View source for Coenzyme F420-0:L-glutamate ligase

{{Infobox enzyme
| Name = Asparagine synthase (glutamine-hydrolysing)
| EC_number = 6.3.5.4
| CAS_number = 37318-72-2
| IUBMB_EC_number = 6/3/5/4
| GO_code = 
| image = 
| width = 
| caption =
}}
'''Asparagine synthase (glutamine-hydrolysing)''' ({{EC number|6.3.5.4}}, ''[[asparagine synthetase]] (glutamine-hydrolysing)'', ''glutamine-dependent asparagine synthetase'', ''asparagine synthetase B'', ''AS'', ''AS-B'') is an [[enzyme]] with system name ''L-aspartate:L-glutamine amido-ligase (AMP-forming)''.<ref>{{cite journal | title = Asparagine biosynthesis by the Novikoff hepatoma. Isolation, purification, property, and mechanism studies of the enzyme system |author = Patterson, M.K., Jr. and Orr, G.R. |journal = J. Biol. Chem. |year = 1968 |volume = 243 |pages = 376–380 |pmid = 4295091 |issue=2}}</ref><ref>{{cite journal | title = Glutamine-dependent nitrogen transfer in <em>Escherichia coli</em> asparagine synthetase B. Searching for the catalytic triad |author = Boehlein, S.K., Richards, N.G. and Schuster, S.M. |journal = J. Biol. Chem. |year = 1994 |volume = 269 |pages = 7450–7457 |pmid = 7907328 |issue=10}}</ref><ref>{{cite journal | title = Mechanistic issues in asparagine synthetase catalysis |author = Richards, N.G. and Schuster, S.M. |journal = Adv. Enzymol. Relat. Areas Mol. Biol. |year = 1998 |volume = 72 |pages = 145–198 |pmid = 9559053}}</ref><ref>{{cite journal | title = Three-dimensional structure of <em>Escherichia coli</em> asparagine synthetase B: a short journey from substrate to product |author = Larsen, T.M., Boehlein, S.K., Schuster, S.M., Richards, N.G., Thoden, J.B., Holden, H.M. and Rayment, I. |journal = Biochemistry |year = 1999 |volume = 38 |pages = 16146–16157 |pmid = 10587437 |issue=49}}</ref><ref>{{cite journal | title = Channeling of substrates and intermediates in enzyme-catalyzed reactions |author = Huang, X., Holden, H.M. and Raushel, F.M. |journal = Annu. Rev. Biochem. |year = 2001 |volume = 70 |pages = 149–180 |pmid = 11395405 |doi=10.1146/annurev.biochem.70.1.149}}</ref><ref>{{cite journal | title = Revisiting the steady state kinetic mechanism of glutamine-dependent asparagine synthetase from <em>Escherichia coli</em> |author = Tesson, A.R., Soper, T.S., Ciustea, M. and Richards, N.G. |journal = Arch. Biochem. Biophys. |year = 2003 |volume = 413 |pages = 23–31 |pmid = 12706338 |issue=1}}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]

: ATP + L-[[aspartate]] + L-[[glutamine]] + H<sub>2</sub>O <math>\rightleftharpoons</math> AMP + [[diphosphate]] + L-[[asparagine]] + L-[[glutamate]] (overall reaction)
: (1a) L-glutamine + H<sub>2</sub>O <math>\rightleftharpoons</math> L-glutamate + NH<sub>3</sub>
: (1b) ATP + L-aspartate + NH<sub>3</sub> <math>\rightleftharpoons</math> AMP + diphosphate + L-asparagine

The enzyme from ''[[Escherichia coli]]'' has two active sites6].

== References ==
{{reflist}}

== External links ==
* {{MeshName|Asparagine+synthase+(glutamine-hydrolysing)}}

[[Category:EC 6.3.5]]