Insights into class D beta-lactamases are revealed by the crystal structure of the OXA10 enzyme from Pseudomonas aeruginosa (Q27629767)

4

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Laurent Maveyraud

object named as

L Maveyraud

1

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author name string

D Golemi

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L P Kotra

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S Vakulenko

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J P Samama

Serine beta-lactamases and penicillin-binding proteins

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publication date

15 December 2000

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published in

Structure

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volume

8

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issue

12

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page(s)

1289-98

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cites work

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ampC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of beta-lactamases of the penicillinase type

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Sequence of PSE-2 beta-lactamase

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X-ray analysis of the NMC-A beta-lactamase at 1.64-A resolution, a class A carbapenemase with broad substrate specificity

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Refined crystal structure of beta-lactamase from Citrobacter freundii indicates a mechanism for beta-lactam hydrolysis

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OXA-24, a novel class D beta-lactamase with carbapenemase activity in an Acinetobacter baumannii clinical strain

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Carbapenems as inhibitors of OXA-13, a novel, integron-encoded beta-lactamase in Pseudomonas aeruginosa.

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OXA-15, an extended-spectrum variant of OXA-2 beta-lactamase, isolated from a Pseudomonas aeruginosa strain

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OXA-16, a further extended-spectrum variant of OXA-10 beta-lactamase, from two Pseudomonas aeruginosa isolates

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The First Structural and Mechanistic Insights for Class D β-Lactamases: Evidence for a Novel Catalytic Process for Turnover of β-Lactam Antibiotics

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Laboratory mutants of OXA-10 beta-lactamase giving ceftazidime resistance in Pseudomonas aeruginosa

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