N-acetylglucosamine kinase
| N-acetylglucosamine kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
![]() N-acetylglucosamine kinase dimer, Thermotoga maritima | |||||||||
| Identifiers | |||||||||
| EC no. | 2.7.1.59 | ||||||||
| CAS no. | 9027-48-9 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
N-acetylglucosamine kinase (EC 2.7.1.59) is an enzyme that catalyzes the chemical reaction
The enzyme characterised from the bacteria, Streptococcus pyogenes and Escherichia coli, converts N-acetylglucosamine to N-acetylglucosamine 6-phosphate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP).[1][2] The enzyme has also been found in hog spleen.[3] Its structure in Thermotoga maritima has been determined.[4]
This enzyme is a transferase, specifically one transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:N-acetyl-D-glucosamine 6-phosphotransferase. Other names in common use include acetylglucosamine kinase (phosphorylating), ATP:2-acetylamino-2-deoxy-D-glucose 6-phosphotransferase, 2-acetylamino-2-deoxy-D-glucose kinase, and acetylaminodeoxyglucokinase.[5]
References
- ↑ Barkulis SS (1966). "[76a] N-Acetyl-d-glucosamine kinase". N-Acetyl-D-glucosamine kinase. I. Streptococcus pyogenes. Methods Enzymol. Vol. 9. pp. 415–420. doi:10.1016/0076-6879(66)09085-2. ISBN 978-0-12-181809-8.
- ↑ Asensio C, Ruiz-Amil M (1966). "[76b] N-acetyl-d-glucosamine kinase". N-Acetyl-D-glucosamine kinase. II. Escherichia coli. Methods Enzymol. Vol. 9. pp. 421–425. doi:10.1016/0076-6879(66)09086-4. ISBN 978-0-12-181809-8.
- ↑ Datta A (October 1970). "Studies on hog spleen N-acetylglucosamine kinase. I. Purification and properties of N-acetylglucosamine kinase". Biochimica et Biophysica Acta. 220 (1): 51–60. doi:10.1016/0005-2744(70)90228-7. PMID 4319609.
- ↑ "Crystal structure of N-acetylglucosamine kinase (TM1224) from Thermotoga maritima at 2.46 a resolution". 2006. doi:10.2210/pdb2HOE/pdb.
- ↑ Enzyme 2.7.1.59 at KEGG Pathway Database.


