carboxypeptidase-b and glycerylcysteine

carboxypeptidase-b has been researched along with glycerylcysteine* in 1 studies

Other Studies

1 other study(ies) available for carboxypeptidase-b and glycerylcysteine

ArticleYear
Structure of the peptidoglycan-associated lipoprotein (PAL) of the Proteus mirabilis outer membrane. II. Sequence of the amino-terminal part of the peptidoglycan-associated lipoprotein.
    Journal of biochemistry, 1981, Volume: 89, Issue:4

    The amino acid of the lipooligopeptide (LOP) derived from the N-terminal region of the peptidoglycan-associated lipoprotein (PAL) of Proteus mirabilis was determined to be [X]-Ser-Ser-Asn-Lys. An unidentified compound[X] present at the N-terminus was identified as glycerylcysteine [S-(propane-2,'3'-diol)-3-thio, 2-amino-propanoic acid]. The partial amino acid sequence of the lipopolypeptide (LPP), which contained the lipooligopeptide (LOP) at its N-terminal part, was also determined, mainly by Edman-degradation. The structure of the N-terminal part of PAL was determined to be [3 Fatty acids approximately glycerylcysteine-Ser-Ser-Asn-Lys-Asn-Asp-Asp-Glu-Thr-Asp-Thr-Ser...]. The structure of PAL is discussed in comparison with Braun's lipoprotein.

    Topics: Amino Acid Sequence; Bacterial Outer Membrane Proteins; Carboxypeptidase B; Carboxypeptidases; Carboxypeptidases A; Cysteine; Escherichia coli Proteins; Fatty Acids; Lipoproteins; Peptidoglycan; Proteoglycans; Proteus mirabilis

1981