{{infobox enzyme | Name = xylulokinase | EC_number = 2.7.1.17 | CAS_number = 9030-58-4 | GO_code = 0004856 | image = 4bc2.jpg | width = 270 | caption = D-xylulokinase monomer, Human }} In [[enzymology]], a '''xylulokinase''' ({{EC number|2.7.1.17}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

: ATP + D-xylulose {{eqm}} ADP + D-xylulose 5-phosphate

Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[adenosine triphosphate|ATP]] and [[D-xylulose]], whereas its two [[product (chemistry)|products]] are [[adenosine diphosphate|ADP]] and [[Xylulose 5-phosphate|D-xylulose 5-phosphate]].

This enzyme belongs to the family of [[transferase]]s, specifically those transferring phosphorus-containing groups ([[phosphotransferase]]s) with an alcohol group as acceptor. The [[List of enzymes|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 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|2ITM}} and {{PDB link|2NLX}}.

== Applications ==

=== Hydrogen production ===

In 2014 a low-temperature {{convert|50|C|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.<ref>{{cite journal|url=http://www.greencarcongress.com/2013/04/vt-20130403.html |title=Virginia Tech team develops process for high-yield production of hydrogen from xylose under mild conditions |doi=10.1002/anie.201300766|publisher=Green Car Congress |date=2013-04-03 |pmid=23512726 |access-date=2014-01-22|last1=Martín Del Campo |first1=J. S. |last2=Rollin |first2=J. |last3=Myung |first3=S. |last4=Chun |first4=Y. |last5=Chandrayan |first5=S. |last6=Patiño |first6=R. |last7=Adams |first7=M. W. |last8=Zhang |first8=Y. H. |journal=Angewandte Chemie International Edition in English |volume=52 |issue=17 |pages=4587–90 |url-access=subscription }}</ref><ref>{{cite journal | vauthors = Martín del Campo JS, Rollin J, Myung S, Chun Y, Chandrayan S, Patiño R, Adams MW, Zhang YH | title = High-yield production of dihydrogen from xylose by using a synthetic enzyme cascade in a cell-free system | journal = Angewandte Chemie | volume = 52 | issue = 17 | pages = 4587–90 | date = April 2013 | pmid = 23512726 | doi = 10.1002/anie.201300766 }}</ref>

== References == {{reflist}}

== Further reading == {{refbegin}} * {{cite journal | vauthors = Bunker RD, Bulloch EM, Dickson JM, Loomes KM, Baker EN | title = Structure and function of human xylulokinase, an enzyme with important roles in carbohydrate metabolism | journal = The Journal of Biological Chemistry | volume = 288 | issue = 3 | pages = 1643–52 | date = January 2013 | pmid = 23179721 | pmc = 3548474 | doi = 10.1074/jbc.m112.427997 | doi-access = free }} * {{cite journal |author1 = Hickman J |author2 =Ashwell G | date = 1958 | title = Purification and properties of D-xylulokinase in liver | journal = J. Biol. Chem. | volume = 232 |issue =2 | pages = 737&ndash;748 |doi =10.1016/S0021-9258(19)77394-3 |pmid =13549459 |doi-access =free }} * {{cite book | vauthors = Simpson FJ | chapter = D-Xylulokinase | date = 1966 | title = Carbohydrate Metabolism | series = Methods Enzymol. | volume = 9 | pages = 454&ndash;458 | doi=10.1016/0076-6879(66)09093-1| isbn = 978-0-12-181809-8 }} * {{cite journal | vauthors = Slein MW | date = 1955 | title = Xylose isomerase from Pasteurella pestis, strain A-1122 | journal = J. Am. Chem. Soc. | volume = 77 | pages = 1663&ndash;1667 | doi = 10.1021/ja01611a074 | issue = 6 | bibcode = 1955JAChS..77.1663S }} * {{cite journal | vauthors = Stumpf PK, Horecker BL | title = The role of xylulose 5-phosphate in xylose metabolism of Lactobacillus pentosus | journal = The Journal of Biological Chemistry | volume = 218 | issue = 2 | pages = 753–68 | date = February 1956 | doi = 10.1016/S0021-9258(18)65840-5 | pmid = 13295228 | doi-access = free }} {{refend}}

{{Kinases}} {{Enzymes}} {{Portal bar|Biology|border=no}}

[[Category:EC 2.7.1]] [[Category:Enzymes of known structure]]

{{2.7-enzyme-stub}}