The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity (Q28143460)

Trends in Biochemical Sciences

Europe PubMed Central

title

The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity (English)

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author name string

A Chapman-Smith

series ordinal

1

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J E Cronan

series ordinal

2

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language of work or name

English

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publication date

September 1999

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published in

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volume

24

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issue

9

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page(s)

359-63

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cites work

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Kinetics of biotinyl-5'-adenylate synthesis catalyzed by the Escherichia coli repressor of biotin biosynthesis and the stability of the enzyme-product complex

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Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains

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A tale of two synthetases

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Evidence for interdomain interaction in the Escherichia coli repressor of biotin biosynthesis from studies of an N-terminal domain deletion mutant.

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Evidence for distinct ligand-bound conformational states of the multifunctional Escherichia coli repressor of biotin biosynthesis.

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Coupling of site-specific DNA binding to protein dimerization in assembly of the biotin repressor-biotin operator complex

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Identifiers

DOI

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Consolidated OpenCitations Corpus – April 2017

1408958

1408958

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Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

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