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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.3 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
2.7.2.4 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

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.3 additional information construction of a hybrid enzyme AKIII-HDHI+ by fusing a wild-type monofunctional aspartate kinase AKIII enzyme to the thrA2+ gene, encoding the homoserine dehydrogenase including the interface region of the wild-type bifunctional enzyme, the hybrid enzyme shows highly improved kinetic properties for homoserine dehydrogenase activity, and is not sensitive to L-threonine inhibition Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.2.4 L-threonine feedback inhibition Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.3 0.41
-
 L-homoserine recombinant hybrid bifunctional holoenzyme AKIII-HDHI+ containing the interface region, homoserine dehydrogenase activity Escherichia coli
1.1.1.3 0.68
-
 L-homoserine recombinant isolated catalytic HDH-domain containing the interface region, homoserine dehydrogenase activity Escherichia coli
1.1.1.3 1.2
-
 L-homoserine recombinant wild-type bifunctional holoenzyme, homoserine dehydrogenase activity Escherichia coli
1.1.1.3 17.2
-
 L-homoserine recombinant isolated catalytic HDH-domain not containing the interface region, homoserine dehydrogenase activity Escherichia coli
2.7.2.4 0.51
-
 L-aspartate recombinant hybrid bifunctional holoenzyme AKIII-HDHI+ containing the interface region, asparate kinase activity Escherichia coli
2.7.2.4 0.63
-
 L-aspartate recombinant wild-type bifunctional holoenzyme, asparate kinase activity Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.3 L-aspartate 4-semialdehyde + NADPH Escherichia coli part of the aspartate pathway of amino acid biosynthesis L-homoserine + NADP+
-
 r
2.7.2.4 ATP + L-aspartate Escherichia coli part of the aspartate pathway of amino acid biosynthesis ADP + 4-phospho-L-aspartate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.3 Escherichia coli
-
-
-
2.7.2.4 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.3 recombinant separated catalytic domains Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.3 L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+ bifunctional enzyme showing aspartate kinase, EC 2.7.2.4, and homoserine dehydrogenase activities Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.3 L-aspartate 4-semialdehyde + NADPH
-
 Escherichia coli L-homoserine + NADP+
-
 r
1.1.1.3 L-aspartate 4-semialdehyde + NADPH part of the aspartate pathway of amino acid biosynthesis Escherichia coli L-homoserine + NADP+
-
 r
2.7.2.4 ATP + L-aspartate part of the aspartate pathway of amino acid biosynthesis Escherichia coli ADP + 4-phospho-L-aspartate
-
 ?
2.7.2.4 ATP + L-aspartate aspartate kinase activity Escherichia coli ADP + 4-phospho-L-aspartate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.3 AK-HDH
-
 Escherichia coli
1.1.1.3 aspartokinase-homoserine dehydrogenase I
-
 Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.3 0.24
-
 L-homoserine recombinant wild-type bifunctional holoenzyme, homoserine dehydrogenase activity Escherichia coli
1.1.1.3 0.51
-
 L-homoserine recombinant isolated catalytic HDH-domain not containing the interface region, homoserine dehydrogenase activity Escherichia coli
1.1.1.3 3.3
-
 L-homoserine recombinant isolated catalytic HDH-domain containing the interface region, homoserine dehydrogenase activity Escherichia coli
1.1.1.3 24
-
 L-homoserine recombinant hybrid bifunctional holoenzyme AKIII-HDHI+ containing the interface region, homoserine dehydrogenase activity Escherichia coli
2.7.2.4 0.16
-
 L-aspartate recombinant hybrid bifunctional holoenzyme AKIII-HDHI+ containing the interface region, asparate kinase activity Escherichia coli
2.7.2.4 0.39
-
 L-aspartate recombinant wild-type bifunctional holoenzyme, asparate kinase activity Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.2.4 0.33
-
 L-threonine recombinant wild-type bifunctional holoenzyme, inhibition of asparate kinase activity Escherichia coli