.7.1.56 Haloferax volcanii enzyme expression is specifically upregulated in fructose-grown cells up
2.7.1.69 Haloferax volcanii during growth on fructose, the gene cluster HVO_1495 to HVO_1499, encoding homologues of the five bacterial phosphotransferase system (PTS) components enzyme IIB (EIIB), enzyme I (EI), histidine protein (HPr), EIIA, and EIIC, is highly upregulated as a cotranscript up
2.7.3.9 Haloferax volcanii during growth on fructose the gene cluster HVO1495 to HVO1499, encoding homologs of the five bacterial phosphotransferase system components inclusive enzyme I is highly upregulated as a cotranscript up
4.1.2.13 Haloferax volcanii highly increased transcript levels of fba in fructose-grown cells compared to those in glucose-grown cells, indicating fructosespecific upregulation up

General Information

EC Number General Information Comment Organism
2.7.1.56 metabolism the enzyme is involved in fructose catabolism Haloferax volcanii
2.7.1.69 additional information during growth on fructose, the gene cluster HVO_1495 to HVO_1499, encoding homologues of the five bacterial phosphotransferase system (PTS) components enzyme IIB (EIIB), enzyme I (EI), histidine protein (HPr), EIIA, and EIIC, is highly upregulated as a cotranscript. Functional involvement of this putative PTS and of 1-PFK and FBA in fructose degradation, modeling, overview Haloferax volcanii
2.7.3.9 metabolism the enzyme I gene is involved in fructose metabolism Haloferax volcanii
4.1.2.13 malfunction deletion mutant loses the ability to grow on fructose, but growth on glucose is not inhibited and is even slightly stimulated Haloferax volcanii
4.1.2.13 physiological function the enzyme has an anabolic function catalyzing fructose-1,6-bisphosphate formation in the course of gluconeogenesis. The enzyme is essential for growth on fructose Haloferax volcanii

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.7.1.56 34
-
 D-fructose 6-phosphate in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C Haloferax volcanii
2.7.1.56 1200
-
 D-Fructose 1-phosphate in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C Haloferax volcanii