Structure of human argininosuccinate synthetase
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چکیده
منابع مشابه
Nitro analogs of substrates for argininosuccinate synthetase and argininosuccinate lyase.
The nitro analogs of aspartate and argininosuccinate were synthesized and tested as substrates and inhibitors of argininosuccinate synthetase and argininosuccinate lyase, respectively. The Vmax for 3-nitro-2-aminopropionic acid was found to be 60% of the maximal rate of aspartate utilization in the reaction catalyzed by argininosuccinate synthetase. Only the nitronate form of this substrate, in...
متن کاملMolecular analysis of argininosuccinate synthetase deficiency in human fibroblasts.
We have analyzed cultured skin fibroblasts derived from patients with argininosuccinate synthetase deficiency for alterations in gene structure, mRNA content, and protein structure. Genomic DNA was digested with the endonucleases EcoRI or HindIII, and the fragments were analyzed by Southern blotting and hybridization with a cDNA probe for argininosuccinate synthetase. The blot pattern is comple...
متن کاملExpression of the human argininosuccinate synthetase gene in hamster transferents.
The structural gene for human argininosuccinate synthetase [L-citrulline:L-aspartate ligase (AMP-forming), EC 6.3.4.5] was transferred to argininosuccinate synthetase-deficient Chinese hamster cells via metaphase chromosomes isolated from human lymphoblast line MGL8D1, a constitutive overproducer of argininosuccinate synthetase, and from its repressible parent, MGL8B2. Argininosuccinate synthet...
متن کاملMolecular definition of bovine argininosuccinate synthetase deficiency.
Citrullinemia is an inborn error of metabolism due to deficiency of the urea cycle enzyme, argininosuccinate synthetase [L-citrulline:L-aspartate ligase (AMP-forming), EC 6.3.4.5]. The disease was first described in humans but was recently reported in dairy cattle in Australia. Here we report the nucleotide sequence of the normal bovine cDNA for argininosuccinate synthetase and the mutation pre...
متن کاملCrystal structure of argininosuccinate synthetase from Thermus thermophilus HB8. Structural basis for the catalytic action.
Argininosuccinate synthetase catalyzes the ATP-dependent condensation of a citrulline with an aspartate to give argininosuccinate. The three-dimensional structures of the enzyme from Thermus thermophilus HB8 in its free form, complexed with intact ATP, and complexed with an ATP analogue (adenylyl imidodiphosphate) and substrate analogues (arginine and succinate) have been determined at 2.3-, 2....
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ژورنال
عنوان ژورنال: Acta Crystallographica Section D Biological Crystallography
سال: 2008
ISSN: 0907-4449
DOI: 10.1107/s0907444907067455