Mutational analysis of two putative catalytic motifs of the type IV restriction endonuclease Eco57I. (Q43513160)

24 November 2017

Mutational analysis of two putative catalytic motifs of the type IV restriction endonuclease Eco57I. (English)

1 reference

24 November 2017

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Rimseliene R

1

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PubMed ID

11124947

24 November 2017

Janulaitis A

series ordinal

2

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PubMed ID

11124947

24 November 2017

language of work or name

English

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publication date

21 December 2000

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Journal of Biological Chemistry

24 November 2017

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24 November 2017

276

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24 November 2017

13

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24 November 2017

10492-10497

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REBASE - restriction enzymes and methylases

24 November 2017

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Class-IIS restriction enzymes--a review

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Purification and properties of the Eco57I restriction endonuclease and methylase--prototypes of a new class (type IV)

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Cloning and sequence analysis of the genes coding for Eco57I type IV restriction-modification enzymes

21 January 2018

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Single amino acid substitutions uncouple the DNA binding and strand scission activities of Fok I endonuclease.

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FokI dimerization is required for DNA cleavage

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EcoKI with an amino acid substitution in any one of seven DEAD-box motifs has impaired ATPase and endonuclease activities

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Sequence of the Salmonella typhimurium StyLT1 restriction-modification genes: homologies with EcoP1 and EcoP15 type-III R-M systems and presence of helicase domains

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Chimeric restriction endonuclease

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Structure prediction of the EcoRV DNA methyltransferase based on mutant profiling, secondary structure analysis, comparison with known structures of methyltransferases and isolation of catalytically inactive single mutants

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On the structure and operation of type I DNA restriction enzymes

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Identifiers

DOI

10.1074/JBC.M008687200

1 reference

24 November 2017

1 reference

PubMed ID

11124947