PMID:10930738: Difference between revisions

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<span style = 'font-size: large'> '''von Rechenberg, M and Höltje, JV'''  (2000) Two-step procedure for purification and separation of the essential penicillin-binding proteins PBP 1A and 1Bs of Escherichia coli.''FEMS Microbiol. Lett.'' '''189''':201-4</span>
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'''von Rechenberg, M and Höltje, JV'''  (2000) Two-step procedure for purification and separation of the essential penicillin-binding proteins PBP 1A and 1Bs of Escherichia coli. ''FEMS Microbiol. Lett.'' '''189''':201-4
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!align=left  |Abstract
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The penicillin-binding proteins PBP 1A and 1Bs are the essential murein polymerases of Escherichia coli. Purification of these membrane-bound bifunctional transglycosylase-transpeptidases was a major obstacle in studying the details of both enzymatic reactions. Here we describe a simple, highly specific affinity chromatography method that takes advantage of the availability of the specific inhibitor of the transglycosylase site moenomycin A in order to enrich PBP 1A and 1Bs in one step from crude membrane preparations. Separation of PBP 1A from PBP 1Bs is achieved in a second step employing cation exchange chromatography yielding enzymatically active native murein polymerases.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=10930738 PubMed]


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|{{TableHeadingColor}} |'''Abstract''' || The penicillin-binding proteins PBP 1A and 1Bs are the essential murein polymerases of Escherichia coli. Purification of these membrane-bound bifunctional transglycosylase-transpeptidases was a major obstacle in studying the details of both enzymatic reactions. Here we describe a simple, highly specific affinity chromatography method that takes advantage of the availability of the specific inhibitor of the transglycosylase site moenomycin A in order to enrich PBP 1A and 1Bs in one step from crude membrane preparations. Separation of PBP 1A from PBP 1Bs is achieved in a second step employing cation exchange chromatography yielding enzymatically active native murein polymerases.
!align=left  |Keywords
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Bacterial Proteins; Carrier Proteins; Escherichia coli/metabolism; Hexosyltransferases/isolation & purification; Hexosyltransferases/metabolism; Multienzyme Complexes/isolation & purification; Multienzyme Complexes/metabolism; Muramoylpentapeptide Carboxypeptidase; Penicillin-Binding Proteins; Peptidyl Transferases/isolation & purification; Peptidyl Transferases/metabolism
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=10930738 PubMed]
 
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Latest revision as of 04:13, 15 September 2013

Citation

von Rechenberg, M and Höltje, JV (2000) Two-step procedure for purification and separation of the essential penicillin-binding proteins PBP 1A and 1Bs of Escherichia coli. FEMS Microbiol. Lett. 189:201-4

Abstract

The penicillin-binding proteins PBP 1A and 1Bs are the essential murein polymerases of Escherichia coli. Purification of these membrane-bound bifunctional transglycosylase-transpeptidases was a major obstacle in studying the details of both enzymatic reactions. Here we describe a simple, highly specific affinity chromatography method that takes advantage of the availability of the specific inhibitor of the transglycosylase site moenomycin A in order to enrich PBP 1A and 1Bs in one step from crude membrane preparations. Separation of PBP 1A from PBP 1Bs is achieved in a second step employing cation exchange chromatography yielding enzymatically active native murein polymerases.

Links

PubMed

Keywords

Bacterial Proteins; Carrier Proteins; Escherichia coli/metabolism; Hexosyltransferases/isolation & purification; Hexosyltransferases/metabolism; Multienzyme Complexes/isolation & purification; Multienzyme Complexes/metabolism; Muramoylpentapeptide Carboxypeptidase; Penicillin-Binding Proteins; Peptidyl Transferases/isolation & purification; Peptidyl Transferases/metabolism

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