Search by BoMiProt ID - Bomi230

Primary Information

BoMiProt ID Bomi230
Protein Name Argininosuccinate synthase
Organism Bos taurus
Uniprot IDP14568
Milk FractionExosome
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,
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.