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MetaCyc Pathway: L-asparagine biosynthesis I
Traceable author statement to experimental supportInferred from experiment

Enzyme View:

Pathway diagram: L-asparagine biosynthesis I

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: BiosynthesisAmino Acids BiosynthesisProteinogenic Amino Acids BiosynthesisL-asparagine Biosynthesis

Some taxa known to possess this pathway include : Bos taurus, Escherichia coli K-12 substr. MG1655, Homo sapiens, Rattus norvegicus, Saccharomyces cerevisiae

Expected Taxonomic Range: Bacteria , Eukaryota

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 L-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.

The mammalian asparagine synthetase uses only cellular L-glutamine as amide donor. An archael-type asparagine synthetase has been crystallized [Charron04].

The only known role of L-asparagine is incorporation into proteins [Gottschalk86].

Superpathways: superpathway of L-asparagine biosynthesis

Variants: cyanide detoxification I, L-asparagine biosynthesis II, L-asparagine biosynthesis III (tRNA-dependent)


Revised 06-Mar-2007 by Fulcher CA, SRI International


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

Gottschalk86: Gottschalk, G "Bacterial Metabolism, Second Edition." Springer-Verlag, New York. 1986.

Hongo78: Hongo S, Matsumoto T, Sato T (1978). "Purification and properties of asparagine synthetase from rat liver." Biochim Biophys Acta 522(1);258-66. PMID: 23163

Voet04: Voet D, Voet JG (2004). "Biochemistry, 3rd Edition." John Wiley & Sons Inc.

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

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

Felton80: Felton J, Michaelis S, Wright A (1980). "Mutations in two unlinked genes are required to produce asparagine auxotrophy in Escherichia coli." J Bacteriol 142(1);221-8. PMID: 6102983

Gaudet10: Gaudet P, Livstone M, Thomas P (2010). "Annotation inferences using phylogenetic trees." PMID: 19578431

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Hongo81: Hongo S, Sato T (1981). "Purification of rat liver asparagine synthetase by affinity chromatography on reactive blue 2-agarose." Anal Biochem 114(1);163-6. PMID: 6116467

Hongo83: Hongo S, Sato T (1983). "Some molecular properties of asparagine synthetase from rat liver." Biochim Biophys Acta 742(3);484-9. PMID: 6132621

Hongo85: Hongo S, Sato T (1985). "Kinetic studies of asparagine synthetase from rat liver: role of Mg2+ in enzyme catalysis." Arch Biochem Biophys 238(2);410-7. PMID: 2859838

Hongo96: Hongo S, Chiyo T, Takeda M (1996). "Cloning of cDNA for asparagine synthetase from rat Sertoli cell." Biochem Mol Biol Int 38(1);189-96. PMID: 8932534

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

Hwang11: Hwang IS, An SH, Hwang BK (2011). "Pepper asparagine synthetase 1 (CaAS1) is required for plant nitrogen assimilation and defense responses to microbial pathogens." Plant J. PMID: 21535260

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

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

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

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".

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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