Conservation of primary structure of the pyridoxyl peptide of Escherichia coli and Serratia marcescens tryptophan synthase beta2 protein

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Abstract
Two labeled peptides were recovered from tryptic digests of the NaB3H4-reduced, performic acid-oxidized .beta.2 protein of S. marcescens tryptophan synthase [EC 4.2.1.20]. These two pyridoxyl peptides were identical except for the presence or absence of an NH2-terminal arginyl residue. Tryptic digestion of nonreduced, performic acid-oxidized protein allowed isolation of the peptides that comprise the 2 halves of the pyridoxyl peptide. The partial primary structure for this region of the protein was Arg-Glx-Asx-Leu-Leu-His(Gly,Gly,Ala,His)Lys(Pxy)-Thr-Asx-Glx-Val(Leu,Gly,Glx,Ala,Leu,Leu,Ala)Lys. All the data available indicate that the sequence is identical with the homologous region from the E. coli enzyme.