Activating Compound | Comment | Organism | Structure |
---|---|---|---|
L-valine | - |
Bacillus subtilis |
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 | 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 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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | - |
- |
- |
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 | Comment | Organism |
---|---|---|
More | the short C-terminal regulatory domain is composed of only one ACT-like subdomain | Bacillus subtilis |
Synonyms | Comment | Organism |
---|---|---|
Threonine deaminase | - |
Bacillus subtilis |