D-glycero-beta-D-manno-heptose-7-phosphate kinase

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D-glycero-beta-D-manno-heptose-7-phosphate kinase
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EC no. 2.7.1.167
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D-glycero-beta-D-manno-heptose-7-phosphate kinase (EC 2.7.1.167, heptose 7-phosphate kinase, D-beta-D-heptose 7-phosphotransferase, D-beta-D-heptose-7-phosphate kinase, HldE1 heptokinase, glycero-manno-heptose 7-phosphate kinase, D-beta-D-heptose 7-phosphate kinase/D-beta-D-heptose 1-phosphate adenylyltransferase, hldE (gene), rfaE (gene)) is an enzyme with systematic name ATP:D-glycero-beta-D-manno-heptose 7-phosphate 1-phosphotransferase. [1] [2] [3] [4] [5] This enzyme catalyses the following chemical reaction

D-glycero-beta-D-manno-heptose 7-phosphate + ATP D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP

The bifunctional protein hldE includes D-glycero-beta-D-manno-heptose-7-phosphate kinase and D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase activity (cf. EC 2.7.7.70).

Related Research Articles

A heptose is a monosaccharide with seven carbon atoms.

<span class="mw-page-title-main">Phosphofructokinase 2</span> Class of enzymes

Phosphofructokinase-2 (6-phosphofructo-2-kinase, PFK-2) or fructose bisphosphatase-2 (FBPase-2), is an enzyme indirectly responsible for regulating the rates of glycolysis and gluconeogenesis in cells. It catalyzes formation and degradation of a significant allosteric regulator, fructose-2,6-bisphosphate (Fru-2,6-P2) from substrate fructose-6-phosphate. Fru-2,6-P2 contributes to the rate-determining step of glycolysis as it activates enzyme phosphofructokinase 1 in the glycolysis pathway, and inhibits fructose-1,6-bisphosphatase 1 in gluconeogenesis. Since Fru-2,6-P2 differentially regulates glycolysis and gluconeogenesis, it can act as a key signal to switch between the opposing pathways. Because PFK-2 produces Fru-2,6-P2 in response to hormonal signaling, metabolism can be more sensitively and efficiently controlled to align with the organism's glycolytic needs. This enzyme participates in fructose and mannose metabolism. The enzyme is important in the regulation of hepatic carbohydrate metabolism and is found in greatest quantities in the liver, kidney and heart. In mammals, several genes often encode different isoforms, each of which differs in its tissue distribution and enzymatic activity. The family described here bears a resemblance to the ATP-driven phospho-fructokinases, however, they share little sequence similarity, although a few residues seem key to their interaction with fructose 6-phosphate.

<span class="mw-page-title-main">Fructose-bisphosphate aldolase</span>

Fructose-bisphosphate aldolase, often just aldolase, is an enzyme catalyzing a reversible reaction that splits the aldol, fructose 1,6-bisphosphate, into the triose phosphates dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (G3P). Aldolase can also produce DHAP from other (3S,4R)-ketose 1-phosphates such as fructose 1-phosphate and sedoheptulose 1,7-bisphosphate. Gluconeogenesis and the Calvin cycle, which are anabolic pathways, use the reverse reaction. Glycolysis, a catabolic pathway, uses the forward reaction. Aldolase is divided into two classes by mechanism.

In enzymology, an ADP-L-glycero-D-manno-heptose 6-epimerase is an enzyme that catalyzes the chemical reaction

In enzymology, 1-phosphatidylinositol-4-phosphate 5-kinase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Butyrate kinase</span> Class of enzymes

In enzymology, a butyrate kinase is an enzyme that catalyzes the chemical reaction

In enzymology, a dephospho-CoA kinase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Hydroxyethylthiazole kinase</span>

In enzymology, a hydroxyethylthiazole kinase is an enzyme that catalyzes the chemical reaction

D-beta-D-heptose 7-phosphate kinase/D-beta-D-heptose 1-phosphate adenylyltransferase may refer to:

HldE may refer to:

RfaE (gene) may refer to:

RFAE may refer to:

D-glycero-alpha-D-manno-heptose-7-phosphate kinase is an enzyme with systematic name ATP:D-glycero-alpha-D-manno-heptose 7-phosphate 1-phosphotransferase. This enzyme catalyses the following chemical reaction

Isopentenyl phosphate kinase is an enzyme with systematic name ATP:isopentenyl phosphate phosphotransferase. This enzyme catalyses the following chemical reaction

D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase is an enzyme with systematic name ATP:D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase. This enzyme catalyses the following chemical reaction

D-glycero-alpha-D-manno-heptose 1-phosphate guanylyltransferase is an enzyme with systematic name GTP:D-glycero-alpha-D-manno-heptose 1-phosphate guanylyltransferase. This enzyme catalyses the following chemical reaction

D-glycero-β-D-manno-heptose 1,7-bisphosphate 7-phosphatase (EC 3.1.3.82) is an enzyme with systematic name D-glycero-β-D-manno-heptose 1,7-bisphosphate 7-phosphohydrolase. This enzyme catalyses the following chemical reaction

GmhB may refer to:

D-glycero-α-D-manno-heptose 1,7-bisphosphate 7-phosphatase (EC 3.1.3.83) is an enzyme with systematic name D-glycero-α-D-manno-heptose 1,7-bisphosphate 7-phosphohydrolase. This enzyme catalyses the following chemical reaction

D-sedoheptulose 7-phosphate isomerase is an enzyme with systematic name D-glycero-D-manno-heptose 7-phosphate aldose-ketose-isomerase. This enzyme catalyses the following chemical reaction

References

  1. ↑ McArthur F, Andersson CE, Loutet S, Mowbray SL, Valvano MA (August 2005). "Functional analysis of the glycero-manno-heptose 7-phosphate kinase domain from the bifunctional HldE protein, which is involved in ADP-L-glycero-D-manno-heptose biosynthesis". Journal of Bacteriology. 187 (15): 5292–300. doi:10.1128/jb.187.15.5292-5300.2005. PMC   1196024 . PMID   16030223.
  2. ↑ Kneidinger B, Marolda C, Graninger M, Zamyatina A, McArthur F, Kosma P, Valvano MA, Messner P (January 2002). "Biosynthesis pathway of ADP-L-glycero-beta-D-manno-heptose in Escherichia coli". Journal of Bacteriology. 184 (2): 363–9. doi:10.1128/jb.184.2.363-369.2002. PMC   139585 . PMID   11751812.
  3. ↑ Valvano MA, Messner P, Kosma P (July 2002). "Novel pathways for biosynthesis of nucleotide-activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides". Microbiology. 148 (Pt 7): 1979–89. doi: 10.1099/00221287-148-7-1979 . PMID   12101286.
  4. ↑ Jin UH, Chung TW, Lee YC, Ha SD, Kim CH (October 2001). "Molecular cloning and functional expression of the rfaE gene required for lipopolysaccharide biosynthesis in Salmonella typhimurium". Glycoconjugate Journal. 18 (10): 779–87. PMID   12441667.
  5. ↑ Wang L, Huang H, Nguyen HH, Allen KN, Mariano PS, Dunaway-Mariano D (February 2010). "Divergence of biochemical function in the HAD superfamily: D-glycero-D-manno-heptose-1,7-bisphosphate phosphatase (GmhB)". Biochemistry. 49 (6): 1072–81. doi:10.1021/bi902018y. PMC   2844805 . PMID   20050615.
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