Engineering an Arginine Catabolizing Bioconjugate: Biochemical and Pharmacological Characterization of PEGylated Derivatives of Arginine Deiminase fromMycoplasma arthritidis
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چکیده
منابع مشابه
Arginine Deiminase from Mycoplasma arthritidis
Hydrodynamic, chemical, and optical properties of arginine deiminase (EC 3.5.3.6) from Mycoplasma arthritidis are reported for the enzyme isolated from log phase cells. The s& +, and D’& values of the enzyme are 5.48 S and 5.87 x 10V7 cm’/s, respectively; the molecular weight is 87,300. Determination of the amino acid composition shows that about 45% of the residues are nonpolar. Another unique...
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UNLABELLED Arginine deiminase (ADI), an arginine-metabolizing enzyme involved in cell signaling, is dysregulated in multiple inflammatory diseases and cancers. We hypothesized that pegylated ADI (ADI-PEG) provide protection against colitis. METHODS Dextran sodium sulfate colitis was induced in IL-10-deficient and BALB/c (WT) mice. ADI-PEG was administered i.p., and inflammatory mediators and ...
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The strategy of enzymatic degradation of amino acids to deprive malignant cells of important nutrients is an established component of induction therapy of acute lymphoblastic leukemia. Here we show that acute myeloid leukemia (AML) cells from most patients with AML are deficient in a critical enzyme required for arginine synthesis, argininosuccinate synthetase-1 (ASS1). Thus, these ASS1-deficie...
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We have analyzed the evolution of the three genes encoding structural enzymes of the arginine deiminase (ADI) pathway, arginine deiminase (ADI), ornithine transcarbamoylase (OTC), and carbamate kinase (CK) in a wide range of organisms, including Archaea, Bacteria, and Eukarya. This catabolic route was probably present in the last common ancestor to all the domains of life. The results obtained ...
متن کاملArginine deiminase uses an active-site cysteine in nucleophilic catalysis of L-arginine hydrolysis.
Arginine deiminase (EC 3.5.3.6) catalyzes the hydrolysis of l-arginine to citrulline and ammonium ion, which is the first step of the microbial l-arginine degradation pathway. The deiminase conserves the active-site Cys-His-Asp motif found in several related enzymes that catalyze group-transfer reactions from the guanidinium center of arginine-containing substrates. For each of these enzymes, n...
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ژورنال
عنوان ژورنال: Bioconjugate Chemistry
سال: 2007
ISSN: 1043-1802,1520-4812
DOI: 10.1021/bc060380z