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
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1.4.3.1
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d-amino
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n-methyl-d-aspartate
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nmda
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d-serine
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d-glutamate
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octopus
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nmdar-dependent
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d-alanine
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prepulse
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humicola
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d-amino-acid
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d-ser
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d-glu
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drug development
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molecular biology
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medicine
- 1.4.3.1
-
d-amino
- n-methyl-d-aspartate
- nmda
- d-serine
- d-glutamate
- octopus
-
nmdar-dependent
- d-alanine
-
prepulse
- humicola
-
d-amino-acid
- d-ser
- d-glu
- drug development
- molecular biology
- medicine
Reaction
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
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Engineering
Engineering on EC 1.4.3.1 - D-aspartate oxidase
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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
R216X
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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
R237X
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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
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
H56A
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
H56N
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
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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
R237A
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site-directed mutagenesis, active site mutant, shows reduced binding of inhibitor thiolactomycin compared to the wild-type enzyme
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
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the mutation results in lack of a side-chain OH group at position 308, and increases mutant enzyme catalytic efficiency against D-Asp and NMDA to about 7-10times higher than that of the wild-type enzyme. Moreover, the dissociation-constant value for FAD of this Gly-substitution mutant is significantly lower than that of the wild-type enzyme, suggesting that it has enhanced ability to bind to FAD
the mutant exhibits no significant activity toward acidic D-amino acids
H56A
the mutant gains the ability to utilize neutral D-amino acids as substrates, such as D-methionine, D-phenylalanine and D-glutamine
the mutant exhibits no significant activity toward acidic D-amino acids
H56N
the mutant gains the ability to utilize neutral D-amino acids as substrates, such as D-methionine, D-phenylalanine and D-glutamine