Many of the functional differences between acetohydroxyacid synthase (AHAS) isozyme I and other AHASs are a result of the rapid formation and breakdown of the covalent acetolactate-thiamin diphosphate adduct in AHAS I. (Q43760392)

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English	Many of the functional differences between acetohydroxyacid synthase (AHAS) isozyme I and other AHASs are a result of the rapid formation and breakdown of the covalent acetolactate-thiamin diphosphate adduct in AHAS I.	scientific article

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22443469

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title

Many of the functional differences between acetohydroxyacid synthase (AHAS) isozyme I and other AHASs are a result of the rapid formation and breakdown of the covalent acetolactate-thiamin diphosphate adduct in AHAS I. (English)

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22443469

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26 November 2017

author

Inna Belenky

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1

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22443469

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26 November 2017

author name string

Andrea Steinmetz

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2

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22443469

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26 November 2017

Maria Vyazmensky

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3

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22443469

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26 November 2017

Ze'ev Barak

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4

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22443469

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26 November 2017

Kai Tittmann

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5

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22443469

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26 November 2017

David M Chipman

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6

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22443469

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26 November 2017

language of work or name

English

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publication date

20 April 2012

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22443469

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26 November 2017

published in

FEBS Journal

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22443469

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26 November 2017

volume

279

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22443469

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26 November 2017

issue

11

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22443469

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26 November 2017

page(s)

1967-1979

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22443469

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cites work

Physiological implications of the specificity of acetohydroxy acid synthase isozymes of enteric bacteria

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Crossref

reference URL

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2012.08577.X

retrieved

21 January 2018

Acetohydroxy acid synthase I is required for isoleucine and valine biosynthesis by Salmonella typhimurium LT2 during growth on acetate or long-chain fatty acids.

1 reference

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Crossref

reference URL

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2012.08577.X

retrieved

21 January 2018

Acetohydroxy acid synthase I, a required enzyme for isoleucine and valine biosynthesis in Escherichia coli K-12 during growth on acetate as the sole carbon source

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2012.08577.X

retrieved

21 January 2018

Physiological implications of the substrate specificities of acetohydroxy acid synthases from varied organisms

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Crossref

reference URL

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2012.08577.X

retrieved

21 January 2018

Acetohydroxyacid synthase from Mycobacterium avium and its inhibition by sulfonylureas and imidazolinones

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2012.08577.X

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21 January 2018

Purification of Escherichia coli acetohydroxyacid synthase isoenzyme II and reconstitution of active enzyme from its individual pure subunits

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2012.08577.X

retrieved

21 January 2018

Construction of an active acetohydroxyacid synthase I with a flexible linker connecting the catalytic and the regulatory subunits

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2012.08577.X

retrieved

21 January 2018

Identifiers

DOI

10.1111/J.1742-4658.2012.08577.X

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Europe PubMed Central

PubMed publication ID

22443469

retrieved

26 November 2017

PubMed publication ID

22443469

1 reference

stated in

Europe PubMed Central

PubMed publication ID

22443469

retrieved

26 November 2017

ResearchGate publication ID

221972269

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