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Literature summary for 2.7.2.4 extracted from

  • James, C.L.; Viola, R.E.
    Production and characterization of bifunctional enzymes. Domain swapping to produce new bifunctional enzymes in the aspartate pathway (2002), Biochemistry, 41, 3720-3725.
    View publication on PubMed
Search for more literature for 2.7.2.4

Cloned(Commentary)

Cloned (Comment) Organism
both catalytic domains of the enzyme, performing each one of the enzyme activities, are expressed separately with or without the interface region, resulting in increased activity of each domain compared to the wild-type bifunctional holoenzyme, the isolated catalytic domains are no longer allosterically regulated, expression of hybrid holoenzyme AKIII-HDHI+ Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
L-threonine feedback inhibition Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.51
-
 L-aspartate recombinant hybrid bifunctional holoenzyme AKIII-HDHI+ containing the interface region, asparate kinase activity Escherichia coli
0.63
-
 L-aspartate recombinant wild-type bifunctional holoenzyme, asparate kinase activity Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-aspartate Escherichia coli part of the aspartate pathway of amino acid biosynthesis ADP + 4-phospho-L-aspartate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-aspartate part of the aspartate pathway of amino acid biosynthesis Escherichia coli ADP + 4-phospho-L-aspartate
-
 ?
ATP + L-aspartate aspartate kinase activity Escherichia coli ADP + 4-phospho-L-aspartate
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.16
-
 L-aspartate recombinant hybrid bifunctional holoenzyme AKIII-HDHI+ containing the interface region, asparate kinase activity Escherichia coli
0.39
-
 L-aspartate recombinant wild-type bifunctional holoenzyme, asparate kinase activity Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.33
-
 L-threonine recombinant wild-type bifunctional holoenzyme, inhibition of asparate kinase activity Escherichia coli