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1.1.1.3: homoserine dehydrogenase

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

Word Map on EC 1.1.1.3

Reaction

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

Synonyms

AK-HDH, AK-HSD-1, AK-HSDH, AK-HseDH, aspartate kinase-homoserine dehydrogenase, aspartokinase-homoserine dehydrogenase I, bifunctional aspartate kinase-homoserine dehydrogenase, BsHSD, HDH, hom, hom-1, Hom6, homoserine dehydrogenase 1, homoserine dehydrogenase 2, HSD, HSDH, HseDH, More, orf19.2951, PbHSD, SACOL1362, StHSD, thrA, TM_0547, TTHA0489, TtHSD

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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PROTEIN VARIANTS
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
G378S
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
-
G433R
site-directed mutagenesis, strain HS33/pACYC-pycP458S-thrAG433R-lysC shows increased activity (62.4% of the maximum theoretical yield)
P458S
site-directed mutagenesis, strain HS33/pACYC-pycP458S-thrAG433R-lysC shows increased activity (62.4% of the maximum theoretical yield)
G433R
-
site-directed mutagenesis, strain HS33/pACYC-pycP458S-thrAG433R-lysC shows increased activity (62.4% of the maximum theoretical yield)
-
P458S
-
site-directed mutagenesis, strain HS33/pACYC-pycP458S-thrAG433R-lysC shows increased activity (62.4% of the maximum theoretical yield)
-
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
-
K195A
site-directed mutagenesis, inactive mutant. In the crystal structure, the positions of Lys195 and L-Hse are significantly retained with those of the wild-type enzyme, enzyme crystal structure analysis
K99A
site-directed mutagenesis, inactive mutant. In the crystal structure, the productive geometry of the ternary complex is almost preserved with one new water molecule taking over the hydrogen bonds associated with Lys99, mutant enzyme crystal structure analysis
additional information