Membrane penicillinase of Bacillus licheniformis 749/C:sequence and possible repeated tetrapeptide structure of the phospholipopeptide region.
AUTOR(ES)
Yamamoto, S
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=430315Documentos Relacionados
- Lipoprotein nature of Bacillus licheniformis membrane penicillinase.
- Immunoelectron microscopic double labeling of alkaline phosphatase and penicillinase with colloidal gold in frozen thin sections of Bacillus licheniformis 749/C.
- Alkaline phosphatase secretion-negative mutant of Bacillus licheniformis 749/C.
- Cloning and nucleotide sequence of the penicillinase antirepressor gene penJ of Bacillus licheniformis.
- The penicillinase of Bacillus licheniformis is an outer membrane protein in Escherichia coli.