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:||Degradation/Utilization/Assimilation → Amino Acids Degradation → Proteinogenic Amino Acids Degradation → L-asparagine Degradation|
Some taxa known to possess this pathway include : Dickeya chrysanthemi, Escherichia coli K-12 substr. MG1655, Hordeum vulgare, Lupinus albus, Neonectria obtusispora, Pectobacterium carotovorum, Pisum sativum, Thermus thermophilus, Vicia faba, Zea mays
L-Asparagine is hydrolyzed to L-aspartate and ammonia by the enzyme asparaginase [Voet04]. The enzyme has been characterized from diverse sources, including bacteria, archaea [Yao05], fungi [Sinclair94, Kil95, Raha90], ciliates [Tsavdaridis94] and plants [Sodek80]. It has also been characterized from the liver and serum of guinea pigs [Zhang95b].
The enzyme has anti-tumor activity and purified L-asparaginase from Escherichia coli K-12 and Dickeya chrysanthemi have been used clinically to treat lymphoblastic leukemia and lymphosarcoma (in [Kotzia05]). The enzyme from some species contains glutaminase activity, believed to cause clinical side-effects. Enzyme preparations from species with decreased glutaminase activity, such as Pectobacterium carotovorum (previously known as Erwinia carotovora) have been characterized as potential therapeutics [Kotzia05].
Asparagine Degradation in Plants
Asparagine is the first amino acid discovered in plants, where it is the major nitrogen transport and storage compound. Asparagine is metabolized in plants in two routes, either via asparaginase (this pathway|) or via asparagine aminotransferase (see L-asparagine degradation II). Studies in pea suggested that the predominant route differs in different tissues. The asparaginase pathway predominates in seeds, whereas the aminotransferase pathway predominates in leaves [Ireland81].
In the asparaginase pathway, as depicted here, asparagine is deaminated to release aspartate and ammonia. The liberated ammonia is reassimilated and utilized for synthesis of all nitrogen containing compounds of the cell and in particular the amino acids. There is no evidence that aspartate is metabolized further in plants.
Unification Links: EcoCyc:ASPARAGINE-DEG1-PWY
Sodek80: Sodek, Ladaslav, Lea, Peter, Miflin, Benjamin "Distribution and properties of a potassium-dependdent asparaginase isolated from developing seeds of Pisum sativa and other plants." Plant Physiology, 1980, 65:22-26.
Yao05: Yao M, Yasutake Y, Morita H, Tanaka I (2005). "Structure of the type I L-asparaginase from the hyperthermophilic archaeon Pyrococcus horikoshii at 2.16 angstroms resolution." Acta Crystallogr D Biol Crystallogr 61(Pt 3);294-301. PMID: 15735339
Zhang95b: Zhang N, Clarke F, Di Trapani G, Keough D, Beacham I (1995). "Guinea pig serum L-asparaginase: purification, and immunological relationship to liver L-asparaginase and serum L-asparaginases in other mammals." Comp Biochem Physiol B Biochem Mol Biol 112(4);607-12. PMID: 8590375
Aghaiypour01a: Aghaiypour K, Wlodawer A, Lubkowski J (2001). "Structural basis for the activity and substrate specificity of Erwinia chrysanthemi L-asparaginase." Biochemistry 40(19);5655-64. PMID: 11341830
Bahreini14: Bahreini E, Aghaiypour K, Abbasalipourkabir R, Goodarzi MT, Saidijam M, Safavieh SS (2014). "An optimized protocol for overproduction of recombinant protein expression in Escherichia coli." Prep Biochem Biotechnol 44(5);510-28. PMID: 24219068
Borek00: Borek D, Jaskolski M (2000). "Crystallization and preliminary crystallographic studies of a new L-asparaginase encoded by the Escherichia coli genome." Acta Crystallogr D Biol Crystallogr 2000;56 ( Pt 11);1505-7. PMID: 11053866
Borek04: Borek D, Michalska K, Brzezinski K, Kisiel A, Podkowinski J, Bonthron DT, Krowarsch D, Otlewski J, Jaskolski M (2004). "Expression, purification and catalytic activity of Lupinus luteus asparagine beta-amidohydrolase and its Escherichia coli homolog." Eur J Biochem 271(15);3215-26. PMID: 15265041
Borek14: Borek D, Kozak M, Pei J, Jaskolski M (2014). "Crystal structure of active site mutant of antileukemic L-asparaginase reveals conserved zinc-binding site." FEBS J 281(18);4097-111. PMID: 25040257
Cantor09: Cantor JR, Stone EM, Chantranupong L, Georgiou G (2009). "The human asparaginase-like protein 1 hASRGL1 is an Ntn hydrolase with beta-aspartyl peptidase activity." Biochemistry 48(46);11026-31. PMID: 19839645
Derst00: Derst C, Henseling J, Rohm KH (2000). "Engineering the substrate specificity of Escherichia coli asparaginase II. Selective reduction of glutaminase activity by amino acid replacements at position 248." Protein Sci 9(10);2009-17. PMID: 11106175
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
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