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Literature summary for 4.3.1.19 extracted from

  • Favrot, L.; Amorim Franco, T.M.; Blanchard, J.S.
    Biochemical characterization of the threonine deaminase (2018), Biochemistry, 57, 6003-6012 .
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
L-valine activator, (0-10 mM) leads to a nearly 50% increase in MsIlvA activity Mycolicibacterium smegmatis

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Mycolicibacterium smegmatis

Protein Variants

Protein Variants Comment Organism
K67A inactive mutant enzyme, the mutant enzyme is not yellow, as observed for the wild-type enzyme Mycolicibacterium smegmatis
K67Q inactive mutant enzyme, the mutant enzyme is not yellow, as observed for the wild-type enzyme Mycolicibacterium smegmatis

Inhibitors

Inhibitors Comment Organism Structure
L-Cycloserine powerful suicide inactivator that generates a covalent pyridoxal 5'-phosphate-isoxazole complex Mycolicibacterium smegmatis
L-isoleucine less than 2% activity remains after addition of 0.5 mM L-isoleucine Mycolicibacterium smegmatis
L-valine
-
Mycolicibacterium smegmatis
Mn2+ 50 mM, 50% loss of activity Mycolicibacterium smegmatis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.66
-
L-threonine pH 8.0, 30°C Mycolicibacterium smegmatis
2.86
-
L-allo-threonine pH 8.0, 30°C Mycolicibacterium smegmatis
3.01
-
beta-chloro-L-alanine pH 8.0, 30°C Mycolicibacterium smegmatis
106.3
-
L-serine pH 8.0, 30°C Mycolicibacterium smegmatis

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ 50 mM, 1.7fold activation Mycolicibacterium smegmatis
K+ 50 mM, 1.5fold activation Mycolicibacterium smegmatis
Li+ 50 mM, 1.5fold activation Mycolicibacterium smegmatis
Mg2+ 50 mM, 1.6fold activation Mycolicibacterium smegmatis
Na+ 50 mM, 1.5fold activation Mycolicibacterium smegmatis
NH4+ 50 mM, 1.75fold activation Mycolicibacterium smegmatis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
180000
-
gel filtration Mycolicibacterium smegmatis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-threonine Mycolicibacterium smegmatis the enzyme is involved in the biosynthesis of L-isoleucine 2-oxobutanoate + NH3
-
?

Organism

Organism UniProt Comment Textmining
Mycolicibacterium smegmatis A0QX60
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Mycolicibacterium smegmatis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-chloro-L-alanine
-
Mycolicibacterium smegmatis 3-chloro-2-oxopropionate + NH3
-
?
L-allo-threonine
-
Mycolicibacterium smegmatis ?
-
?
L-serine
-
Mycolicibacterium smegmatis pyruvate + NH3
-
?
L-threonine
-
Mycolicibacterium smegmatis 2-oxobutanoate + NH3
-
?
L-threonine the enzyme is involved in the biosynthesis of L-isoleucine Mycolicibacterium smegmatis 2-oxobutanoate + NH3
-
?

Subunits

Subunits Comment Organism
homotetramer
-
Mycolicibacterium smegmatis

Synonyms

Synonyms Comment Organism
ilvA
-
Mycolicibacterium smegmatis
MSMEG3183
-
Mycolicibacterium smegmatis
Threonine deaminase
-
Mycolicibacterium smegmatis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Mycolicibacterium smegmatis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.69
-
L-allo-threonine pH 8.0, 30°C Mycolicibacterium smegmatis
9.42
-
L-threonine pH 8.0, 30°C Mycolicibacterium smegmatis
27.15
-
beta-chloro-L-alanine pH 8.0, 30°C Mycolicibacterium smegmatis
32.59
-
L-serine pH 8.0, 30°C Mycolicibacterium smegmatis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Mycolicibacterium smegmatis

pH Range

pH Minimum pH Maximum Comment Organism
6.8 8.9 pH has no significant effect on activity Mycolicibacterium smegmatis

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate dependent on Mycolicibacterium smegmatis

General Information

General Information Comment Organism
metabolism the enzyme is involved in the biosynthesis of L-isoleucine Mycolicibacterium smegmatis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.03
-
L-serine pH 8.0, 30°C Mycolicibacterium smegmatis
1.99
-
L-allo-threonine pH 8.0, 30°C Mycolicibacterium smegmatis
5.7
-
L-threonine pH 8.0, 30°C Mycolicibacterium smegmatis
9.02
-
beta-chloro-L-alanine pH 8.0, 30°C Mycolicibacterium smegmatis