In enzymology, a xylulokinase (EC 2.7.1.17) is an enzyme that catalyzes the chemical reaction

xylulokinase
D-xylulokinase monomer, Human
Identifiers
EC no.2.7.1.17
CAS no.9030-58-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins
ATP + D-xylulose ⇌ ADP + D-xylulose 5-phosphate

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.

Structural studies

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As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2ITM and 2NLX.

Applications

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Hydrogen production

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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]

References

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  1. ^ Martín Del Campo, J. S.; Rollin, J.; Myung, S.; Chun, Y.; Chandrayan, S.; Patiño, R.; Adams, M. W.; Zhang, Y. H. (2013-04-03). "Virginia Tech team develops process for high-yield production of hydrogen from xylose under mild conditions". Angewandte Chemie International Edition in English. 52 (17). Green Car Congress: 4587–90. doi:10.1002/anie.201300766. PMID 23512726. Retrieved 2014-01-22.
  2. ^ Martín del Campo JS, Rollin J, Myung S, Chun Y, Chandrayan S, Patiño R, Adams MW, Zhang YH (April 2013). "High-yield production of dihydrogen from xylose by using a synthetic enzyme cascade in a cell-free system". Angewandte Chemie. 52 (17): 4587–90. doi:10.1002/anie.201300766. PMID 23512726.

Further reading

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