EC 6.3.5.4 - Asparagine synthase (glutamine-hydrolysing)

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IntEnz Enzyme Nomenclature
EC 6.3.5.4

Names

Accepted name:
asparagine synthase (glutamine-hydrolysing)
Other names:
asparagine synthetase (glutamine-hydrolysing)
glutamine-dependent asparagine synthetase
asparagine synthetase B
AS
AS-B
Systematic name:
L-aspartate:L-glutamine amido-ligase (AMP-forming)

Reactions

Comments:

The enzyme from Escherichia coli has two active sites [4] that are connected by an intramolecular ammonia tunnel [6,7]. The enzyme catalyses three distinct chemical reactions: glutamine hydrolysis to yield ammonia takes place in the N-terminal domain. The C-terminal active site mediates both the synthesis of a β-aspartyl-AMP intermediate and its subsequent reaction with ammonia. The ammonia released is channeled to the other active site to yield asparagine [7].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00406
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004066
CAS Registry Number: 37318-72-2
UniProtKB/Swiss-Prot: (36) [show] [UniProt]

References

  1. Patterson, M.K., Jr. and Orr, G.R.
    Asparagine biosynthesis by the Novikoff hepatoma. Isolation, purification, property, and mechanism studies of the enzyme system.
    J. Biol. Chem. 243: 376-380 (1968). [PMID: 4295091]
  2. Boehlein, S.K., Richards, N.G.J. and Schuster, S.M.
    Glutamine-dependent nitrogen transfer in Escherichia coli asparagine synthetase B. Searching for the catalytic triad.
    J. Biol. Chem. 269: 7450-7457 (1994). [PMID: 7907328]
  3. Richards, N.G.J. and Schuster, S.M.
    Mechanistic issues in asparagine synthetase catalysis.
    Adv. Enzymol. Relat. Areas Mol. Biol. 72: 145-198 (1998). [PMID: 9559053]
  4. Larsen, T.M., Boehlein, S.K., Schuster, S.M., Richards, N.G.J., Thoden, J.B., Holden, H.M. and Rayment, I.
    Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product.
    Biochemistry 38: 16146-16157 (1999). [PMID: 10587437]
  5. Larsen, T.M., Boehlein, S.K., Schuster, S.M., Richards, N.G.J., Thoden, J.B., Holden, H.M. and Rayment, I.
    Erratum report. Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product.
    Biochemistry 39: 7330 (2000). [PMID: 10852734]
  6. Huang, X., Holden, H.M. and Raushel, F.M.
    Channeling of substrates and intermediates in enzyme-catalyzed reactions.
    Annu. Rev. Biochem. 70: 149-180 (2001). [PMID: 11395405]
  7. Tesson, A.R., Soper, T.S., Ciustea, M. and Richards, N.G.J.
    Revisiting the steady state kinetic mechanism of glutamine-dependent asparagine synthetase from Escherichia coli.
    Arch. Biochem. Biophys. 413: 23-31 (2003). [PMID: 12706338]

[EC 6.3.5.4 created 1972, modified 2006]