Cloning human pyrroline-5-carboxylate reductase cDNA by complementation in Saccharomyces cerevisiae.
نویسندگان
چکیده
منابع مشابه
Crystal structure of human pyrroline-5-carboxylate reductase.
Pyrroline-5-carboxylate reductase (P5CR) is a universal housekeeping enzyme that catalyzes the reduction of Delta(1)-pyrroline-5-carboxylate (P5C) to proline using NAD(P)H as the cofactor. The enzymatic cycle between P5C and proline is very important for the regulation of amino acid metabolism, intracellular redox potential, and apoptosis. Here, we present the 2.8 Angstroms resolution structure...
متن کاملPurification, characterization, and crystallization of human pyrroline-5-carboxylate reductase.
Pyrroline-5-carboxylate reductase (P5CR) catalyzes the reduction of Delta1-pyrroline-5-carboxylate (P5C) to proline with concomitant oxidation of NAD(P)H to NAD(P)(+). The enzymatic cycle between P5C and proline is very important in many physiological and pathological processes. Human P5CR was over-expressed in Escherichia coli and purified to homogeneity by chromatography. Enzymatic assays of ...
متن کاملCLONING AND EXPRESSION OF HUMAN IFNα2B GENE IN SACCHAROMYCES CEREVISIAE
Interferon is a protein secreted by eucaryotic cells following stimulation by viruses, bacteria, and many other immunogenes. Recent medical studies indicate that interferons have effective role in the treatment of virus infections, immunodeficiency and certain types of cancer such as hairy cell leukaemia (HCL). The aim of the present study is to apply yeast strain for secreting human IFNα2b fol...
متن کاملPurification to homogeneity of pyrroline-5-carboxylate reductase of barley.
An enzyme has been purified to homogeneity from barley seedlings which has ;proline dehydrogenase' and the pyrroline-5-carboxylic acid reductase activities. The purification achieved is 39,000-fold as calculated from the proline dehydrogenase activity. The subunit molecular weight of the protein is 30 kilodaltons. The native enzyme has molecular weights up to 480 kilodaltons, depending on the b...
متن کاملResolving the cofactor-binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1.
Pyrroline-5-carboxylate reductase (PYCR) is the final enzyme in proline biosynthesis, catalyzing the NAD(P)H-dependent reduction of Δ1-pyrroline-5-carboxylate (P5C) to proline. Mutations in the PYCR1 gene alter mitochondrial function and cause the connective tissue disorder cutis laxa. Furthermore, PYCR1 is overexpressed in multiple cancers, and the PYCR1 knock-out suppresses tumorigenic growth...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1992
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)48364-0