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Structure of Human Argininosuccinate Synthetase [PDF]

Acta Crystallographica Section D: Biological Crystallography, 2008
Argininosuccinate synthetase catalyzes the transformation of citrulline and aspartate into argininosuccinate and pyrophosphate using the hydrolysis of ATP to AMP and pyrophosphate. This enzymatic process constitutes the rate-limiting step in both the urea and arginine-citrulline cycles.
Martin Högbom, Tobias Karlberg, Jonas Uppenberg   +2 more
exaly   +6 more sources

Argininosuccinate Synthetase From the Urea Cycle to the Citrulline–NO Cycle

FEBS Journal, 2003
Argininosuccinate synthetase (ASS, EC 6.3.4.5) catalyses the condensation of citrulline and aspartate to form argininosuccinate, the immediate precursor of arginine. First identified in the liver as the limiting enzyme of the urea cycle, ASS is now recognized as a ubiquitous enzyme in mammalian tissues.
Alain Lavoinne, Annie Husson
exaly   +5 more sources

High Cerebral Guanidinoacetate and Variable Creatine Concentrations in Argininosuccinate Synthetase and Lyase Deficiency: Implications for Treatment?

Molecular Genetics and Metabolism, 2006
Cerebral creatine and guanidinoacetate and blood and urine metabolites were studied in four patients with argininosuccinate synthetase (ASS) or argininosuccinate lyase (ASL) deficiency receiving large doses of arginine. Urine and blood metabolites varied
N M Verhoeven, D J Reijngoud, F J van Spronsen   +2 more
exaly   +2 more sources

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Argininosuccinate synthetase of Neurospora crassa

Archives of Biochemistry and Biophysics, 1967
Abstract The argininosuccinate synthetase ( l -citrulline: l -aspartate ligase (AMP), E.C.6.3.4.5) of Neurospora crassa has been studied in crude extracts and in partially purified form. The conditions necessary for enzyme activity resemble closely those previously described for the corresponding enzyme from other sources. Both l -α-amino-n-butyric
D E, Wampler, J L, Fairley
openaire   +2 more sources

Kinetic mechanism of argininosuccinate synthetase

Archives of Biochemistry and Biophysics, 1983
The kinetic mechanism of bovine liver argininosuccinate synthetase has been determined at pH 7.5. The initial velocity and product and dead-end inhibition patterns are consistent with the ordered addition of MgATP, citrulline, and aspartate, followed by the ordered release of argininosuccinate, MgPPi, and AMP.
F M, Raushel, J L, Seiglie
openaire   +2 more sources

Amplification of human argininosuccinate synthetase pseudogenes

Journal of Molecular Biology, 1986
The human genome contains multiple pseudogenes for an argininosuccinate synthetase (AS) gene. To elucidate the molecular mechanisms of generation and dispersion, complete nucleotide sequences of four different AS pseudogenes, psi AS-Y, psi AS-A1, psi AS-A2 and psi AS-A3, have been determined. A comparison of these sequences with those of three reported
H, Nomiyama, K, Obaru, Y, Jinno, I, Matsuda, K, Shimada, T, Miyata   +5 more
openaire   +2 more sources

Expression of Argininosuccinate Synthetase in Patients With Hepatocellular Carcinoma

Journal of Gastroenterology and Hepatology (Australia), 2013
AbstractBackground and AimArginine is a nonessential amino acid for humans and mice because it can be synthesized from citrulline by argininosuccinate synthetase (ASS) and argininosuccinate lyase. Hepatocellular carcinoma (HCC) is believed to be auxotrophic for arginine through the lack of expression of ASS.
Li Li, Zebin Mao, Ruizhao Qi
exaly   +3 more sources

Stereochemical probes of the argininosuccinate synthetase reaction

Biochemistry, 1986
The stereochemical course of the argininosuccinate synthetase reaction has been determined. The SP isomer of [alpha-17O,alpha-18O,alpha beta-18O]ATP is cleaved to (SP)-[16O,17O,18O]AMP by the action of argininosuccinate synthetase in the presence of citrulline and aspartate. The overall stereochemical transformation is therefore net inversion, and thus
T L, Chapman, T B, Shull, F M, Raushel
openaire   +2 more sources

Abnormal mRNA for argininosuccinate synthetase in citrullinaemia

Nature, 1983
Citrullinaemia is a human inborn error of metabolism resulting from the deficiency of argininosuccinate synthetase. In a previous study of cultured skin fibroblasts from citrullinaemia patients, we showed that the presumed defects in DNA were not detectable by Southern blotting analysis, and that only 2 of 11 cell lines contained detectable enzyme ...
T S, Su, A L, Beaudet, W E, O'Brien
openaire   +2 more sources