Literature summary for 1.1.1.3 extracted from

Chen, Z.; Rappert, S.; Zeng, A.P.
Rational design of allosteric regulation of homoserine dehydrogenase by a nonnatural inhibitor L-lysine (2015), ACS Synth. Biol., 4, 126-131.

Search for more literature for 1.1.1.3

Protein Variants

Protein Variants	Comment	Organism
additional information	design of an artificial allosteric enzyme to sense an unnatural signal for a precise and dynamical control of fluxes of growth-essential but byproduct pathways in metabolic engineering of industrial microorganisms. The natural threonine binding sites of the enzyme are engineered to a lysine binding pocket. The reengineered enzyme only responds to lysine inhibition but not to threonine	Corynebacterium glutamicum

Inhibitors

Inhibitors	Comment	Organism	Structure
L-lysine	allosteric regulation of recombinant engineered homoserine dehydrogenase by nonnatural inhibitor L-lysine	Corynebacterium glutamicum
L-threonine	the natural threonine binding sites of the enzyme are predicted and verified by mutagenesis experiments	Corynebacterium glutamicum
additional information	the natural threonine binding sites of the enzyme are engineered to a lysine binding pocket. The reengineered enzyme only responds to lysine inhibition but not to threonine	Corynebacterium glutamicum

Organism

Organism	UniProt	Comment	Textmining
Corynebacterium glutamicum	P08499	-	-

Synonyms

Synonyms	Comment	Organism
HSD	-	Corynebacterium glutamicum
HSDH	-	Corynebacterium glutamicum

General Information

General Information	Comment	Organism
physiological function	the enzyme is naturally allosterically regulated by threonine and isoleucine	Corynebacterium glutamicum

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Release 2023.1 (January 2023)