Asparagine synthase (glutamine-hydrolysing)

Asparagine synthase (glutamine-hydrolysing) (EC 6.3.5.4, asparagine synthetase (glutamine-hydrolysing), glutamine-dependent asparagine synthetase, asparagine synthetase B, AS, AS-B) is an enzyme with systematic name L-aspartate:L-glutamine amido-ligase (AMP-forming).[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction

ATP + L-aspartate + L-glutamine + H2O AMP + diphosphate + L-asparagine + L-glutamate (overall reaction)
(1a) L-glutamine + H2O L-glutamate + NH3
(1b) ATP + L-aspartate + NH3 AMP + diphosphate + L-asparagine
Asparagine synthase (glutamine-hydrolysing)
Asparagine synthetase B dimer, E.Coli
Identifiers
EC no.6.3.5.4
CAS no.37318-72-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

The enzyme from Escherichia coli has two active sites.[6]

References
  1. Patterson MK, Orr GR (January 1968). "Asparagine biosynthesis by the Novikoff Hepatoma isolation, purification, property, and mechanism studies of the enzyme system". The Journal of Biological Chemistry. 243 (2): 376–80. PMID 4295091.
  2. Boehlein SK, Richards NG, Schuster SM (March 1994). "Glutamine-dependent nitrogen transfer in Escherichia coli asparagine synthetase B. Searching for the catalytic triad". The Journal of Biological Chemistry. 269 (10): 7450–7. PMID 7907328.
  3. Richards NG, Schuster SM (1998). "Mechanistic issues in asparagine synthetase catalysis". Advances in Enzymology and Related Areas of Molecular Biology. 72: 145–98. PMID 9559053.
  4. Larsen TM, Boehlein SK, Schuster SM, Richards NG, Thoden JB, Holden HM, Rayment I (December 1999). "Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product". Biochemistry. 38 (49): 16146–57. CiteSeerX 10.1.1.453.5998. doi:10.1021/bi9915768. PMID 10587437.
  5. Huang X, Holden HM, Raushel FM (2001). "Channeling of substrates and intermediates in enzyme-catalyzed reactions". Annual Review of Biochemistry. 70: 149–80. doi:10.1146/annurev.biochem.70.1.149. PMID 11395405.
  6. Tesson AR, Soper TS, Ciustea M, Richards NG (May 2003). "Revisiting the steady state kinetic mechanism of glutamine-dependent asparagine synthetase from Escherichia coli". Archives of Biochemistry and Biophysics. 413 (1): 23–31. doi:10.1016/s0003-9861(03)00118-8. PMID 12706338.
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