Asparagine synthase (glutamine-hydrolysing)
Asparagine synthase (glutamine-hydrolysing) | |||||||||
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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 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
- ↑ 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.
- ↑ 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.
- ↑ Richards, N.G.; Schuster, S.M. (1998). "Mechanistic issues in asparagine synthetase catalysis". Adv. Enzymol. Relat. Areas Mol. Biol. 72: 145–198. PMID 9559053.
- ↑ 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.
- ↑ 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.
- ↑ 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
- Asparagine synthase (glutamine-hydrolysing) at the US National Library of Medicine Medical Subject Headings (MeSH)
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