Asparagine synthase (glutamine-hydrolysing)

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Asparagine synthase (glutamine-hydrolysing)
1ct9.jpg
Asparagine synthetase B dimer, E.Coli
Identifiers
EC number 6.3.5.4
CAS number 37318-72-2
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

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

The enzyme from Escherichia coli has two active sites6].

References[edit]

  1. ^ Patterson, M.K.; Jr.; Orr, G.R. (1968). "Asparagine biosynthesis by the Novikoff hepatoma. Isolation, purification, property, and mechanism studies of the enzyme system". J. Biol. Chem. 243 (2): 376–380. PMID 4295091. 
  2. ^ Boehlein, S.K.; Richards, N.G.; Schuster, S.M. (1994). "Glutamine-dependent nitrogen transfer in Escherichia coli asparagine synthetase B. Searching for the catalytic triad". J. Biol. Chem. 269 (10): 7450–7457. PMID 7907328. 
  3. ^ Richards, N.G.; Schuster, S.M. (1998). "Mechanistic issues in asparagine synthetase catalysis". Adv. Enzymol. Relat. Areas Mol. Biol. 72: 145–198. PMID 9559053. 
  4. ^ Larsen, T.M.; Boehlein, S.K.; Schuster, S.M.; Richards, N.G.; Thoden, J.B.; Holden, H.M.; Rayment, I. (1999). "Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product". Biochemistry. 38 (49): 16146–16157. doi:10.1021/bi9915768. PMID 10587437. 
  5. ^ Huang, X.; Holden, H.M.; Raushel, F.M. (2001). "Channeling of substrates and intermediates in enzyme-catalyzed reactions". Annu. Rev. Biochem. 70: 149–180. doi:10.1146/annurev.biochem.70.1.149. PMID 11395405. 
  6. ^ Tesson, A.R.; Soper, T.S.; Ciustea, M.; Richards, N.G. (2003). "Revisiting the steady state kinetic mechanism of glutamine-dependent asparagine synthetase from Escherichia coli". Arch. Biochem. Biophys. 413 (1): 23–31. doi:10.1016/s0003-9861(03)00118-8. PMID 12706338. 

External links[edit]