3q98

Publication Abstract from PubMed

The allantoin degradation pathway in E. coli has long been thought to involve a putative novel oxamate transcarbamylase (OXTCase) that converts oxaluric acid to oxamate and carbamyl phosphate (CP), a substrate for carbamate kinase (CK). In the genome sequence of E. coli, the only gene that could encode a novel transcarbamylase is the ygeW gene. However, the recombinant protein has no transcarbamylase activity with oxamate, allantoin, or twenty five other related compounds as potential substrates. The crystal structures of this transcarbamylase with unknown function (UTCase) has been determined and refined at 2.0 A resolution, providing structural insights into its possible function. Like N-acetyl-L-ornithine transcarbamylase and N-succinyl-L-transcarbamylase, UTCase has a deep 3(1) trefoil knot close to the active site, in contrast to aspartate transcarbamylase and ornithine transcarbamylase which do not have a knot. A Blast search of completed genomes indicates that 52 species including one non-bacterial species, Trichomonas vaginalis G3, have the ygeW gene. Gene context analysis and the structure of UTCase suggest that it is probably an ancestral catabolic transcarbamylase.

The ygeW encoded protein from Escherichia coli is a knotted ancestral catabolic transcarbamylase.,Li Y, Jin Z, Yu X, Allewell NM, Tuchman M, Shi D Proteins. 2011 Jul;79(7):2327-34. doi: 10.1002/prot.23043. Epub 2011 May 9. PMID:21557323^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.