Properties and crystallization of a genetically engineered, water-soluble derivative of penicillin-binding protein 5 of Escherichia coli K12
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1988.tb13751.x/fullpdf
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1. Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12.
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3. Occurrence of a serine residue in the penicillin-binding site of the exocellular DD-carboxy-peptidase-transpeptidase fromStreptomycesR61
4. Penicillinase active sites: Labelling of serine-44 in β-lactamase I by 6β-bromopenicillanic acid
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