GFPT2
GFPT2, also known as GFAT2, is glutamine--fructose-6-phosphate aminotransferase [isomerizing] 2, the rate-limiting enzyme of the hexosamine biosynthetic pathway. It converts fructose-6-phosphate and glutamine into glucosamine-6-phosphate, controlling the flux of glucose into this pathway. Browse Assay Genie's current range of GFPT2 research reagents below, or read on for the biology behind the target.
GFPT2 is the rate-limiting enzyme of the hexosamine biosynthetic pathway (HBP). It catalyses the formation of glucosamine-6-phosphate from fructose-6-phosphate and glutamine, and in doing so controls how much glucose flux enters the pathway. Through this control, GFPT2 is likely to regulate the availability of precursors for N-linked and O-linked protein glycosylation.
The enzyme is subject to feedback inhibition by UDP-N-acetylglucosamine (UDP-GlcNAc), a downstream product of the pathway, although this inhibition is weaker than that seen with GFPT1, its paralogue. NCBI Gene annotates the GFPT2 gene as enabling L-glutamine:D-fructose-6-phosphate transaminase (isomerizing) activity and as involved in the UDP-N-acetylglucosamine biosynthetic process and in fructose 6-phosphate metabolism. The protein is predicted to be located in the cytosol.
GFPT2 belongs to the glutamine--fructose-6-phosphate transaminase family in HGNC nomenclature. It has previously been named glutamine-fructose-6-phosphate transaminase 2 and is commonly abbreviated GFAT2. Orthologues are present in mouse and rat, both designated Gfpt2. GFPT2 has been implicated in type 2 diabetes mellitus, which fits its position at the junction between glucose metabolism and glycosylation precursor supply.
As a rate-limiting enzyme, GFPT2 is a key point for studying how glucose flux is directed into the hexosamine biosynthetic pathway.
GFPT2 likely influences the supply of precursors for N- and O-linked glycosylation, making it relevant to glycobiology.
GFPT2 is implicated in type 2 diabetes mellitus, linking hexosamine pathway activity to metabolic disease research.
GFPT2 shows feedback inhibition by UDP-GlcNAc, weaker than GFPT1, offering a model for comparing paralogue regulation.
GFPT2 is the rate-limiting enzyme of the hexosamine biosynthetic pathway. It catalyses formation of glucosamine-6-phosphate from fructose-6-phosphate and glutamine, controlling glucose flux into the pathway and likely the supply of precursors for N- and O-linked glycosylation.
GFPT2 is also called GFAT2, and its HGNC name is glutamine--fructose-6-phosphate transaminase 2. UniProt lists it as glutamine--fructose-6-phosphate aminotransferase [isomerizing] 2. It was previously named glutamine-fructose-6-phosphate transaminase 2.
Both enzymes are inhibited by UDP-GlcNAc, but GFPT2 is inhibited to a lesser extent than GFPT1. The gene has mouse and rat orthologues, both called Gfpt2. Check the datasheet of any product for its validated reactivity.
The paralogous hexosamine pathway enzyme GFPT1, with related reagents at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt O94808; product specifications from Assay Genie datasheets.