About: Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases

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About: Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases Goto Sponge NotDistinct Permalink

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scientific article published on June 1979

Attributes	Values
rdf:type	Item
description	videnskabelig artikel (da) article científic (ca) articolo scientifico (it) artigo científico (pt) bilimsel makale (tr) vedecký článok (sk) vetenskaplig artikel (sv) vědecký článek (cs) wetenschappelijk artikel (nl) wissenschaftlicher Artikel (de) научни чланак (sr) article scientifique (fr) artículu científicu espublizáu en 1979 (ast) 1979年學術文章 (zh) наукова стаття, опублікована в червні 1979 (uk) مقالة علمية نشرت في يونيو 1979 (ar) scientific article published on June 1979 (en)
publication date	wds:Q37333017-51FBCB2F-C4CF-4C15-AA2D-1DC9EE2D1D44
publication date	1979-06-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q37333017-93D8D9CC-463A-4312-BD9D-01C7C197E979
language of work or name	English
cites work	wds:Q37333017-02CC8BAF-8FBA-4EBF-ACF4-44185408B9C6 wds:Q37333017-04FE80FA-DC4C-495B-BE98-9F7A7FF78D89 wds:Q37333017-0B989F1A-DEF9-4492-9F53-B1B86CE96D8D wds:Q37333017-1B44589C-E711-4E7D-AB93-862ACD5EBCD0 wds:Q37333017-1DCC15DB-626B-4AB7-831D-0302C812A016 wds:Q37333017-423D3E6C-A7B4-484D-939B-F29ADF31C5E8 wds:Q37333017-5AAA0F3B-083A-4E26-874B-F73AEE537889 wds:Q37333017-5AF90F0C-BB7F-4ABA-91DA-2513F9C5922E wds:Q37333017-5C3B2FF5-2330-41FB-9323-054AE98BCF63 wds:Q37333017-62A7B5C5-D35F-440E-ACBA-4D6984DB3F65 wds:Q37333017-651BE851-3F98-4525-9377-4E99809D88FB wds:Q37333017-7269A6D2-2DFC-46B7-B994-AD98998A39F1 wds:Q37333017-7CAC94DF-4419-4EE8-8146-E4877DE475DC wds:Q37333017-7F2556F7-4498-4F84-8562-43E783D2C456 wds:Q37333017-94624C06-FB7C-44E1-8550-37F1918C2D40 wds:Q37333017-98E18D70-CEFB-4709-8B2C-794F0AB0D302 wds:Q37333017-AD99767B-1469-4BA4-B89B-1BA619181007 wds:Q37333017-B095CA5E-5871-4579-AADC-ED80DD8E16DD wds:Q37333017-C2BEC683-8726-42FB-809C-396EFE20B14E wds:Q37333017-D2AC8AAE-9840-4283-9C06-20E0DBFEB5A3 wds:Q37333017-D4F1673E-E8CC-41A8-ADA9-09E8330FCB13 wds:Q37333017-D52096C5-D7AB-4E08-89EF-59CABB2D412A wds:Q37333017-F62A0863-FBD1-4DAC-8716-1209576194C4 wds:Q37333017-F981F178-1EFF-4028-86FA-834A98BABF6F wds:Q37333017-FA534E08-1F08-4B4D-B700-CB846F99ADD3
cites work	Biosynthesis of the peptidoglycan of bacterial cell walls. 8. Peptidoglycan transpeptidase and D-alanine carboxypeptidase: penicillin-sensitive enzymatic reaction in strains of Escherichia coli. Conformation of penicillin as a transition-state analog of the substrate of peptidoglycan transpeptidase. Penicillin: its basic site of action as an inhibitor of a peptide cross-linking reaction in cell wall mucopeptide synthesis 6-beta-bromopenicillanic acid, a potent beta-lactamase inhibitor Penicillinase active sites: Labelling of serine-44 in β-lactamase I by 6β-bromopenicillanic acid The nature of the binding of penicillin by bacterial cells Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine Interaction of penicillin with the bacterial cell: penicillin-binding proteins and penicillin-sensitive enzymes. The penicillin receptor in Streptomyces Biosynthesis of the peptidoglycan of bacterial cell walls. XV. The binding of radioactive penicillin to the particulate enzyme preparation of Bacillus subtilis and its reversal with hydroxylamine or thiols. Purification and characterization of the thermophilic D-alanine carboxypeptidase from membranes of Bacillus stearothermophilus. A membrane enzyme from Staphylococcus aureus which catalyzes transpeptidase, carboxypeptidase, and penicillinase activities Kinetic evidence for an acyl-enzyme intermediate in D-alanine carboxypeptidases of Bacillus subtilis and Bacillus stearothermophilus Primary structure of the λ repressor Purification to homogeneity and properties of two D-alanine carboxypeptidases I From Escherichia coli Transition state structures of a dipeptide related to the mode of action of beta-lactam antibiotics Degradation of penicillin G to phenylacetylglycine by D-alanine carboxypeptidase from Bacillus stearothermophilus Effects of sulfhydryl reagents on the binding and release of penicillin G by D-alanine carboxypeptidase IA of Escherichia coli Utilization of a depsipeptide substrate for trapping acyl—enzyme intermediates of penicillin-sensitive D-alanine carboxypeptidases Occurrence of a serine residue in the penicillin-binding site of the exocellular DD-carboxy-peptidase-transpeptidase from Streptomyces R61 Effects of nucleophiles on the breakdown of the benzylpenicilloyl–enzyme complex EI formed between benzylpenicillin and the exocellular DD-carboxypeptidase–transpeptiase of Streptomyces strain R61 Fragmentation of benzylpenicillin after interaction with the exocellular DD-carboxypeptidase-transpeptidases of Streptomyces R61 and R39 Isolation of the penicillin-binding peptide from D-alanine carboxypeptidase of Bacillus subtilis Binding of (14C)penicillin G to the membrane-bound and the purified D-alanine carboxypeptidases from Bacillus stearothermophilus and Bacillus subtilis and its release. Hydroxylaminolysis of penicillin binding componenets is enzymatically catalyzed
author name string	wds:Q37333017-1F01969A-2AD5-46AA-B040-EFA5495AFFC1 wds:Q37333017-9B9B41B2-9CBD-4DE4-90E8-14FCB6564A1F
author name string	Rasmussen JR Yocum RR
rdfs:label	Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases (en) Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases (nl) Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases (ast)
skos:prefLabel	Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases (en) Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases (nl) Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases (ast)
name	Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases (en) Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases (nl) Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases (ast)
author	wds:Q37333017-BB56EAE2-F43F-448A-A73F-97481B15D613 wds:Q37333017-D59F0E0E-5CF6-4D1C-9B85-068EDC98A72A
author	Jack L. Strominger David J. Waxman
title	wds:Q37333017-3D1E0B47-A251-40BB-8358-BC81C2BAD262
title	Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases (en)
page(s)	wds:Q37333017-D3D2A415-CCD7-4A0B-9E19-DE27D6A6A4B6
page(s)	2730-2734
instance of	wds:Q37333017-D5E76E03-3071-41D9-897A-1C7FAB130918
instance of	scholarly article
main subject	wds:Q37333017-CC5AA436-8071-41F4-A97C-AACAEA16A663
main subject	medication
PubMed ID	wds:Q37333017-866DF210-E7C7-49A4-BD86-948F4CAC467D
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/111240
PubMed ID	111240

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