PMID:10913105
| Citation |
Maynes, JT, Yuan, RG and Snyder, FF (2000) Identification, expression, and characterization of Escherichia coli guanine deaminase. J. Bacteriol. 182:4658-60 |
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| Abstract |
Using the human cDNA sequence corresponding to guanine deaminase, the Escherichia coli genome was scanned using the Basic Local Alignment Search Tool (BLAST), and a corresponding 439-residue open reading frame of unknown function was identified as having 36% identity to the human protein. The putative gene was amplified, subcloned into the pMAL-c2 vector, expressed, purified, and characterized enzymatically. The 50.2-kDa protein catalyzed the conversion of guanine to xanthine, having a K(m) of 15 microM with guanine and a k(cat) of 3.2 s(-1). The bacterial enzyme shares a nine-residue heavy metal binding site with human guanine deaminase, PG[FL]VDTHIH, and was found to contain approximately 1 mol of zinc per mol of subunit of protein. The E. coli guanine deaminase locus is 3' from an open reading frame which shows homology to a bacterial purine base permease. |
| Links | |
| Keywords |
Amino Acid Sequence; Cloning, Molecular; DNA, Complementary; Escherichia coli/enzymology; Escherichia coli/genetics; Guanine Deaminase/chemistry; Guanine Deaminase/genetics; Guanine Deaminase/metabolism; Humans; Kinetics; Molecular Sequence Data; Open Reading Frames; Sequence Alignment; Sequence Homology, Amino Acid |
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