Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.4 (deaminase)
 5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The assay of the ethyl chloride metabolite S-ethyl-N-acetyl-L-cysteine in human urine by HPLC is described. The compound is enriched by adsorption on a non-polar adsorbent of graphitized non-porous carbon, and then stripped from positively charged compounds by application onto a strong acid cation-exchanger. Subsequently, an enzymatic deacetylation is carried out and the acylase is removed by centrifugal ultrafiltration. Separation of the sample is performed by cation-exchange chromatography applying an eluent of a very low elution strength (diluted formic acid). In the column effluent S-ethyl-L-cysteine is derivatized by o-phthaldialdehyde and the reaction product is detected by fluorescence measurement. In human urine a detection limit in the low ppb range is achieved.
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PMID:Assay of S-ethyl-N-acetyl-l-cysteine in urine by high-performance liquid chromatography using post-column reaction detection. 951 45

Helicobacter pylori AmiF formamidase that hydrolyzes formamide to produce formic acid and ammonia belongs to a member of the nitrilase superfamily. The crystal structure of AmiF was solved to 1.75A resolution using single-wavelength anomalous dispersion methods. The structure consists of a homohexamer related by 3-fold symmetry in which each subunit has an alpha-beta-beta-alpha four-layer architecture characteristic of the nitrilase superfamily. One exterior alpha layer faces the solvent, whereas the other one associates with that of the neighbor subunit, forming a tight alpha-beta-beta-alpha-alpha-beta-beta-alpha dimer. The apo and liganded crystal structures of an inactive mutant C166S were also determined to 2.50 and 2.30 A, respectively. These structures reveal a small formamide-binding pocket that includes Cys(166), Glu(60), and Lys(133) catalytic residues, in which Cys(166) acts as a nucleophile. Analysis of the liganded AmiF and N-carbamoyl d-amino acid amidohydrolase binding pockets reveals a common Cys-Glu-Lys triad, another conserved glutamate, and different subsets of ligand-binding residues. Molecular dynamic simulations show that the conserved triad has minimal fluctuations, catalyzing the hydrolysis of a specific nitrile or amide in the nitrilase superfamily efficiently.
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PMID:Crystal structure of Helicobacter pylori formamidase AmiF reveals a cysteine-glutamate-lysine catalytic triad. 1730 42