Xylulokinase

xylulokinase
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
Search PMC articles PubMed articles NCBI proteins

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

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

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

Applications

Hydrogen production

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

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

• Bunker RD, Bulloch EM, Dickson JM, Loomes KM, Baker EN (January 2013). "Structure and function of human xylulokinase, an enzyme with important roles in carbohydrate metabolism". The Journal of Biological Chemistry. 288 (3): 1643–52. doi: 10.1074/jbc.m112.427997 . PMC   3548474 . PMID   23179721.
• Hickman J; Ashwell G (1958). "Purification and properties of D-xylulokinase in liver". J. Biol. Chem. 232 (2): 737–748. doi: 10.1016/S0021-9258(19)77394-3 . PMID   13549459.
• Simpson FJ (1966). "D-Xylulokinase". Carbohydrate Metabolism. Methods Enzymol. Vol. 9. pp. 454–458. doi:10.1016/0076-6879(66)09093-1. ISBN   978-0-12-181809-8.
• Slein MW (1955). "Xylose isomerase from Pasteurella pestis, strain A-1122". J. Am. Chem. Soc. 77 (6): 1663–1667. Bibcode:1955JAChS..77.1663S. doi:10.1021/ja01611a074.
• Stumpf PK, Horecker BL (February 1956). "The role of xylulose 5-phosphate in xylose metabolism of Lactobacillus pentosus". The Journal of Biological Chemistry. 218 (2): 753–68. doi: 10.1016/S0021-9258(18)65840-5 . PMID   13295228.