EC Number   |
General Information |
Reference |
|---|
   2.7.7.83 | malfunction |
the naturally occuring UAP1 A229T mutation is potentially pathogenic. The A229T mutation induces structural changes, leading to reduced thermal stability and activity of the mutant compared to wild-type |
761091 |
| 2.7.7.83 | metabolism |
the enzyme is involved in biosyntheis of UDP-N-acetylgalactosamine |
-, 748113 |
| 2.7.7.83 | more |
analysis of the overall structure of wild-type ST0452 protein (PDB ID 2GGO), residue 97 (Asn) interacts with the O-5 atom of N-acetylglucosamine (GlcNAc) in the complex without metal ions. UTP forms hydrogen bond interactions with seven residues, i.e. the main chain atoms of the position 8 Ala, position 9 Gly, position 12 Glu, position 79 Gly, and position 98 Gly residues and the side chain atoms of the position 13 Arg and position 73 Gln residues. The position 13 Arg and position 73 Gln residues appear to form more stable interactions than the other residues, with the position 13 Arg residue forming two hydrogen bonds with the phosphoryl group at the gamma-site and the amide group of the position 73 Gln residue forming a salt bridge with the uracil nucleobase in UTP |
-, 760395 |
| 2.7.7.83 | more |
the human UAP1 gene encodes two different isoforms, named AGX1 and AGX2, with AGX1 being more abundant in testis and AGX2 in somatic tissues |
761091 |
| 2.7.7.83 | more |
the ST0452 protein contains only two Cys residues, it is unlikely that CysCys bonds contribute to its thermostability |
-, 729696 |
| 2.7.7.83 | physiological function |
because the multifunctional ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon |
-, 725249 |
| 2.7.7.83 | physiological function |
enzyme ST0452 is multifunctional |
-, 760395 |
