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| Reference : The Dmpa Aminopeptidase from Ochrobactrum Anthropi Lmg7991 Is the Prototype of a New Ter... |
| Scientific journals : Article | |||
| Life sciences : Biochemistry, biophysics & molecular biology | |||
| http://hdl.handle.net/2268/106946 | |||
| The Dmpa Aminopeptidase from Ochrobactrum Anthropi Lmg7991 Is the Prototype of a New Terminal Nucleophile Hydrolase Family | |
| English | |
| Fanuel, L. [> > > >] | |
Goffin, Colette  [Université de Liège - ULg > > Centre d'ingénierie des protéines >] | |
| Cheggour, A. [> > > >] | |
| Devreese, B. [> > > >] | |
| Van Driessche, G. [> > > >] | |
| Joris, Bernard [Université de Liège - ULg > > Centre d'ingénierie des protéines >] | |
| Van Beeumen, J. [> > > >] | |
| Frère, Jean-Marie [Université de Liège - ULg > Département des sciences de la vie > Département des sciences de la vie >] | |
| 1-Jul-1999 | |
| Biochemical Journal | |
| 341 | |
| (Pt 1) | |
| 147-55 | |
| International | |
| 0264-6021 | |
| [en] The DmpA (d-aminopeptidase A) protein produced by Ochrobactrum anthropi hydrolyses p-nitroanilide derivatives of glycine and d-alanine more efficiently than that of l-alanine. When regular peptides are utilized as substrates, the enzyme behaves as an aminopeptidase with a preference for N-terminal residues in an l configuration, thus exemplifying an interesting case of stereospecificity reversal. The best-hydrolysed substrate is l-Ala-Gly-Gly, but tetra- and penta-peptides are also efficiently hydrolysed. The gene encodes a 375-residue precursor, but the active enzyme contains two polypeptides corresponding to residues 2-249 (alpha-subunit) and 250-375 (beta-subunit) of the precursor. Residues 249 and 250 are a Gly and a Ser respectively, and various substitutions performed by site-directed mutagenesis result in the production of an uncleaved and inactive protein. The N-terminal Ser residue of the beta-subunit is followed by a hydrophobic peptide, which is predicted to form a beta-strand structure. All these properties strongly suggest that DmpA is an N-terminal amidohydrolase. An exploration of the databases highlights the presence of a number of open reading frames encoding related proteins in various bacterial genomes. Thus DmpA is very probably the prototype of an original family of N-terminal hydrolases. | |
| http://hdl.handle.net/2268/106946 |
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