2.6.1.16	A38T	mutant shows increased resistance against glucosamine-6-phosphate	672444	
2.6.1.16	A594G	site-directed mutagenesis, the mutant shows unaltered activity (5 U/l) compared to wild-type (5 U/l)	-, 758961	
2.6.1.16	A602L	enhanced activity compared to the wild type enzyme, the behaviour of the mutant is similar to that of the wild type counterpart during purification demonstrating no significant modification in the overall protein structure	673687	
2.6.1.16	biotechnology	the recombinant enzyme expressed in Saccharomyces cereviaise reveals some differences from the wild type enzyme, such as improved stability and less sensitivity to UDP-GlcNAc	739575	
2.6.1.16	C1A	C1A-GlmS does not reveal glutaminase activity at 37°C when tested in the presence of Gln only	721419	
2.6.1.16	C1A	the structure of the inactive C1A mutant, crystallized in the presence of D-fructose 6-phosphate and Gln is deterimined. The C1A-GlmS structure is organized as a hexamer. The enzyme is regulated by a morpheein-type allosteric mechanism, in which functional dimeric GlmS is in equilibrium with the inactive hexamer	722779	
2.6.1.16	G40A	mutant with exchanged guanine is inactive. The 2.7 A resolution crystal structure of the mutant shows that the RNA is in a conformation nearly identical to that of the wild-type glmS ribozyme. The experimental electron density maps indicate that GlcN6P binds to the G40A mutant in the same location as in the wild-type ribozyme. Raman pH titrations of GlcN6P using crystals of the G40A mutant glmS ribozyme show that the pKa of the amine of the ribozyme-bound GlcN6P differs substantially for the wild-type and G40A mutant ribozymes	722453	
2.6.1.16	G471S	mutant shows increased resistance against glucosamine-6-phosphate	672444	
2.6.1.16	I271T	mutant shows increased resistance against glucosamine-6-phosphate	672444	
2.6.1.16	I3T	mutant shows increased resistance against glucosamine-6-phosphate	672444	
2.6.1.16	K595H	site-directed mutagenesis, the mutant shows unaltered activity (5 U/l) compared to wild-type (5 U/l)	-, 758961	
2.6.1.16	L468P	mutant shows increased resistance against glucosamine-6-phosphate	672444	
2.6.1.16	L593S	site-directed mutagenesis, the mutant shows highly increased activity (48 U/l) compared to wild-type (5 U/l)	-, 758961	
2.6.1.16	additional information	combinatorial fine-tuning of glucosamine-6-phosphate N-acetyltransferase (GNA1) and glutamine-fructose-6-phosphate aminotransferase (GlmS) expression by 5-terminus fusion engineering leads to overproduction of N-acetylglucosamine in Bacillus subtilis. Enhanced expression of GlmS is achieved at the transcriptional and translational levels by fusing an mRNA stabilizer to the 5'-terminus of GlmS gene. Under the control of GNA1 (fusion with cMyc tag and with the optimum RBS M-Rm) and GlmS (fusion with mRNA stabilizer DELTAermC+14/7A), the GlcNAc titer and yield in the shake flask increase to 18.5 g/l and 0.37 g GlcNAc/g glucose, which are 2.9fold and 2.3fold that of the control, respectively. Synthetic pathway fine-tuning method at the transcriptional and translational levels by combinatorial modulation of regulatory elements, including epitope tag, RBS sequence, and mRNA stabilizer, method evaluation, overview	-, 756261	
2.6.1.16	additional information	Crispr-mediated elimination of Drosophila gfat genes and generation of single gene null mutations in the fly counterparts of gfat1 and gfat2 (gfat1-/- and gfat2-/-). Deletions for either enzyme are fully lethal and homozygotes lacking either GFAT1 or GFAT2 die at or prior to the first instar larval stage. When genetically eliminated, neither isoform is able to compensate for the other. Dietary supplementation with D-glucosamine-6-phosphate rescues GFAT2 deficiency and restores viability to gfat2-/- mutants. In contrast, glucosamine-6-phosphate does not rescue gfat1-/- animals	759211	
2.6.1.16	additional information	expression of truncated enzyme variants as His-tagged proteins. Fragments encompassing residues 1-345 and 346-712 represent the functional glutamine amide-hydrolysing GAH and hexose phosphate-isomerizing domains ISOM, respectively. The native GAH domain is monomeric, whereas the native ISOM domain forms tetramers, as does the whole enzyme. The binding site for the feedback inhibitor, uridine 5'-diphospho-N-acetyl-D-glucosamine, is located in the ISOM domain. Inhibitor binding affects amidohydrolysing activity of the GAH domain and, as a consequence, the D-glucosamine-6-phosphate-synthetic activity of the whole enzyme. The fragment containing residues 218-283 is neither involved in ligand binding nor in protein oligomerization. An intramolecular channel connects the GAH and ISOM domains. The channel becomes leaky upon deletion of amino acids 709-712 and in the W97F and W97G mutants	671896	
2.6.1.16	additional information	improvement of enzyme BsGlms activity through computer simulation and site saturation mutagenesis, method, overview	-, 758961	
2.6.1.16	additional information	three recombinant versions containing internal oligoHis fragments are constructed: (a) by substituting residues 343-348 of the interdomain undecapeptide linker with hexaHis, (b) by replacing solvent-exposed residues 655-660 of the isomerase domain with hexaHis, and (c) by replacing amino acids at positions 568 and 569 with His residues to generate the three-dimensional hexaHis microdomain in the enzyme quaternary structure. The resulting constructs are purified to homogeneity. Catalytic properties are comparable with that of the wild-type enzyme. The construct containing the 655-660 hexaHis insert is found to be a homodimeric protein	723015	
2.6.1.16	S243E	increase in activity, 2fold lower Km value for D-fructose 6-phosphate than wild-type	685109	
2.6.1.16	S449P	mutant shows increased resistance against glucosamine-6-phosphate	672444	
2.6.1.16	S596F	site-directed mutagenesis, the mutant shows slightly increased activity (7 U/l) compared to wild-type (5 U/l)	-, 758961	
2.6.1.16	V597R	site-directed mutagenesis, the mutant shows slightly increased activity (8 U/l) compared to wild-type (5 U/l)	758961	
2.6.1.16	V605L	enhanced activity compared to the wild type enzyme, the behaviour of the mutant is similar to that of the wild type counterpart during purification demonstrating no significant modification in the overall protein structure	673687	
2.6.1.16	V711F	mutation results in an almost complete elimination of the GlcN-6-P-synthetic activity, with the retention of the amidohydrolase and sugar phosphate-isomerizing activities	671896	
2.6.1.16	V711F	reduction of the glucosamine 6-phosphate-synthetic activity, with the retention of the amidohydrolase and sugar phosphate-isomerizing activities	671896	
2.6.1.16	W74A	efficiency of ammonia transfer is close to zero. No use of ammonia as a substrate	673687	
2.6.1.16	W74A	enhanced activity compared to the wild type enzyme, the behaviour of the mutant is similar to that of the wild type counterpart during purification demonstrating no significant modification in the overall protein structure	673687	
2.6.1.16	W74F	enhanced activity compared to the wild type enzyme, the behaviour of the mutant is similar to that of the wild type counterpart during purification demonstrating no significant modification in the overall protein structure	673687	
2.6.1.16	W74L	decrease in ammonia transfer, 5-7fold increase in the affinity for glutamine in the presence of fructose 6-phosphate	673687	
2.6.1.16	W74L	enhanced activity compared to the wild type enzyme, the behaviour of the mutant is similar to that of the wild type counterpart during purification demonstrating no significant modification in the overall protein structure	673687	
2.6.1.16	W97F	mutation results in an almost complete elimination of the GlcN-6-P synthetic activity, with the retention of the amidohydrolase and sugar phosphate-isomerizing activities	671896	
2.6.1.16	W97F	reduction of the glucosamine 6-phosphate-synthetic activity, with the retention of the amidohydrolase and sugar phosphate-isomerizing activities. Residue W97 functions as a molecular gate, opening and closing the intramolecular channel that connects the glutamine amide-hydrolysing and hexose phosphate-isomerizing domains	671896	
2.6.1.16	W97G	almost complete elimination of the glucosamine 6-phosphate-synthetic activity, with the retention of the amidohydrolase and sugar phosphate-isomerizing activities. Residue W97 functions as a molecular gate, opening and closing the intramolecular channel that connects the glutamine amide-hydrolysing and hexose phosphate-isomerizing domains	671896	
2.6.1.16	W97G	mutation results in an almost complete elimination of the GlcN-6-P-synthetic activity, with the retention of the amidohydrolase and sugar phosphate-isomerizing activities	671896