# Xylulokinase

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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](/source/Enzymology), a **xylulokinase** ([EC](/source/Enzyme_Commission_number) [2.7.1.17](https://enzyme.expasy.org/EC/2.7.1.17)) is an [enzyme](/source/Enzyme) that [catalyzes](/source/Catalysis) the [chemical reaction](/source/Chemical_reaction)

- ATP + D-xylulose ⇌ ADP + D-xylulose 5-phosphate

Thus, the two [substrates](/source/Substrate_(biochemistry)) of this enzyme are [ATP](/source/Adenosine_triphosphate) and [D-xylulose](/source/D-xylulose), whereas its two [products](/source/Product_(chemistry)) are [ADP](/source/Adenosine_diphosphate) and [D-xylulose 5-phosphate](/source/Xylulose_5-phosphate).

This enzyme belongs to the family of [transferases](/source/Transferase), specifically those transferring phosphorus-containing groups ([phosphotransferases](/source/Phosphotransferase)) with an alcohol group as acceptor. The [systematic name](/source/List_of_enzymes) 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](/source/Pentose_and_glucuronate_interconversions).

## Structural studies

As of late 2007, two [structures](/source/Tertiary_structure) have been solved for this class of enzymes, with [PDB](/source/Protein_Data_Bank) accession codes [PDB](/source/Protein_Data_Bank): [2ITM](https://www.rcsb.org/structure/2ITM)​ and [PDB](/source/Protein_Data_Bank): [2NLX](https://www.rcsb.org/structure/2NLX)​.

## Applications

### Hydrogen production

In 2014 a low-temperature 50 °C (122 °F), atmospheric-pressure [enzyme](/source/Enzyme)-driven process to convert [xylose](/source/Xylose) into hydrogen with nearly 100% of the theoretical yield was announced. The process employs 13 enzymes, including xylulokinase.[1][2]

## References

1. **[^](#cite_ref-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"](http://www.greencarcongress.com/2013/04/vt-20130403.html). *Angewandte Chemie International Edition in English*. **52** (17). Green Car Congress: 4587–90. [doi](/source/Doi_(identifier)):[10.1002/anie.201300766](https://doi.org/10.1002%2Fanie.201300766). [PMID](/source/PMID_(identifier)) [23512726](https://pubmed.ncbi.nlm.nih.gov/23512726). Retrieved 2014-01-22.

1. **[^](#cite_ref-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](/source/Doi_(identifier)):[10.1002/anie.201300766](https://doi.org/10.1002%2Fanie.201300766). [PMID](/source/PMID_(identifier)) [23512726](https://pubmed.ncbi.nlm.nih.gov/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"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3548474). *The Journal of Biological Chemistry*. **288** (3): 1643–52. [doi](/source/Doi_(identifier)):[10.1074/jbc.m112.427997](https://doi.org/10.1074%2Fjbc.m112.427997). [PMC](/source/PMC_(identifier)) [3548474](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3548474). [PMID](/source/PMID_(identifier)) [23179721](https://pubmed.ncbi.nlm.nih.gov/23179721).

- Hickman J; Ashwell G (1958). ["Purification and properties of D-xylulokinase in liver"](https://doi.org/10.1016%2FS0021-9258%2819%2977394-3). *J. Biol. Chem*. **232** (2): 737–748. [doi](/source/Doi_(identifier)):[10.1016/S0021-9258(19)77394-3](https://doi.org/10.1016%2FS0021-9258%2819%2977394-3). [PMID](/source/PMID_(identifier)) [13549459](https://pubmed.ncbi.nlm.nih.gov/13549459).

- Simpson FJ (1966). "D-Xylulokinase". *Carbohydrate Metabolism*. Methods Enzymol. Vol. 9. pp. 454–458. [doi](/source/Doi_(identifier)):[10.1016/0076-6879(66)09093-1](https://doi.org/10.1016%2F0076-6879%2866%2909093-1). [ISBN](/source/ISBN_(identifier)) [978-0-12-181809-8](https://en.wikipedia.org/wiki/Special:BookSources/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](/source/Bibcode_(identifier)):[1955JAChS..77.1663S](https://ui.adsabs.harvard.edu/abs/1955JAChS..77.1663S). [doi](/source/Doi_(identifier)):[10.1021/ja01611a074](https://doi.org/10.1021%2Fja01611a074).

- Stumpf PK, Horecker BL (February 1956). ["The role of xylulose 5-phosphate in xylose metabolism of Lactobacillus pentosus"](https://doi.org/10.1016%2FS0021-9258%2818%2965840-5). *The Journal of Biological Chemistry*. **218** (2): 753–68. [doi](/source/Doi_(identifier)):[10.1016/S0021-9258(18)65840-5](https://doi.org/10.1016%2FS0021-9258%2818%2965840-5). [PMID](/source/PMID_(identifier)) [13295228](https://pubmed.ncbi.nlm.nih.gov/13295228).

v t e Transferases: phosphorus-containing groups (EC 2.7) 2.7.1–2.7.4: phosphotransferase/kinase (PO4) 2.7.1: OH acceptor Hexo- Gluco- Fructo- Hepatic Galacto- Phosphofructo- 1 Liver Muscle Platelet 2 Riboflavin Shikimate Thymidine ADP-thymidine NAD+ Glycerol Pantothenate Mevalonate Pyruvate Deoxycytidine PFP Diacylglycerol Phosphoinositide 3 Class I PI 3 Class II PI 3 Sphingosine Glucose-1,6-bisphosphate synthase 2.7.2: COOH acceptor Phosphoglycerate Aspartate kinase Glutamate 5-kinase 2.7.3: N acceptor Creatine 2.7.4: PO4 acceptor Phosphomevalonate Adenylate Nucleoside-diphosphate Uridylate Guanylate Thiamine-diphosphate 2.7.6: diphosphotransferase (P2O7) Ribose-phosphate diphosphokinase Thiamine diphosphokinase 2.7.7: nucleotidyltransferase (PO4-nucleoside) Polymerase DNA polymerase DNA-directed DNA polymerase I/A γ θ ν T7 Taq II/B α δ ε ζ Pfu III/C IV/X β λ μ TDT V/Y η ι κ RNA-directed DNA polymerase Reverse transcriptase Telomerase RNA polymerase Template-directed RNA polymerase I II III IV V ssRNAP POLRMT Primase 1 2 PrimPol RNA-dependent RNA polymerase Polyadenylation PAP PNPase Phosphorolytic 3′ to 5′ exoribonuclease RNase PH PNPase Nucleotidyltransferase UTP—glucose-1-phosphate uridylyltransferase Galactose-1-phosphate uridylyltransferase Guanylyltransferase mRNA guanylyltransferase Other Recombinase (Integrase) Transposase 2.7.8: miscellaneous Phosphatidyltransferases CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase CDP-diacylglycerol—serine O-phosphatidyltransferase CDP-diacylglycerol—inositol 3-phosphatidyltransferase CDP-diacylglycerol—choline O-phosphatidyltransferase Glycosyl-1-phosphotransferase N-acetylglucosamine-1-phosphate transferase 2.7.10–2.7.13: protein kinase (PO4; protein acceptor) 2.7.10: protein-tyrosine see tyrosine kinases 2.7.11: protein-serine/threonine see serine/threonine-specific protein kinases 2.7.12: protein-dual-specificity see serine/threonine-specific protein kinases 2.7.13: protein-histidine Protein-histidine pros-kinase Protein-histidine tele-kinase Histidine kinase

v t e Enzymes Activity Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis Regulation Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator Classification EC number Enzyme superfamily Enzyme family List of enzymes Kinetics Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics Types EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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Adapted from the Wikipedia article [Xylulokinase](https://en.wikipedia.org/wiki/Xylulokinase) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/Xylulokinase?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.