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PMID: 775489 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

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

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 73 ·No. 5 ·1976-05-00 ·Pages 1457-61

Yamamoto S, Lampen JO

Abstract

The membrane penicillinase (EC 3.5.2.6; penicillin amido-beta-lactamhydrolase) of Bacillus licheniforis 749/C, which appears to be an intermediate in the formation of the exoenzyme, is a phospholipoprotein that carries an NH2-terminal chain of 24 amino acids (only serine, glycine, aspartic acid, asparagine, glutamic acid, and glutamine) and a phosphatidylserine that is not present in the exoenzyme.

MeSH Terms

Amino Acid Sequence Apoproteins/analysis Bacillus/enzymology,ultrastructure Cell Membrane/enzymology Lipoproteins/analysis Papain Penicillinase/analysis,metabolism Pepsin A Phospholipids/analysis

Chemicals

Apoproteins Lipoproteins Phospholipids Papain Pepsin A Penicillinase

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Yamamoto S

Lampen J O

References (16)

16 references, click to expand

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In vitro synthesis of hydrophobic penicillinase in extracts of Bacillus licheniforms 749/C.
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Membrane penicillinase of Bacillus licheniformis 749/C, a phospholipoprotein.
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Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.73.5.1457

Published

1976-05-00

Pages

1457-61

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC430315

Subset

External Links

PubMed source DOI: 10.1073/pnas.73.5.1457 PMC Full Text View journal details

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

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