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Literature summary for 1.1.1.3 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 1.1.1.3

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

Protein Variants

Protein Variants Comment Organism
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

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant separated catalytic domains Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate 4-semialdehyde + NADPH
-
 Escherichia coli L-homoserine + NADP+
-
 r
L-aspartate 4-semialdehyde + NADPH part of the aspartate pathway of amino acid biosynthesis Escherichia coli L-homoserine + NADP+
-
 r

Synonyms

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

Turnover Number [1/s]

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