Catalysis of site-specific recombination by Tn3 resolvase.
about
Vaccinia virus F16 protein, a predicted catalytically inactive member of the prokaryotic serine recombinase superfamily, is targeted to nucleoli.Stereospecific suppression of active site mutants by methylphosphonate substituted substrates reveals the stereochemical course of site-specific DNA recombination.Topoisomerases and site-specific recombinases: similarities in structure and mechanism.Intermediates in serine recombinase-mediated site-specific recombination.Large serine recombinase domain structure and attachment site binding.Nicked-site substrates for a serine recombinase reveal enzyme-DNA communications and an essential tethering role of covalent enzyme-DNA linkages.Distribution of the blaTEM gene and blaTEM-containing transposons in commensal Escherichia coli.
P2860
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P2860
Catalysis of site-specific recombination by Tn3 resolvase.
description
article científic
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article scientifique
@fr
articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on April 2010
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vedecký článok
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vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
Catalysis of site-specific recombination by Tn3 resolvase.
@en
Catalysis of site-specific recombination by Tn3 resolvase.
@nl
type
label
Catalysis of site-specific recombination by Tn3 resolvase.
@en
Catalysis of site-specific recombination by Tn3 resolvase.
@nl
prefLabel
Catalysis of site-specific recombination by Tn3 resolvase.
@en
Catalysis of site-specific recombination by Tn3 resolvase.
@nl
P356
P1476
Catalysis of site-specific recombination by Tn3 resolvase
@en
P2093
Femi J Olorunniji
P304
P356
10.1042/BST0380417
P577
2010-04-01T00:00:00Z