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. 1981

T Mizuno

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.

UI MeSH Term Description Entries
D008074 Lipoproteins Lipid-protein complexes involved in the transportation and metabolism of lipids in the body. They are spherical particles consisting of a hydrophobic core of TRIGLYCERIDES and CHOLESTEROL ESTERS surrounded by a layer of hydrophilic free CHOLESTEROL; PHOSPHOLIPIDS; and APOLIPOPROTEINS. Lipoproteins are classified by their varying buoyant density and sizes. Circulating Lipoproteins,Lipoprotein,Lipoproteins, Circulating
D010457 Peptidoglycan A structural polymer of the bacterial cell envelope consisting of sugars and amino acids which is responsible for both shape determination and cellular integrity under osmotic stress in virtually all bacteria. Murein,Pseudomurein
D011509 Proteoglycans Glycoproteins which have a very high polysaccharide content. Proteoglycan,Proteoglycan Type H
D011513 Proteus mirabilis A species of gram-negative, facultatively anaerobic, rod-shaped bacteria that is frequently isolated from clinical specimens. Its most common site of infection is the urinary tract.
D002268 Carboxypeptidases Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue. Carboxypeptidase
D003545 Cysteine A thiol-containing non-essential amino acid that is oxidized to form CYSTINE. Cysteine Hydrochloride,Half-Cystine,L-Cysteine,Zinc Cysteinate,Half Cystine,L Cysteine
D005227 Fatty Acids Organic, monobasic acids derived from hydrocarbons by the equivalent of oxidation of a methyl group to an alcohol, aldehyde, and then acid. Fatty acids are saturated and unsaturated (FATTY ACIDS, UNSATURATED). (Grant & Hackh's Chemical Dictionary, 5th ed) Aliphatic Acid,Esterified Fatty Acid,Fatty Acid,Fatty Acids, Esterified,Fatty Acids, Saturated,Saturated Fatty Acid,Aliphatic Acids,Acid, Aliphatic,Acid, Esterified Fatty,Acid, Saturated Fatty,Esterified Fatty Acids,Fatty Acid, Esterified,Fatty Acid, Saturated,Saturated Fatty Acids
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001425 Bacterial Outer Membrane Proteins Proteins isolated from the outer membrane of Gram-negative bacteria. OMP Proteins,Outer Membrane Proteins, Bacterial,Outer Membrane Lipoproteins, Bacterial
D043422 Carboxypeptidases A Carboxypeptidases that are primarily found the DIGESTIVE SYSTEM that catalyze the release of C-terminal amino acids. Carboxypeptidases A have little or no activity for hydrolysis of C-terminal ASPARTIC ACID; GLUTAMIC ACID; ARGININE; LYSINE; or PROLINE. This enzyme requires ZINC as a cofactor and was formerly listed as EC 3.4.2.1 and EC 3.4.12.2. Carboxypeptidase A,Carboxypeptidase A1,Carboxypeptidase A2,Carboxypeptidase A5,PCPA1 Enzyme,PCPA2 Enzyme,Procarboxypeptidase A,Procarboxypeptidase A1,Procarboxypeptidase A2

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