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1.4.3.16: L-aspartate oxidase

This is an abbreviated version!
For detailed information about L-aspartate oxidase, go to the full flat file.

Word Map on EC 1.4.3.16

Reaction

L-aspartate
+
O2
=
iminosuccinate
 +
H2O2

Synonyms

AO, At5g14760, FIN4, L-Asp oxidase, L-aspartate oxidase, LAO, LASPO, More, nadB, oxidase, L-aspartate, StLASPO, Tl-LASPO

ECTree

     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.3 With oxygen as acceptor
                1.4.3.16 L-aspartate oxidase

Engineering

Engineering on EC 1.4.3.16 - L-aspartate oxidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E121A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, catalytically inactive against either 3-OH-erythro- or 3-OH-threo-L-aspartate, but is active with N-acetyl- and N-formyl-L-aspartate
E121D
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, catalytically inactive against either 3-OH-erythro- or 3-OH-threo-L-aspartate
E121K
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, catalytically inactive against either 3-OH-erythro- or 3-OH-threo-L-aspartate
E121Q
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, catalytically inactive against either 3-OH-erythro- or 3-OH-threo-L-aspartate
H244A
-
binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate
H244S
-
binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate
H351A
-
binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate
H351S
-
binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate
R386L
-
binds substrate analogues with higher dissociation constants and presens lower kcat/Km values in the reduction of fumarate
H244A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
H351A
-
inactive
Q242A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R290A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R386A
-
inactive
S389A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
T259A
-
inactive
additional information