Cocrystal Structures of Diaminopimelate Decarboxylase (Q57077250)

Mariana G. Pinho

4

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Alexander Tomasz

Alexander Tomasz

7

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Jeffrey B Bonanno

2

Jeffrey B. Bonanno

0 references

Hermínia de Lencastre

1 reference

ORCID Public Data File 2021

Stephen K Burley

8

Stephen K. Burley

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Soumya Jyoti Ray

1

Soumya S. Ray

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author name string

K.R. Rajashankar

3

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Guoshun He

5

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Herminia De Lencastre

The evolution of methicillin resistance in Staphylococcus aureus: similarity of genetic backgrounds in historically early methicillin-susceptible and -resistant isolates and contemporary epidemic clones.

6

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publication date

November 2002

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published in

Structure

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volume

10

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issue

11

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page(s)

1499-1508

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cites work

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Role of an altered penicillin-binding protein in methicillin- and cephem-resistant Staphylococcus aureus

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Reassessment of the number of auxiliary genes essential for expression of high-level methicillin resistance in Staphylococcus aureus

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Antigelling and antisickling bisphenyl oligopeptides and peptide analogues have similar structural features

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Structure of a Michaelis complex analogue: propionate binds in the substrate carboxylate site of alanine racemase

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Altering the reaction specificity of eukaryotic ornithine decarboxylase

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For the record: The three-dimensional structure of the ternary complex ofCorynebacterium glutamicumdiaminopimelate dehydrogenase-NADPH-L-2-amino-6-methylene-pimelate

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Vinylogous Amide Analogues of Diaminopimelic Acid (DAP) as Inhibitors of Enzymes Involved in Bacterial Lysine Biosynthesis

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Effect of analogues of diaminopimelic acid on the meso -diaminopimelate-adding enzyme from Escherichia coli

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Substrate and inhibitor binding sites in Corynebacterium glutamicum diaminopimelate dehydrogenase

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Not your average density.

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