Primary Information |
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| BoMiProt ID | Bomi226 |
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| Protein Name | Argininosuccinate lyase |
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| Organism | Bos taurus |
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| Uniprot ID | Q3SZJ0 |
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| Milk Fraction | Exosome |
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| Ref Sequence ID | NP_001029600.1 |
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| Aminoacid Length | 473 |
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| Molecular Weight | 52743 |
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| FASTA Sequence |
Download |
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| Gene Name | ASL |
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| Gene ID | 512771 |
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| Protein Existence Status | Reviewed: Experimental evidence at transcript level |
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Secondary Information |
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| Presence in other biological fluids/tissue/cells | bovine liver,
bovine kidney, all human tissues, cultured
human skin fibroblasts, found
in greatest concentrations in the livers of urea-forming animals |
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| Protein Function | catalyzes argininosuccinate = arginine + fumarate; catalyzes the fourth reaction of the Krebs-Henseleit ornithine cycle; biosynthesis of arginine from ornithine or citrulline. Argininosuccinate lyase (ASL) catalyzes the fourth reaction in this cycle, resulting in the breakdown of argininosuccinic acid to arginine and fumarate. |
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| Biochemical Properties | specific activity of
10.3 nmol min'1 mg'1 in the forward, argininosuccinate
cleaving, reaction and 8.0 nmol min^-1 mg^-1 in the reverse
reaction; enzyme appears to
be a tetramer composed of subunits of identical molecular
weight; Km values were 0.20 mM for argininosuccinate,
5.3 mM for fumarate, and 3.0 mM for arginine; The enzyme
exhibited normal Michaelis-Menten kinetics, and guanosine 5'-triphosphate (GTP) had no affect on the activity of the
enzyme |
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| Significance in milk | dietary supply of arginine in milk |
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| PTMs | N-acetylation at Alanine,N6-Acetylation at Lys |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Significance of PTMs | Acetylation on Lys-288 is decreased on the addition of extra amino acids resulting in activation of enzyme activity. |
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| Additional Comments | ASLD is typically established with elevation of plasma citrulline together with elevated argininosuccinic acid in the plasma or urine. |
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| Bibliography | 1. O’Brien, W. E. and Barr, R. H. (1981) ‘Argininosuccinate lyase: purification and characterization from human liver’, Biochemistry, 20(7), pp. 2056–2060. doi: 10.1021/bi00510a049. 2.Nagamani SC, Erez A, Lee B. Argininosuccinate lyase deficiency. Genet Med. 2012 May;14(5):501-7. doi: 10.1038/gim.2011.1. Epub 2012 Jan 5. PMID: 22241104; PMCID: PMC3709024. |
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