MG_453_TETRAMER – UTP-glucose-1-phosphate uridylyltransferase

Name
WID MG_453_TETRAMER View in model
Name UTP-glucose-1-phosphate uridylyltransferase View in model
Cross references PDB: 2E3D
 
Structure
Biosynthesis [c]: (4) MG_453_MONOMERMG_453_TETRAMER View in model
No. subunits 4
Empirical formula (pH 7.5) H9540C5920N1520O1700S28
Molecular weight (pH 7.5; Da) 130105.69 View in model
Extinction coefficient 
(260 nm, 25C, pH 7.0)
-55640.00
Half life (OD (600 nm) = 0.3, 
M9 media, 36C; min)
1200.00 View in model
 
Synthesis
Formation process Process_MacromolecularComplexation View in model
Localization c
 
Function
Enzyme UTP-glucose-1-phosphate uridylyltransferase (irreversible)
[c]: G1P + H + UTPPPI + UDPG
View in model
Complex subunit UTP-glucose-1-phosphate uridylyltransferase
[c]: (4) MG_453_MONOMERMG_453_TETRAMER
View in model
 
Comments
Comments E. coli GalF is a structural protein which stabilizes galU and increases enzymatic activity [PUB_0426]. In other words, GalU alone is enzymatically active. M. genitalium appears to have only a GalU homolog. [PUB_0431]
References
  1. Marolda CL, Valvano MA. The GalF protein of Escherichia coli is not a UDP-glucose pyrophosphorylase but interacts with the GalU protein possibly to regulate cellular levels of UDP-glucose. Mol Microbiol 22, 827-40 (1996). WholeCell: PUB_0426, PubMed: 8971705

  2. Weissborn AC, Liu Q, Rumley MK, Kennedy EP. UTP: alpha-D-glucose-1-phosphate uridylyltransferase of Escherichia coli: isolation and DNA sequence of the galU gene and purification of the enzyme. J Bacteriol 176, 2611-8 (1994). WholeCell: PUB_0431, PubMed: 8169209

 
Metadata
Created 2012-10-01 15:07:42
Last updated 2012-10-01 15:14:16