xylulokinase | |||||||||
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![]() D-xylulokinase monomer, Human | |||||||||
Identifiers | |||||||||
EC no. | 2.7.1.17 | ||||||||
CAS no. | 9030-58-4 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a xylulokinase (EC 2.7.1.17) is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme are ATP and D-xylulose, whereas its two products are ADP and D-xylulose 5-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-xylulose 5-phosphotransferase. Other names in common use include xylulokinase (phosphorylating), and D-xylulokinase. This enzyme participates in pentose and glucuronate interconversions.
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2ITM and 2NLX.
In 2014 a low-temperature 50 °C (122 °F), atmospheric-pressure enzyme-driven process to convert xylose into hydrogen with nearly 100% of the theoretical yield was announced. The process employs 13 enzymes, including xylulokinase. [1] [2]
Phosphoglucomutase is an enzyme that transfers a phosphate group on an α-D-glucose monomer from the 1 to the 6 position in the forward direction or the 6 to the 1 position in the reverse direction.
Xylose is a sugar first isolated from wood, and named for it. Xylose is classified as a monosaccharide of the aldopentose type, which means that it contains five carbon atoms and includes an aldehyde functional group. It is derived from hemicellulose, one of the main constituents of biomass. Like most sugars, it can adopt several structures depending on conditions. With its free aldehyde group, it is a reducing sugar.
A serine/threonine protein kinase is a kinase enzyme, in particular a protein kinase, that phosphorylates the OH group of the amino-acid residues serine or threonine, which have similar side chains. At least 350 of the 500+ human protein kinases are serine/threonine kinases (STK).
D-Xylose is a five-carbon aldose that can be catabolized or metabolized into useful products by a variety of organisms.
In enzymology, a D-xylulose reductase (EC 1.1.1.9) is an enzyme that is classified as an Oxidoreductase (EC 1) specifically acting on the CH-OH group of donors (EC 1.1.1) that uses NAD+ or NADP+ as an acceptor (EC 1.1.1.9). This enzyme participates in pentose and glucuronate interconversions; a set of metabolic pathways that involve converting pentose sugars and glucuronate into other compounds.
In enzymology, a dihydrofolate synthase is an enzyme that catalyzes the chemical reaction
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
In enzymology, a dephospho-[reductase kinase] kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a D-ribulokinase is an enzyme that catalyzes the chemical reaction
In enzymology, a guanylate kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a L-xylulokinase is an enzyme that catalyzes the chemical reaction
In enzymology, a myosin-heavy-chain kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a N-acylmannosamine kinase is an enzyme that catalyzes the chemical reaction
Phosphoribulokinase (PRK) (EC 2.7.1.19) is an essential photosynthetic enzyme that catalyzes the ATP-dependent phosphorylation of ribulose 5-phosphate (RuP) into ribulose 1,5-bisphosphate (RuBP), both intermediates in the Calvin Cycle. Its main function is to regenerate RuBP, which is the initial substrate and CO2-acceptor molecule of the Calvin Cycle. PRK belongs to the family of transferase enzymes, specifically those transferring phosphorus-containing groups (phosphotransferases) to an alcohol group acceptor. Along with ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCo), phosphoribulokinase is unique to the Calvin Cycle. Therefore, PRK activity often determines the metabolic rate in organisms for which carbon fixation is key to survival. Much initial work on PRK was done with spinach leaf extracts in the 1950s; subsequent studies of PRK in other photosynthetic prokaryotic and eukaryotic organisms have followed. The possibility that PRK might exist was first recognized by Weissbach et al. in 1954; for example, the group noted that carbon dioxide fixation in crude spinach extracts was enhanced by the addition of ATP. The first purification of PRK was conducted by Hurwitz and colleagues in 1956.
ATP + Mg2+ - D-ribulose 5-phosphate ADP + D-ribulose 1,5-bisphosphate
In enzymology, a protein-histidine tele-kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a rhamnulokinase is an enzyme that catalyzes the chemical reaction
In enzymology, a riboflavin kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a ribokinase is an enzyme that catalyzes the chemical reaction
In molecular biology, the ATP:guanido phosphotransferase family is a family of structurally and functionally related enzymes, that reversibly catalyse the transfer of phosphate between ATP and various phosphagens. The enzymes belonging to this family include: