Membrane penicillinase of Bacillus licheniformis 749/C:sequence and possible repeated tetrapeptide structure of the phospholipopeptide region.
نویسندگان
چکیده
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.
منابع مشابه
Further evidence for a partially folded intermediate in penicillinase secretion by Bacillus licheniformis.
Protoplasis of Bacillus licheniformis 749/C (a mutant constitutive for penicillinase production) continued to synthesize and release penicillinase in hypertonic growth medium in the presence of trypsin and chymotrypsin at 25 mug each per ml. When the protoplasts were stripped of about half of their membrane-bound penicillinase by pretreatment at pH 9.5 or with a higher level of trypsin, penicil...
متن کاملMorphological phenomena associated with penicillinase induction and secretion in Bacillus licheniformis.
Cells of uninduced Bacillus licheniformis (strain 749) in mid-logarithmic phase have no extensive intracytoplasmic membrane. After induction with cephalosporin C, characteristic organelles that contain tubules and vesicles with single-layered membranes and no visible internal substructure can be seen in thin sections in the periplasm. A magnoconstitutive penicillinase producer (749/C) contains ...
متن کاملPurification and characteristics of plasma membrane penicillinase from Bacillus licheniformis 749-C.
The plasma membrane-bound penicillinase of Bacillus licheniformis 749/C has been purified from bacteria grown in a medium containing [2-3H]glycerol and W-labeled aminoacids, and the purified enzyme compared with exopenicillinase. The procedure consisted of repeated chromatography on DEAE-Sephadex in the presence of Triton X-100, and gel filtration on Sephadex G-75 in the presence of taurodeoxyc...
متن کاملPurification of plasma membrane penicillinase from Bacillus licheniformis 749/C and comparison with exoenzyme.
The membrane penicillinase of Bacillus licheniformis 749/C has been demonstrated to be a phospholipoprotein. The homogeneous enzyme gives a positive reaction for phosphorous and for unsaturated fatty acids, has a molecular weight of 33,000 in contrast to 29,000 for the exoenzyme, and contains 8 to 9 additional residues of aspartate or asparagine, 4 to 5 of serine, 7 of glutamate or glutamine, a...
متن کاملImmunoelectron microscopic localization of penicillinase in Bacillus licheniformis.
Penicillinase was localized in log-phase cells of Bacillus licheniformis 749/C by labeling with ferritin-anti-penicillinase immunoglobulin G conjugate. Mildly fixed homogenized cells, isolated subcellular fractions, and frozen thin sections were labeled. The label was distributed in discrete patches in the cell envelope. The patches extended from the inside part of the membrane to the outside p...
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ورودعنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 73 5 شماره
صفحات -
تاریخ انتشار 1976