Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:6.3.4.6 (urease)
 7,490 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Urea occurs in liver of the coelacanth Latimeria chalumnae to the extent of about 1.7 percent by weight. It was determined quantitatively by reaction with 1-phenyl-1,2-propanedione-2-oxime (Archibald reagent) and by measurement of ammonia released upon treatment with urease. Arginase and ornithine carbamoyltransferase, enzymes instrumental in the formation of urea in typical ureotelic vertebrates, occur in homogenates of coelacanth liver. Formed in part by the ornithine-urea cycle, urea may have an osmoregulatory function in the coelacanth as it has in elasmobranchs.
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PMID:Urea and its formation in coelacanth liver. 601 72

A cDNA for beta-alanine synthase from rat liver has been isolated, sequenced, and characterized. beta-Alanine synthase clones were isolated from rat liver cDNA libraries in lambda gt11, using affinity-purified polyclonal antibodies against beta-alanine synthase protein. beta-Alanine synthase protein was not expressed with equal efficiency by all clones. One of the expressed fusion proteins has normal specific enzyme activity, and a second has reduced specific activity. Both clones were completely sequenced and yielded identical DNA sequence, except that one clone contained an additional 36 bases of 5' sequence. The various clones of this cDNA code for an EcoRI insert of 1.5 +/- 0.1 kb, and the open reading frame corresponds to a protein of 393 amino acids (M(r) = 44,042), in good agreement with the M(r) of approximately 42,000 for the native enzyme on SDS-gel electrophoresis. An 11-amino acid sequence was obtained from a tryptic peptide of native beta-alanine synthase; 11 codons for these same amino acids were found at the expected site in the sequenced cDNA, and confirm the open reading frame of the beta-alanine synthase cDNA. Chemical analysis of the native enzyme shows 2 zinc atoms per subunit, and the sequence of beta-alanine synthase contains 2 putative zinc-binding site motifs. Comparison of amino acid sequence, deduced from the cDNA sequence, to sequences in the protein data base showed that it is a unique sequence and that it has about 20% identity to aspartate carbamoyltransferase, ornithine carbamoyltransferase, urease, and leucine aminopeptidase; enzymes that bind comparable ligands or have a similar mechanism.
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PMID:Cloning, sequencing, and expression of a cDNA encoding beta-alanine synthase from rat liver. 844 31

Slackia exigua ATCC 700122(T) and Cryptobacterium curtum ATCC 700683(T) were our isolates from infected root canal and human periodontal pocket, respectively; they are asaccharolytic anaerobic gram-positive rods, which are predominant in the oral cavity. They utilize arginine, so our aim was to investigate the pathway of arginine degradation. Metabolic end products were determined with high-performance liquid chromatography. The related enzymatic activities in cell-free extract were also assayed. Both S. exigua and C. curtum degraded arginine and produced substantial amounts of citrulline, ornithine and ammonia. Arginine and citrulline supported the growth of both strains. As the related enzymatic activities, arginine deiminase, ornithine carbamoyltransferase and carbamate kinase activities were detected in the cell-free extract of S. exigua and C. curtum. Arginase and urease activities were not detected in either organism. These results suggest that arginine was metabolized by the arginine deiminase pathway. Both S. exigua and C. curtum degrade arginine via the arginine deiminase pathway.
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PMID:Degradation of arginine by Slackia exigua ATCC 700122 and Cryptobacterium curtum ATCC 700683. 1706 96