EC Number   |
General Information |
Reference |
|---|
    2.7.7.23 | evolution |
although Entamoeba histolytica UAP exhibits the same three-domain global architecture as other UAPs, it appears to lack three alpha-helices at the N-terminus and contains two amino acids in the allosteric pocket that make it appear more like the enzyme from the human host than that from the other parasite Trypanosoma brucei |
737391 |
| 2.7.7.23 | 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 |
| 2.7.7.23 | 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 |
| 2.7.7.23 | evolution |
comparison of the activities of the ST0452 protein to those of similar enzymes from bacteria show that both the apparent Km and kcat values of the ST0452 GlcNAc-1-P UTase activity are smaller than those of Escherichia coli GlmU (EcGlmU) enzymes indicating that the archaeal ST0452 protein can accept a low concentration of substrate but that its turnover rate is lower than that of the EcGlmU enzyme |
-, 755852 |
| 2.7.7.23 | physiological function |
down-regulation of transcripts by RNA interference prevents larval growth or results in pupal paralysis, depending on time of injection of double-stranded RNAs. Down-regulation of transcripts at the mature adult stage results in cessation of oviposition in females, as well as fat body depletion and eventual death in both sexes |
722387 |
| 2.7.7.23 | physiological function |
down-regulation of transcripts by RNA interference results for isoform UAP1 in specific arrest at the larval-larval, larval-pupal or pupal-adult molts, depending on time of injection of double-stranded RNAs, loss of structural integrity and chitin staining and loss of peritrophic matrix-associated chitin. Down-regulation of transcripts at the mature adult stage results in cessation of oviposition in females, as well as fat body depletion and eventual death in both sexes |
722387 |
| 2.7.7.23 | physiological function |
enzyme ST0452 is multifunctional |
-, 760395 |
| 2.7.7.23 | more |
enzyme structure modeling and structure comparisons, detailed overview. Conformational changes occur in apo- and ligand-bound BmUAPs. Docking and molecular dynamics simulation studies of ligand-bound complexes of BmUAP, determination of binding mode of UTP, GlcNAc-1-P, and UDP-GlcNAc |
760749 |
| 2.7.7.23 | evolution |
GlmU belongs to the large family of sugar nucleotidyl transferases, which can be classified into group-I, which employs the two-metal mechanism-B as in GlmU, and group-II that employs a variant one metal mechanism-B, wherein the role of Mg2+ A is substituted by a conserved lysine. Eukaryotic sugar nucleotidyl transferases appear confined to group-II, structure-based sequence comparisons of sugar nucleotidyl transferases |
740866 |
| 2.7.7.23 | more |
GlmU forms a biological trimer, and two independent domains in each monomer catalyze two independent reactions in the protein. The enzyme uses a two-metal ion mechanism (mechanism-B). In contrast to well-established two-metal mechanism (mechanism-A) for enzymes acting on nucleic acids, mechanism-B is distinct in the way the two Mg2+ ions (Mg2+A and Mg2+B) are positioned and stabilized. Analysis of the catalytic mechanism for the uridyltransfer reaction in GlmU, role of metal ions in substrate binding, overview |
740866 |
