2.5 mM, 81% inhibition of isoenzyme 1, 92% inhibition of isoenzyme 2 and 92.5% inhibition of isoenzyme 3, inhibition by 1.25 mM is reversible upon addition of 2.5 mM dithiothreitol
Upregulation of glucosamine-phosphate N-acetyltransferase 1 is a promising diagnostic and predictive indicator for poor survival in patients with lung adenocarcinoma.
Upregulation of glucosamine-phosphate N-acetyltransferase 1 is a promising diagnostic and predictive indicator for poor survival in patients with lung adenocarcinoma.
HsGNA1 forms a tight dimer shown by crystal structure analysis: Each monomer is composed of 184 residues and the monomer structure belongs to a classic GNAT fold of a/b protein, containing all four motifs (C, D, A and B) conserved among the GNATs. Motif C (b1, g2 and a2) and Motif D (b2 and b3) are located next to and interact with each other, contributing to the hydrophobic core. Motif B (b5 and a5) make up part of the active site. Strands b1-b4 form an antiparallel beta sheet, and helices a1-a4, g1 and g2 are flanked on both sides of the central beta sheet. The HsGNA1 dimer is constructed by joining two subunits such that the C-terminal strand b6 projects to the other subunit. The b6-strand swaps between subunits in a dimer. The loop between strands b3 and b4 also extends to the other subunit, contributing to GlcN6P binding. In each subunit, the AcCoA binding cleft is formed by the diverging strands b4 and b5
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of HsGNA1 in its apo form, complexed with GlcN6P, and the E156A mutant are solved and refined to 2.7 A, 2.3 A and 2.0 A resolution, respectively. Results reveal new features of the GlcN6P binding in HsGNA1. The conserved charge distribution at the GlcN6P binding pocket is important for the acceptor substrate affinity. Glu156, a conserved residue present in GNA1 from various eukaryotic organisms, plays an important role in both the catalytic reaction and substrate affinity. Moreover, the GlcN6P binds to GNA1 without the help of AcCoA binding, suggesting that a pseudo-substrate could bind GNA1 as an inhibitor without the help of AcCoA
crystal structures of human and Aspergillus fumigatus GNA1 are determined: structural differences between the two enzymes are mostly located to the sugar-binding site, whereas the AcCoA-binding site is more conserved. These changes affect not only the electrostatics, but also reveal a more spacious sugar binding site in the Aspergillus fumigatus GNA1 enzyme, whereas large side chains at these positions create a tighter pocket in the HsGNA1 enzyme
hanging-drop vapour-diffusion method. The crystal diffract to better than 2.6 A resolution and belong to space group P4(1)2(1)2 or P4(3)2(1)2. The unit-cell parameters are a = b = 50.08, c = 142.88 A
mutant shows activities of both acetyl- and butyryltransfer, in the range of the wild type enzyme activity. Ratio of butanoyl-to-acetyltransferase activity is increased to 1
mutant shows activities of both acetyl- and butyryltransfer, in the range of the wild type enzyme activity. Ratio of butanoyl-to-acetyltransferase activity is increased to 0.9
mutant shows activities of both acetyl- and butyryltransfer, in the range of the wild type enzyme activity. Ratio of butanoyl-to-acetyltransferase activity is increased to 0.85
mutant shows activities of both acetyl- and butyryltransfer, in the range of the wild type enzyme activity. Ratio of butanoyl-to-acetyltransferase activity is increased to 0.9
mutant shows activities of both acetyl- and butyryltransfer, in the range of the wild type enzyme activity. Ratio of butanoyl-to-acetyltransferase activity is increased to 0.9
analysis of the global protein expression profiles of lung cancer cell A549 treated with abraxane and paclitaxel. The superior drug effect of abraxane is mainly due to the downregulation of GNA1, which causes proliferative delay and cell adhesion defect
Zhao, M.; Li, H.; Ma, Y.; Gong, H.; Yang, S.; Fang, Q.; Hu, Z.
Nanoparticle abraxane possesses impaired proliferation in A549 cells due to the underexpression of glucosamine 6-phosphate N-acetyltransferase 1 (GNPNAT1/GNA1)