(Q47661220)

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Study and reengineering of the binding sites and allosteric regulation of biosynthetic threonine deaminase by isoleucine and valine in Escherichia coli

scientific article published on 7 June 2012

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Europe PubMed Central

PubMed publication ID

4 February 2018

http://europepmc.org/abstract/MED/22669632

Study and reengineering of the binding sites and allosteric regulation of biosynthetic threonine deaminase by isoleucine and valine in Escherichia coli (English)

1 reference

Europe PubMed Central

PubMed publication ID

4 February 2018

http://europepmc.org/abstract/MED/22669632

Escherichia coli

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Jibin Sun

4

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Lin Chen

1

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Europe PubMed Central

PubMed publication ID

4 February 2018

http://europepmc.org/abstract/MED/22669632

Zhen Chen

2

1 reference

Europe PubMed Central

PubMed publication ID

4 February 2018

http://europepmc.org/abstract/MED/22669632

Ping Zheng

3

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Europe PubMed Central

PubMed publication ID

4 February 2018

http://europepmc.org/abstract/MED/22669632

An-Ping Zeng

5

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PubMed publication ID

4 February 2018

http://europepmc.org/abstract/MED/22669632

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publication date

7 June 2012

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Europe PubMed Central

PubMed publication ID

4 February 2018

http://europepmc.org/abstract/MED/22669632

Applied Microbiology and Biotechnology

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Europe PubMed Central

PubMed publication ID

4 February 2018

http://europepmc.org/abstract/MED/22669632

97

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Europe PubMed Central

PubMed publication ID

4 February 2018

http://europepmc.org/abstract/MED/22669632

7

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Europe PubMed Central

PubMed publication ID

4 February 2018

http://europepmc.org/abstract/MED/22669632

2939-2949

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Europe PubMed Central

PubMed publication ID

4 February 2018

http://europepmc.org/abstract/MED/22669632

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The ACT domain family.

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An expanded two-state model accounts for homotropic cooperativity in biosynthetic threonine deaminase from Escherichia coli

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Catabolite inactivation of biodegradative threonine dehydratase of Escherichia coli

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Structure and control of pyridoxal phosphate dependent allosteric threonine deaminase

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Local and global control mechanisms in allosteric threonine deaminase

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The ACT domain: a small molecule binding domain and its role as a common regulatory element

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Metabolic redirection of carbon flow toward isoleucine by expressing a catabolic threonine dehydratase in a threonine-overproducing Corynebacterium glutamicum

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Protein sectors: evolutionary units of three-dimensional structure

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Structure of the regulatory subunit of acetohydroxyacid synthase isozyme III from Escherichia coli.

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Structures of R- and T-state Escherichia coli aspartokinase III. Mechanisms of the allosteric transition and inhibition by lysine

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ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

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Fermentative production of branched chain amino acids: a focus on metabolic engineering

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The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase

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A method for simultaneous alignment of multiple protein structures

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Allosteric regulation of Bacillus subtilis threonine deaminase, a biosynthetic threonine deaminase with a single regulatory domain

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Engineering metabolic systems for production of advanced fuels

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Structural Insight into concerted inhibition of alpha 2 beta 2-type aspartate kinase from Corynebacterium glutamicum

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21 January 2018

Identifiers

10.1007/S00253-012-4176-Z

1 reference

Europe PubMed Central

PubMed publication ID

4 February 2018

http://europepmc.org/abstract/MED/22669632

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

4 February 2018

http://europepmc.org/abstract/MED/22669632

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