In enzymology, a glutamine-fructose-6-phosphate transaminase (isomerizing) (EC 2.6.1.16) is an enzyme that catalyzes the chemical reaction
glutamine-fructose-6-phosphate transaminase (isomerizing) | |||||||||
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![]() Glutamine—fructose-6-phosphate transaminase 1, homodimer, Human | |||||||||
Identifiers | |||||||||
EC no. | 2.6.1.16 | ||||||||
CAS no. | 9030-45-9 | ||||||||
Alt. names |
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Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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- L-glutamine + D-fructose 6-phosphate L-glutamate + D-glucosamine 6-phosphate
Thus, the two substrates of this enzyme are L-glutamine and D-fructose 6-phosphate, whereas its two products are L-glutamate and D-glucosamine 6-phosphate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-glutamine:D-fructose-6-phosphate isomerase (deaminating). This enzyme participates in glutamate metabolism and aminosugars metabolism.
Structural studies
editAs of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes 1JXA, 1MOQ, 1MOR, 1MOS, 1XFF, 1XFG, 2BPL, 2J6H, 2POC, 2PUT, 2PUV, and 2PUW.
References
edit- Ghosh S, Blumenthal HJ, Davidson E, Roseman S (1960). "Glucosamine metabolism. V. Enzymatic synthesis of glucosamine 6-phosphate". J. Biol. Chem. 235: 1265–73. PMID 13827775.
- Gryder RM, Pogell BM (1960). "Further studies on glucosamine 6-phosphate synthesis by rat liver enzymes". J. Biol. Chem. 235: 558–62. PMID 13829889.
- Leloir LF, Cardini CE (1953). "The biosynthesis of glucosamine". Biochim. Biophys. Acta. 12 (1–2): 15–22. doi:10.1016/0006-3002(53)90119-X. hdl:11336/140740. PMID 13115409.
- Teplyakov A, Obmolova G, Badet-Denisot MA, Badet B (1999). "The mechanism of sugar phosphate isomerization by glucosamine 6-phosphate synthase". Protein Sci. 8 (3): 596–602. doi:10.1110/ps.8.3.596. PMC 2144271. PMID 10091662.