Literature summary for 4.3.1.19 extracted from

Shulman, A.; Zalyapin, E.; Vyazmensky, M.; Yifrach, O.; Barak, Z.; Chipman, D.M.
Allosteric regulation of Bacillus subtilis threonine deaminase, a biosynthetic threonine deaminase with a single regulatory domain (2008), Biochemistry, 47, 11783-11792.

Search for more literature for 4.3.1.19

Activating Compound

Activating Compound	Comment	Organism	Structure
L-valine	-	Bacillus subtilis

Protein Variants

Protein Variants	Comment	Organism
G350A	site-directed mutagenesis, the affinity for both allosteric effectors is lower compared to the wild-type, valine binds exclusively to the R state, the mutation causes a shift in the equilibrium between the T and R conformational states of the protein toward the T state with L being higher than that of the wild-type enzyme	Bacillus subtilis
L352A	site-directed mutagenesis, the affinity for both allosteric effectors is lower compared to the wild-type, valine binds exclusively to the R state, the mutation causes a shift in the equilibrium between the T and R conformational states of the protein toward the T state with L being 6.5fold higher than that of the wild-type enzyme	Bacillus subtilis
N363A	site-directed mutagenesis, the mutant acts similar to the wild-type	Bacillus subtilis
Q347A	site-directed mutagenesis, mutant Q347A is very similar to the wild-type enzyme in most of its characteristics, except for a 1.5fold increase in L and a 5fold increase in KTIle	Bacillus subtilis
T367A	site-directed mutagenesis, the T367A mutation causes a decrease in the affinity of bsTD for both allosteric effectors and an increase in substrate affinity compared to the wild-type enzyme	Bacillus subtilis
Y371L	site-directed mutagenesis, the apparent affinities for both of the allosteric effectors are very low and the apparent dissociation constant for isoleucine from the T state is 50fold higher compared to the wild-type	Bacillus subtilis

Inhibitors

Inhibitors	Comment	Organism	Structure
isoleucine	end product inhibition, reversed by valine, the short C-terminal regulatory domain is composed of one ACT-like subdomain, which binds isoleucine and valine	Bacillus subtilis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	Monod-Wyman-Changeux symmetrical model analysis of steady-state kinetics for the wild-type and four mutant enzymes	Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-threonine	Bacillus subtilis	threonine deaminase is a key regulatory enzyme in the pathway for the biosynthesis of isoleucine, allosteric enzyme regulation model, overview	2-oxobutanoate + NH3	-	?

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-threonine	-	Bacillus subtilis	2-oxobutanoate + NH3	-	?
L-threonine	threonine deaminase is a key regulatory enzyme in the pathway for the biosynthesis of isoleucine, allosteric enzyme regulation model, overview	Bacillus subtilis	2-oxobutanoate + NH3	-	?

Subunits

Subunits	Comment	Organism
More	the short C-terminal regulatory domain is composed of only one ACT-like subdomain	Bacillus subtilis

Synonyms

Synonyms	Comment	Organism
Threonine deaminase	-	Bacillus subtilis

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Release 2023.1 (January 2023)