// Workers AI · dad joke modeDoes UDP-N-acetylglucosamine diphosphorylase go on a date? It's a sugar-phosphate match.
| UDP-N-acetylglucosamine diphosphorylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 N-acetyl glucosamine 1-phosphate uridyltransferase homotrimer, Mycobacterium tuberculosis | |||||||||
| Identifiers | |||||||||
| EC no. | 2.7.7.23 | ||||||||
| CAS no. | 9023-06-7 | ||||||||
| 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 | ||||||||
| |||||||||
UDP-N-acetylglucosamine diphosphorylase (EC 2.7.7.23) is an enzyme that catalyzes the reversible chemical reaction
The enzyme first characterised from sheep brain combines uridine triphosphate and N-acetyl-α-D-glucosamine 1-phosphate (1) to give uridine diphosphate N-acetylglucosamine (UDP-GlcNAc), with pyrophosphate (PPi) as a byproduct.[1][2] Initially, the enzyme was found to be catalysing the breakdown of UDP-GlcNAc but subsequent studies of the enzyme from Escherichia coli showed it to be involved in the biosynthesis of that compound.[3][4][5][6]
The crystal structure of two human isoforms of the enzyme have been determined.[7]
Nomenclature
[edit]This enzyme is a transferase, specifically one transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is UTP:N-acetyl-alpha-D-glucosamine-1-phosphate uridylyltransferase. Other names in common use include UDP-N-acetylglucosamine pyrophosphorylase, uridine diphosphoacetylglucosamine pyrophosphorylase, UTP:2-acetamido-2-deoxy-alpha-D-glucose-1-phosphate, uridylyltransferase, UDP-GlcNAc pyrophosphorylase, GlmU uridylyltransferase, Acetylglucosamine 1-phosphate uridylyltransferase, UDP-acetylglucosamine pyrophosphorylase, uridine diphosphate-N-acetylglucosamine pyrophosphorylase, uridine diphosphoacetylglucosamine phosphorylase, and acetylglucosamine 1-phosphate uridylyltransferase.[8]
References
[edit]- ↑ Strominger, Jack L.; Smith, Mildred S. (1959). "Uridine Diphosphoacetylglucosamine Pyrophosphorylase". Journal of Biological Chemistry. 234 (7): 1822–1827. doi:10.1016/S0021-9258(18)69933-8. PMID 13672971.
- ↑ Pattabiraman, T.N.; Bachhawat, B.K. (1961). "Purification of uridine diphosphoacetylglucosamine pyrophosphorylase from sheep brain". Biochimica et Biophysica Acta. 50: 129–134. doi:10.1016/0006-3002(61)91068-X. PMID 13733356.
- ↑ Mengin-Lecreulx, D.; Van Heijenoort, J. (1994). "Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: Characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis". Journal of Bacteriology. 176 (18): 5788–5795. doi:10.1128/jb.176.18.5788-5795.1994. PMC 196783. PMID 8083170.
- ↑ Gehring, Amy M.; Lees, Watson J.; Mindiola, Daniel J.; Walsh, Christopher T.; Brown, Eric D. (1996). "Acetyltransfer Precedes Uridylyltransfer in the Formation of UDP- N -acetylglucosamine in Separable Active Sites of the Bifunctional GlmU Protein of Escherichia coli". Biochemistry. 35 (2): 579–585. doi:10.1021/bi952275a. PMID 8555230.
- ↑ Wang-Gillam, Andrea; Pastuszak, Irena; Elbein, Alan D. (1998). "A 17-Amino Acid Insert Changes UDP-N-Acetylhexosamine Pyrophosphorylase Specificity from UDP-GalNAc to UDP-GlcNAc". Journal of Biological Chemistry. 273 (42): 27055–27057. doi:10.1074/jbc.273.42.27055. PMID 9765219.
- ↑ Olsen, Laurence R.; Roderick, Steven L. (2001). "Structure of the Escherichia coli GlmU Pyrophosphorylase and Acetyltransferase Active Sites,". Biochemistry. 40 (7): 1913–1921. doi:10.1021/bi002503n. PMID 11329257.
- ↑ Peneff, Caroline; Ferrari, Paul; Charrier, Véronique; et al. (2001). "Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: Role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture". The EMBO Journal. 20 (22): 6191–6202. doi:10.1093/emboj/20.22.6191. PMC 125729. PMID 11707391.
- ↑ Enzyme 2.7.7.23 at KEGG Pathway Database.
