Crystallization (Comment) | Organism |
---|---|
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 | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
E156A | Km: 1.2 mM (substrate: glucosamine 6-phosphate), kcat = 9.7/sec (substrate: glucosamine 6-phosphate) | Homo sapiens |
E156D | Km: 0.175 mM (substrate: glucosamine 6-phosphate), kcat = 19.3/sec (substrate: glucosamine 6-phosphate) | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.175 | - |
D-glucosamine 6-phosphate | mutant E156D | Homo sapiens | |
0.2 | - |
D-glucosamine 6-phosphate | wild-type | Homo sapiens | |
1.2 | - |
D-glucosamine 6-phosphate | mutant E156A | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q96EK6 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + D-glucosamine 6-phosphate | - |
Homo sapiens | CoA + N-acetyl-D-glucosamine 6-phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 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 | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
glucosamine-6-phosphate N-acetyltransferase 1 | - |
Homo sapiens |
HsGNA1 | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Homo sapiens |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
9.7 | - |
D-glucosamine 6-phosphate | mutant E156A | Homo sapiens | |
19.3 | - |
D-glucosamine 6-phosphate | mutant E156D | Homo sapiens | |
22.1 | - |
D-glucosamine 6-phosphate | wild-type | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Homo sapiens |