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1.4.3.1: D-aspartate oxidase

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

Word Map on EC 1.4.3.1

Reaction

D-Aspartate
+
H2O
+
O2
=
oxaloacetate
+
NH3
+
H2O2

Synonyms

aspartic oxidase, C47A10.5 gene product, C47Ap, ChDASPO, ChDDO, D-Asp oxidase, D-aspartic oxidase, D-AspO, DAO, DASOX, DASPO, DDO, DDO-1, DDO-2, DDO-3, DDO1, DDO3, F18E3.7a gene product, F18Ep

ECTree

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

Engineering

Engineering on EC 1.4.3.1 - D-aspartate oxidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C141Y
variant produces crystals suitable for X-ray analysis
C143G
variant produces crystals suitable for X-ray analysis
H54A
variant shows a lower maximal activity and kinetic efficiency compared to the wild-type
R216Q
single nucleotiode polymorphism, reduces enzyme activity towards acidic D-amino acids, decreases the binding affinity for the coenzyme FAD and decreases the temperature stability. Cultured mammalian cells reveal elevated D-aspartate level in cultures of R216Q cells
R237A
variant shows a lower maximal activity and kinetic efficiency compared to the wild-type
S308N
single nucleotiode polymorphism, reduces enzyme activity towards acidic D-amino acids, decreases the binding affinity for the coenzyme FAD and decreases the temperature stability. Cultured mammalian cells reveal elevated D-aspartate level in cultures of R216Q cells
R216A
-
mutant with significantly reduced activity
R216E
-
mutant with significantly reduced activity
R216L
-
mutant with significantly reduced activity
R216M
-
mutant with significantly reduced activity
R216X
-
activities of mouse DDO against acidic D-amino acids are virtually extinguished or significantly reduced by replacements of the Arg216 residue with other amino acid residues
R237A
R237E
-
mutant with significantly reduced activity
R237X
-
activities of mouse DDO against acidic D-amino acids are virtually extinguished or significantly reduced by replacements of the Arg237 residue with other amino acid residues
R237Y
-
mutant with significantly reduced activity
S308A
has a significantly higher catalytic efficiency towards D-Asp and N-methyl-D-Asp, and a higher affinity for FAD compared to the wild type enzyme
S308G
S308Y
has a significantly lower catalytic efficiency towards D-Asp and N-methyl-D-Asp, and a lower affinity for FAD compared to the wild type enzyme
F248Y
H56D
the mutant exhibits no significant activity toward acidic D-amino acids
H56F
the mutant exhibits no significant activity toward acidic D-amino acids
H56K
the mutant exhibits no significant activity toward acidic D-amino acids
R243A
site-directed mutagenesis, inactive mutant
R243D
site-directed mutagenesis, the mutant exhibits different spectral features of bound flavin from that of the wild-type enzyme. R243D exhibits approximately 2fold higher DDO activity than that of the wild-type with a high substrate specificity to D-aspartate. Kinetic analysis shows that R243D mutant has a 2.5fold lower Km and a 1.6fold higher kcat for D-aspartate compared to the wild-type enzyme, resulting in approximately 4fold higher catalytic efficiency
R243E
site-directed mutagenesis, the mutant exhibits different spectral features of bound flavin from that of the wild-type enzyme and displays lower DDO activity. The mutant also oxidizes the substrates of DAO, D-Ala and D-Arg, albeit with very low activities
R243K
site-directed mutagenesis, the mutant exhibits different spectral features of bound flavin from that of the wild-type enzyme and displays lower DDO activity
R243M
site-directed mutagenesis, the mutant exhibits different spectral features of bound flavin from that of the wild-type enzyme and displays lower DDO activity. The mutant also oxidizes the substrates of DAO, D-Ala and D-Arg, albeit with very low activities
additional information
-
intense D-Asp immunoreactivity is observed in the intermediate lobe of the pituitary gland of the DDO-deficient mice, phenotype of DDO-deficient mice, detailed overview