tailieunhanh - Báo cáo khoa học: Deamidation of labile asparagine residues in the autoregulatory sequence of human phenylalanine hydroxylase

Two dimensional electrophoresis has revealed a micro-heterogeneity in the recombinant human phenylalanine hydroxylase (hPAH) protomer,that is the result of sponta-neous nonenzymatic deamidations of labile asparagine (Asn) residues [Solstad,T. and Flatmark,T. (2000)Eur. J. –6310]. Using of a computer algorithm, the relative deamidation rates of all Asn residues in hPAH havebeenpredicted,andwehere verify thatAsn32,followed by a glycine residue,as well as Asn28 and Asn30 in a loop region of the N-terminal autoregulatory sequence (residues 19–33) of wt-hPAH,are among the susceptible residues | Eur. J. Biochem. 270 929-938 2003 FEBS 2003 doi Deamidation of labile asparagine residues in the autoregulatory sequence of human phenylalanine hydroxylase Structural and functional implications Therese Solstad1 Raquel N. Carvalho1 Ole A. Andersen2 Dietmar Waidelich3 and Torgeir Flatmark1 1Department of Biochemistry and Molecular Biology and the Proteomic Unit University of Bergen Norway department of Chemistry University of Troms0 Norway 3Applied Biosystems Applera Deutschland GmbH Langen Germany Two dimensional electrophoresis has revealed a microheterogeneity in the recombinant human phenylalanine hydroxylase hPAH protomer that is the result 4 spontaneous nonenzymatic deamidations of labile asparagine Asn residues Solstad T. and Elatmark. T. 2000 Eur. J. Biochem. 267 6302 63IO. Thing of a computer algorithm the relative deamidation rates of all Asn residues in hPAH have been predicted and we here verify that Asn32. folhweed by a glycine residue as well as Ann28 and Asn3 m a hoop region of the N-terminal autoregulatory sequence residues 19-33 of wt-hPAH are amnng die seihoptilhe resideies. First nn MALDI-TOF mass spectrometry ff die 44 h expressed enzyme the E. coli 22-residue peptide L15-K42 containing three Asn residues was recovered with four monoisotopic mass numbers . m z of and of etec. l easinn intenstty that dii tel eel by 1 La. Secondly by reverse-phase chromatography isoaspartyl isoAsp was demonstrated in this 28-residue peptide by its methylation by protein-L-isoaspartic acid O-methyltransferase PIMT EC . Thirdly on incubation at pH and 37 C of the phosphorylated form at Ser16 of this 28-residue peptide a time-dependent mobility shift from tR w 34 min to w 31 min . to a more hydrophilic position was observed on reverse-phase chromatography nnd the reo-oe-en of the tR w 34 min species decreased with a biphasic time-codase with of and days. The .

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