Literature summary for 2.3.1.4 extracted from

Wang, J.; Liu, X.; Liang, Y.H.; Li, L.F.; Su, X.D.
Acceptor substrate binding revealed by crystal structure of human glucosamine-6-phosphate N-acetyltransferase 1 (2008), FEBS Lett., 582, 2973-2978.

Crystallization (Commentary)

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

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

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 [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
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

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q96EK6	-	-

Substrates and Products (Substrate)

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

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

Synonyms	Comment	Organism
glucosamine-6-phosphate N-acetyltransferase 1	-	Homo sapiens
HsGNA1	-	Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism
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

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Homo sapiens