Experimental evidence for structure-activity features in common between mammalian histidine decarboxylase and ornithine decarboxylase

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Mammalian histidine decarboxylase: from structure to function.

Histamine is a multifunctional biogenic amine with relevant roles in intercellular communication, inflammatory processes and highly prevalent pathologies. Histamine biosynthesis depends on a single decarboxylation step, carried out by a PLP-dependent histidine decarboxylase activity (EC 4.1.1.22), an enzyme that still remains to be fully characterized. Nevertheless, during the last few years, i...

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Regulation of mammalian ornithine decarboxylase.

17 Melvin, M. A. L. and Keir, H. M. (1978) Expt. Cell Res. 111,231-236 18 Melvin, M. A. L. and Keir, H. M. (1979) Biochem. SOC. Trans. 7, 689-691 19 Wallace, H. M. and Keir, H. M. (1981) Biochim. Biophys. Acta 676,25-30 20 Melvin, M. A. L., Wallace, H. M. and Keir, H. M. (1980) Physiol. Chem. Phys. 12, 431-439 21 Coleman, C. S. and Wallace, H. M. (1990) 'Biochem. SOC. Trans. 18, 1228-1229 22 Wa...

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The pest regions containing C-termini of mammalian ornithine decarboxylase and histidine decarboxylase play different roles in protein degradation.

Proteasome 26S must recognize the PEST region-containing C-terminus of mammalian ornithine decarboxylase (ODC) monomer to proceed with degradation. We have detected PEST regions in both termini of mammalian histidine decarboxylase (HDC). In the present report, a chimaeric ODC/HDC was used to elucidate whether the PEST region-containing C-termini of ODC and HDC are exchangeable. Wild-type rat OD...

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Ornithine decarboxylase activity in insulin-deficient states.

The activity of ornithine decarboxylase, the rate-controlling enzyme in polyamine biosynthesis, was determined in tissues of normal control rats and rats made diabetic with streptozotocin. In untreated diabetic rats fed ad libitum, ornithine decarboxylase activity was markedly diminished in liver, skeletal muscle, heart and thymus. Ornithine decarboxylase was not diminished in a comparable grou...

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Crystallization and Subunit Structure of Histidine Decarboxylase

Histidine decarboxylase from Lactobacillus 30u has been crystallized in a variety of forms which together indicate a revised subunit structure for the native particle. Octahedral crystals of the wild type enzyme obtained at room temperature from ammonium sulfate solutions in microdiffusion cells belong to tetragonal space group 14122 with a = b = 222 A and c = 107.5 A. Trigonal and hexagonal pl...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1996

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj3200365