Asparagine synthase (glutamine-hydrolysing)
| Asparagine synthase (glutamine-hydrolysing) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Asparagine synthetase B dimer, E.Coli | |||||||||
| Identifiers | |||||||||
| EC no. | 6.3.5.4 | ||||||||
| CAS no. | 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 sites.[6]
References
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ a b 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.
External links
- Asparagine+synthase+(glutamine-hydrolysing) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
