This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
|Superclasses:||Biosynthesis → Amino Acids Biosynthesis → Individual Amino Acids Biosynthesis → Asparagine Biosynthesis|
In both eukaryotes and prokaryotes, L-asparagine is biosynthesized from L-aspartate by amidation using L-glutamine as an amino group donor. In some organisms, including Escherichia coli K-12, a second pathway exists that utilizes ammonia instead (see asparagine biosynthesis II).
In Escherichia coli K-12 asparagine synthetase B, encoded by asnB, catalyzes this pathway, while asparagine synthetase A, encoded by asnA, catalyzes the ammonia-dependent reaction. Null mutations in both genes result in asparagine auxotrophy, as does a null mutation only in asnB under conditions of ammonia-limited growth. A null mutation only in asnA has no observable phenotype.
Superpathways: superpathway of asparagine biosynthesis
Unification Links: EcoCyc:ASPARAGINE-BIOSYNTHESIS
Charron04: Charron C, Roy H, Blaise M, Giege R, Kern D (2004). "Crystallization and preliminary X-ray diffraction data of an archaeal asparagine synthetase related to asparaginyl-tRNA synthetase." Acta Crystallogr D Biol Crystallogr 60(Pt 4);767-9. PMID: 15039580
Boehlein94: Boehlein SK, Richards NG, Schuster SM (1994). "Glutamine-dependent nitrogen transfer in Escherichia coli asparagine synthetase B. Searching for the catalytic triad." J Biol Chem 269(10);7450-7. PMID: 7907328
Cedar69: Cedar H, Schwartz JH (1969). "The asparagine synthetase of Escherhic coli. I. Biosynthetic role of the enzyme, purification, and characterization of the reaction products." J Biol Chem 1969;244(15);4112-21. PMID: 4895361
Ciustea05: Ciustea M, Gutierrez JA, Abbatiello SE, Eyler JR, Richards NG (2005). "Efficient expression, purification, and characterization of C-terminally tagged, recombinant human asparagine synthetase." Arch Biochem Biophys 440(1);18-27. PMID: 16023613
DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114
Humbert80: Humbert R, Simoni RD (1980). "Genetic and biomedical studies demonstrating a second gene coding for asparagine synthetase in Escherichia coli." J Bacteriol 1980;142(1);212-20. PMID: 6102982
Larsen99: Larsen TM, Boehlein SK, Schuster SM, Richards NG, Thoden JB, Holden HM, Rayment I (1999). "Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product." Biochemistry 1999;38(49);16146-57. PMID: 10587437
LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532
Olea04: Olea F, Perez-Garcia A, Canton FR, Rivera ME, Canas R, Avila C, Cazorla FM, Canovas FM, de Vicente A (2004). "Up-regulation and localization of asparagine synthetase in tomato leaves infected by the bacterial pathogen Pseudomonas syringae." Plant Cell Physiol 45(6);770-80. PMID: 15215512
Parr96: Parr IB, Boehlein SK, Dribben AB, Schuster SM, Richards NG (1996). "Mapping the aspartic acid binding site of Escherichia coli asparagine synthetase B using substrate analogs." J Med Chem 39(12);2367-78. PMID: 8691431
Showing only 20 references. To show more, press the button "Show all references".
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493