2.7.7.23	A229T	naturally occuring enzyme AGX1 mutation, and site-directed mutagenesis, the A229T mutation causes a reduction of protein thermal stability compared to wild-type AGX1, and AGX1A229T has lower activity in producing UDP-GlcNA. In diploid organisms, haploinsufficiency is a phenomenon in which a single copy of a functional gene is not sufficient to produce the normal/wild-type phenotype. The patient is only heterozygous for the UAP1 A229T missense mutation. The UAP1 gene is potentially haploinsufficient and LoF intolerant, and the heterozygous UAP1 A229T mutation is potentially pathogenic. The recombinant mutant enzyme shows a reduction of the melting temperature (Tm) by approximately 5.3°C compared to wild-type. The A229T mutation induces structural changes. The R228-E44 interaction is abolished in the AGX1A229T structure caused by the position shift of R228. The pushing effect is likely due to the bulkier side chain of threonine compared to that of alanine. Along with the conformational change of the N-terminal domain in the AGX1A229T structure, is M218 shifted by 0.8 A away from R169, weakening the Q112-R169-M218 interaction	761091	
2.7.7.23	C307S	site-directed mutagenesis	-, 735569	
2.7.7.23	D105A	site-directed mutagenesis, the mutant shows 50% reduced activity compared to the wild-type enzyme	740262	
2.7.7.23	D208A	enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions	725308	
2.7.7.23	D208A	exhibits slightly weaker UDP-N-acetylglucosamine diphosphorylase activity than wild-type enzyme	725308	
2.7.7.23	D208A	GlcNAc-1-P UTase activity is 10% of the activity of wild-type ST0452 protein	748123	
2.7.7.23	D99A	no GlcNAc-1-P UTase activity	-, 748123	
2.7.7.23	DELTA1-130	deletion of N-terminus, very low activity	-, 288688	
2.7.7.23	DELTA1-182	deletion of N-terminus, very low activity	-, 288688	
2.7.7.23	DELTA1-227	deletion of N-terminus, very low activity	-, 288688