GNPDA2 Protein, Human

The GNPDA2 protein catalyzes the reversible conversion of α-D-glucosamine 6-phosphate to β-D-fructose 6-phosphate and ammonium ions, which is a key step in de novo UDP-GlcNAc biosynthesis. GNPDA2 Protein, Human is the recombinant human-derived GNPDA2 protein, expressed by E. coli , with tag free. The total length of GNPDA2 Protein, Human is 275 a.a., .

The GNPDA2 protein assumes a crucial role in cellular metabolism by catalyzing the reversible conversion of alpha-D-glucosamine 6-phosphate (GlcN-6P) into beta-D-fructose 6-phosphate (Fru-6P) and ammonium ion. This enzymatic reaction represents a regulatory step in de novo uridine diphosphate-N-acetyl-alpha-D-glucosamine (UDP-GlcNAc) biosynthesis through the hexosamine pathway. The deamination process is coupled to aldo-keto isomerization, mediating the metabolic flux from UDP-GlcNAc toward Fru-6P. Particularly noteworthy is GNPDA2's capability, under high ammonium levels, to drive amination and isomerization of Fru-6P, promoting hexosamine and UDP-GlcNAc synthesis. This dynamic interplay highlights GNPDA2's role in fine-tuning the metabolic fluctuations of cytosolic UDP-GlcNAc, influencing hyaluronan synthesis during tissue remodeling. The enzyme's regulatory function underscores its significance in coordinating metabolic pathways critical for nucleotide biosynthesis and cellular homeostasis.

Human

E. coli

Tag Free

Q8TDQ7 (R2-N276)

132789

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.