Glutamine—fructose-6-phosphate transaminase (isomerizing)

Glutamine-fructose-6-phosphate transaminase (isomerizing)
Glutamine—fructose-6-phosphate transaminase 1, homodimer, Human
Identifiers
EC no.2.6.1.16
CAS no.9030-45-9
Alt. names
  • hexosephosphate aminotransferase
  • glucosamine-6-phosphate isomerase (glutamine-forming)
  • glutamine-fructose-6-phosphate transaminase (isomerizing)
  • D-fructose-6-phosphate amidotransferase
  • glucosaminephosphate isomerase
  • glucosamine 6-phosphate synthase
  • GlcN6P synthase
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Glutamine-fructose-6-phosphate transaminase (isomerizing) sometimes called glucosaminephosphate isomerase (EC 2.6.1.16) is an enzyme that catalyzes the chemical reaction:

2D representation of the chemical structure of glutamine.
L-glutamine
+
 
2D representation of the chemical structure of fructose 6-phosphate.
fructose 6-phosphate
 
 
 
Reversible left-right reaction arrow
 
 
 
2D representation of the chemical structure of Q26995161.
L-glutamic acid
+
 
2D representation of the chemical structure of Q27120892.
D-glucosamine 6-phosphate

The two substrates of this enzyme first characterised from Neurospora crassa are L-glutamine and D-fructose 6-phosphate (shown in its open-chain ketone form). Its products are L-glutamic acid and D-glucosamine 6-phosphate.

This enzyme is a transferase, specifically a transaminase, 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

As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1JXA​, PDB: 1MOQ​, PDB: 1MOR​, PDB: 1MOS​, PDB: 1XFF​, PDB: 1XFG​, PDB: 2BPL​, PDB: 2J6H​, PDB: 2POC​, PDB: 2PUT​, PDB: 2PUV​, and PDB: 2PUW​.

References

  1. ↑ 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.
  2. ↑ 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.
  3. ↑ Enzyme 2.6.1.16 at KEGG Pathway Database.
  4. ↑ Ghosh S, Blumenthal HJ, Davidson E, Roseman S (1960). "Glucosamine metabolism. V. Enzymatic synthesis of glucosamine 6-phosphate". J. Biol. Chem. 235 (5): 1265–73. doi:10.1016/S0021-9258(18)69397-4. PMID 13827775.
  5. ↑ Gryder RM, Pogell BM (1960). "Further studies on glucosamine 6-phosphate synthesis by rat liver enzymes". J. Biol. Chem. 235 (3): 558–62. doi:10.1016/S0021-9258(19)67904-4. PMID 13829889.