Protonation states of active-site lysines of penicillin-binding protein 6 from Escherichia coli and the mechanistic implications.

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Co-solvents as stabilizing agents during heterologous overexpression in Escherichia coli - application to chlamydial penicillin-binding protein 6.Computation of pH-dependent binding free energies.Mechanisms of proton relay and product release by Class A β-lactamase at ultrahigh resolution.

P2860

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P2860

Protonation states of active-site lysines of penicillin-binding protein 6 from Escherichia coli and the mechanistic implications.

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http://www.wikidata.org/entity/Q40696079

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2014 nî lūn-bûn

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

@zh-hk

2014年論文

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2014年論文

@zh-tw

2014年论文

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2014年论文

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2014年论文

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name

Protonation states of active-s ...... the mechanistic implications.

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type

Item

label

Protonation states of active-s ...... the mechanistic implications.

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prefLabel

Protonation states of active-s ...... the mechanistic implications.

@en

P1476

Protonation states of active-s ...... d the mechanistic implications

@en

P2093

Malika Kumarasiri

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Qicun Shi

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

Shahriar Mobashery

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

Weilie Zhang

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P2860

Crystal Structures of Complexes of Bacterial dd-Peptidases with Peptidoglycan-Mimetic Ligands: The Substrate Specificity Puzzle

Crystal Structures of Penicillin-Binding Protein 6 from Escherichia coli

Crystal structure of a complex between the Actinomadura R39 DD-peptidase and a peptidoglycan-mimetic boronate inhibitor: interpretation of a transition state analogue in terms of catalytic mechanism

Structural Insights into the Recovery of Aldolase Activity inN-Acetylneuraminic Acid Lyase by Replacement of the Catalytically Active Lysine with γ-Thialysine by Using a Chemical Mutagenesis Strategy

Calculations of electrostatic interactions in biological systems and in solutions

Peptidoglycan structure and architecture

Proton binding to proteins: pK(a) calculations with explicit and implicit solvent models.

Contribution of membrane-binding and enzymatic domains of penicillin binding protein 5 to maintenance of uniform cellular morphology of Escherichia coli.

The importance of a critical protonation state and the fate of the catalytic steps in class A beta-lactamases and penicillin-binding proteins.

Contributions of PBP 5 and DD-carboxypeptidase penicillin binding proteins to maintenance of cell shape in Escherichia coli.

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1348-1358

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scholarly article

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10.1002/PROT.24501

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English

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P478

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

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Jed F. Fisher

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2014-02-06T00:00:00Z

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24375650

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4057297

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Protonation states of active-site lysines of penicillin-binding protein 6 from Escherichia coli and the mechanistic implications.

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P2860

P2860

Protonation states of active-site lysines of penicillin-binding protein 6 from Escherichia coli and the mechanistic implications.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932