Biology:Asparagine synthase (glutamine-hydrolysing)
From HandWiki
| Asparagine synthase (glutamine-hydrolysing) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 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 | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] AMP + diphosphate + L-asparagine + L-glutamate (overall reaction)
- (1a) L-glutamine + H2O [math]\displaystyle{ \rightleftharpoons }[/math] L-glutamate + NH3
- (1b) ATP + L-aspartate + NH3 [math]\displaystyle{ \rightleftharpoons }[/math] AMP + diphosphate + L-asparagine
The enzyme from Escherichia coli has two active sites.[6]
References
- ↑ "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. January 1968. PMID 4295091.
- ↑ "Glutamine-dependent nitrogen transfer in Escherichia coli asparagine synthetase B. Searching for the catalytic triad". The Journal of Biological Chemistry 269 (10): 7450–7. March 1994. PMID 7907328.
- ↑ "Mechanistic issues in asparagine synthetase catalysis". Advances in Enzymology and Related Areas of Molecular Biology 72: 145–98. 1998. PMID 9559053.
- ↑ "Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product". Biochemistry 38 (49): 16146–57. December 1999. doi:10.1021/bi9915768. PMID 10587437.
- ↑ "Channeling of substrates and intermediates in enzyme-catalyzed reactions". Annual Review of Biochemistry 70: 149–80. 2001. doi:10.1146/annurev.biochem.70.1.149. PMID 11395405.
- ↑ 6.0 6.1 "Revisiting the steady state kinetic mechanism of glutamine-dependent asparagine synthetase from Escherichia coli". Archives of Biochemistry and Biophysics 413 (1): 23–31. May 2003. doi:10.1016/s0003-9861(03)00118-8. PMID 12706338.
External links
- Asparagine+synthase+(glutamine-hydrolysing) at the US National Library of Medicine Medical Subject Headings (MeSH)
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