1.1.1.3: homoserine dehydrogenase

This is an abbreviated version, for detailed information about homoserine dehydrogenase, go to the full flat file.

Reaction

L-homoserine
+
NAD(P)+
=
L-aspartate 4-semialdehyde
+
NAD(P)H
+
H+

Synonyms

AK-HDH, AK-HSD-1, AK-HSDH, aspartate kinase-homoserine dehydrogenase, aspartokinase-homoserine dehydrogenase I, HDH, hom, hom-1, Hom6, homoserine dehydrogenase 1, homoserine dehydrogenase 2, HSD, HSDH, HseDH, orf19.2951, SACOL1362

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.3 homoserine dehydrogenase

Engineering

Engineering on EC 1.1.1.3 - homoserine dehydrogenase

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Q443A
-
site-directed mutagenesis, altered reaction kinetics for both activities and altered inhibition pattern by L-threonine compared to the wild-type enzyme, asparate kinase activity is completely insensitive to inhibition by L-threonine, overview
Q524A
-
site-directed mutagenesis, altered reaction kinetics for both activities and altered inhibition pattern by L-threonine compared to the wild-type enzyme, overview
G378E
-
feedback resistance of the enzyme
L200F
-
site-directed mutagenesis, compared to mutant L200F, the double mutant shows 2 degree higher optimum temperature, 1.24 times higher activity, but the same pH optimum of pH 7.5 as mutant L200F. Both mutants L200F/D215K and L200F show good resistance to organic solvents and metal ions
L200F/D215A
-
site-directed mutagenesis
L200F/D215E
-
site-directed mutagenesis
L200F/D215G
-
site-directed mutagenesis
L200F/D215K
-
site-directed mutagenesis, compared to mutant L200F, the double mutant shows 2 dgree higher optimum temperature, 1.24 times higher activity, but the same pH optimum of pH 7.5 as mutant L200F. Both mutants L200F/D215K and L200F show good resistance to organic solvents and metal ions
L200F
-
site-directed mutagenesis, compared to mutant L200F, the double mutant shows 2 degree higher optimum temperature, 1.24 times higher activity, but the same pH optimum of pH 7.5 as mutant L200F. Both mutants L200F/D215K and L200F show good resistance to organic solvents and metal ions
-
L200F/D215A
-
site-directed mutagenesis
-
L200F/D215E
-
site-directed mutagenesis
-
L200F/D215G
-
site-directed mutagenesis
-
L200F/D215K
-
site-directed mutagenesis, compared to mutant L200F, the double mutant shows 2 dgree higher optimum temperature, 1.24 times higher activity, but the same pH optimum of pH 7.5 as mutant L200F. Both mutants L200F/D215K and L200F show good resistance to organic solvents and metal ions
-
K57Aa
site-directed mutagenesis, in contrast to the wild-type enzyme, the mutant enzyme shows catalytic activity with NADP+, the activity with NAD+ is increased compared to the wild-type enzyme
R40A
site-directed mutagenesis, in contrast to the wild-type enzyme, the mutant enzyme shows catalytic activity with NADP+, the activity with NAD+ is decreased compared to the wild-type enzyme
K57Aa
-
site-directed mutagenesis, in contrast to the wild-type enzyme, the mutant enzyme shows catalytic activity with NADP+, the activity with NAD+ is increased compared to the wild-type enzyme
-
R40A
-
site-directed mutagenesis, in contrast to the wild-type enzyme, the mutant enzyme shows catalytic activity with NADP+, the activity with NAD+ is decreased compared to the wild-type enzyme
-
H309A
-
decrease of catalytic activity and elimination of substrate inhibition
K105A
-
site-directed double-primer PCR mutagenesis
K105R
-
site-directed double-primer PCR mutagenesis
K205A
-
site-directed double-primer PCR mutagenesis
K105A
-
site-directed double-primer PCR mutagenesis
-
K105R
-
site-directed double-primer PCR mutagenesis
-
K205A
-
site-directed double-primer PCR mutagenesis
-
additional information