Primary Information |
|---|
| BoMiProt ID | Bomi230 |
|---|
| Protein Name | Argininosuccinate synthase |
|---|
| Organism | Bos taurus |
|---|
| Uniprot ID | P14568 |
|---|
| Milk Fraction | Exosome |
|---|
| Ref Sequence ID | NP_776317.1 |
|---|
| Aminoacid Length | 412 |
|---|
| Molecular Weight | 46417 |
|---|
| FASTA Sequence |
Download |
|---|
| Gene Name | ASS1 |
|---|
| Gene ID | 280726 |
|---|
| Protein Existence Status | Reviewed: Experimental evidence at transcript level |
|---|
Secondary Information |
|---|
| Presence in other biological fluids/tissue/cells | liver, endothelial cells, kidney |
|---|
| Protein Function | important
role as the rate-limiting step in providing arginine
for an assortment of metabolic processes,
both catabolic and anabolic; plays a key role in (a) urea synthesis,
(b) nitric oxide synthesis, (c) polyamine synthesis,
(d) creatine synthesis, and (e) the de novo
synthesis of arginine to maintain serum levels; in liver, argininosuccinate synthase
associates with the outside of the mitochondria
to complete the urea cycle, which involves
both the mitochondrial and cytosolic
compartments |
|---|
| Biochemical Properties | Purified argininosuccinate synthetase from bovine liver
exhibits autoregulatory properties; tetrameric with subunits of ~ 45000 molecular weight; human lymphoblast enzyme has no accessible negative charge on the surface like yeast, bovine, and rat enzymes; exhibits negative cooperative substrate
binding activity; bovine liver argininosuccinate synthetase yields biphasic
double-reciprocal plots for citrulline and aspartic acid when
another substrate is limiting |
|---|
| Significance in milk | supplement the low level of arginine found in mother's milk |
|---|
| PTMs | S- nitrosylation |
|---|
Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| |
|---|
| Predicted Disorder Regions | NA |
|---|
| DisProt Annotation | |
|---|
| TM Helix Prediction | No TM helices |
|---|
| Significance of PTMs | Reversibly Inactivation by PTM |
|---|
| Bibliography | 1. Cohen, N. S. and Kuda, A. (1996) ‘Argininosuccinate synthetase and argininosuccinate lyase are localized around mitochondria: an immunocytochemical study.’, Journal of cellular biochemistry, 60(3), pp. 334–40. doi: 10.1002/(SICI)1097-4644(19960301)60:3%3C334::AID-JCB5%3E3.0.CO;2-X.
2. Kimball, M. E. and Jacoby, L. B. (1980) ‘Purification and properties of argininosuccinate synthetase from normal and canavanine-resistant human lymphoblasts’, Biochemistry, 19(4), pp. 705–709. doi: 10.1021/bi00545a015. |
|---|
