Specificity and reversibility of the transpeptidation reaction catalyzed by the Streptomyces R61 D-Ala-D-Ala peptidase.

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A computational evaluation of the mechanism of penicillin-binding protein-catalyzed cross-linking of the bacterial cell wall Recognition of corn defense chitinases by fungal polyglycine hydrolases.

P2860

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P2860

Specificity and reversibility of the transpeptidation reaction catalyzed by the Streptomyces R61 D-Ala-D-Ala peptidase.

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http://www.wikidata.org/entity/Q42282051

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2005 nî lūn-bûn

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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2005年论文

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2005年论文

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name

Specificity and reversibility ...... ces R61 D-Ala-D-Ala peptidase.

@en

Specificity and reversibility ...... ces R61 D-Ala-D-Ala peptidase.

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type

Item

label

Specificity and reversibility ...... ces R61 D-Ala-D-Ala peptidase.

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Specificity and reversibility ...... ces R61 D-Ala-D-Ala peptidase.

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prefLabel

Specificity and reversibility ...... ces R61 D-Ala-D-Ala peptidase.

@en

Specificity and reversibility ...... ces R61 D-Ala-D-Ala peptidase.

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P1476

Specificity and reversibility ...... ces R61 D-Ala-D-Ala peptidase.

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P2093

Eric Sauvage

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Françoise Jacquemotte

http://www.w3.org/2001/XMLSchema#string

Jean-Marie Frère

http://www.w3.org/2001/XMLSchema#string

Kris Devriendt

http://www.w3.org/2001/XMLSchema#string

Léon Ghosez

http://www.w3.org/2001/XMLSchema#string

Michael Delmarcelle

http://www.w3.org/2001/XMLSchema#string

Noureddine Rhazi

http://www.w3.org/2001/XMLSchema#string

Valérie Tallon

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P2860

Structures of two kinetic intermediates reveal species specificity of penicillin-binding proteins

The crystal structure of phosphonate-inhibited D-Ala-D-Ala peptidase reveals an analogue of a tetrahedral transition state

The beta-lactamase of Enterobacter cloacae P99. Chemical properties, N-terminal sequence and interaction with 6 beta-halogenopenicillanates

Inhibition of metallo-beta-lactamases by a series of mercaptoacetic acid thiol ester derivatives.

Toward better antibiotics: crystallographic studies of a novel class of DD-peptidase/beta-lactamase inhibitors.

Accumulation of acyl-enzyme in DD-peptidase-catalysed reactions with analogues of peptide substrates.

On the substrate specificity of bacterial DD-peptidases: evidence from two series of peptidoglycan-mimetic peptides

Kinetics of concomitant transfer and hydrolysis reactions catalysed by the exocellular DD-carboxypeptidase-transpeptidase of streptomyces R61.

The importance of the negative charge of beta-lactam compounds in the interactions with active-site serine DD-peptidases and beta-lactamases.

Streptomyces DD-carboxypeptidases as transpeptidases. The specificity for amino compounds acting as carboxyl acceptors.

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2922-2928

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scholarly article

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10.1110/PS.051641005

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2005-09-30T00:00:00Z

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229935462

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16199665

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2253218

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Specificity and reversibility of the transpeptidation reaction catalyzed by the Streptomyces R61 D-Ala-D-Ala peptidase.

about

P2860

P2860

Specificity and reversibility of the transpeptidation reaction catalyzed by the Streptomyces R61 D-Ala-D-Ala peptidase.

description

name

type

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P1433

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P2860

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