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Updated: Aug 3, 2026

Enrichment of Bacterial Lipoproteins and Preparation of N-terminal Lipopeptides for Structural Determination by Mass Spectrometry
10:59

Enrichment of Bacterial Lipoproteins and Preparation of N-terminal Lipopeptides for Structural Determination by Mass Spectrometry

Published on: May 21, 2018

Membrane penicillinase of Bacillus licheniformis 749/C:sequence and possible repeated tetrapeptide structure of the

S Yamamoto, J O Lampen

    Proceedings of the National Academy of Sciences of the United States of America
    |May 1, 1976
    PubMed

    Insights

    Bacillus licheniformis membrane penicillinase is a phospholipoprotein intermediate. It contains a unique NH2-terminal amino acid chain and phosphatidylserine, absent in the final exoenzyme.

    Area of Science:

    • Biochemistry
    • Microbiology
    • Enzymology

    Background:

    • Penicillinase is crucial for bacterial resistance.
    • Bacillus licheniformis produces extracellular penicillinase (exoenzyme).
    • The membrane-bound form is a potential intermediate.

    Purpose of the Study:

    • To characterize the membrane penicillinase from Bacillus licheniformis 749/C.
    • To identify structural differences between membrane and exoenzyme forms.

    Main Methods:

    • Biochemical analysis of purified membrane penicillinase.
    • Amino acid sequencing of the NH2-terminal chain.
    • Lipid analysis to identify associated phospholipids.

    Main Results:

    • The membrane penicillinase is a phospholipoprotein.
    • It possesses an NH2-terminal chain of 24 amino acids (Ser, Gly, Asp, Asn, Glu, Gln).
    • A phosphatidylserine component is present, which is absent in the exoenzyme.

    Conclusions:

    • The membrane penicillinase represents a precursor or intermediate form.
    • Phosphatidylserine and the specific NH2-terminal chain are distinguishing features of this intermediate.
    • Understanding these differences aids in elucidating penicillinase biogenesis and secretion.

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