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.

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

     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

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Results	in table
2	Activating Compound
342	AA Sequence
4	Application
1	CAS Registry Number
32	Cloned(Commentary)
61	Cofactor
2	Crystallization (Commentary)
3	Disease/ Diagnostics
2	Expression
16	General Information
1	General Stability
38	IC50 Value
133	Inhibitors
51	kcat/KM [mM/s]
21	Ki Value [mM]
153	KM Value [mM]
42	Localization
1	Metals/Ions
30	Molecular Weight [Da]
114	Natural Substrates/ Products (Substrates)
294	Organism
5	Pathway
6	PDB ID
14	pH Optimum
6	pH Range
5	pH Stability
35	Protein Variants
27	Purification (Commentary)
1	Reaction
3	Reaction Type
117	Reference
191	Source Tissue
68	Specific Activity [micromol/min/mg]
1	Storage Stability
338	Substrates and Products (Substrate)
25	Subunits
89	Synonyms
1	Systematic Name
13	Temperature Optimum [°C]
8	Temperature Stability [°C]
70	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.4.3.1 - D-aspartate oxidase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

structure of mutants C141Y and C143G, to 3.22 A resolution. The FAD-binding domain is comprised of residues 1-46, 143-192, 282-335 with the canonical dinucleotide binding fold observed in several flavoenzymes, and the substrate-binding domain (residues 47-142, 193-281) is characterized by a large, eight-stranded, mixed beta-sheet

Homo sapiens

Q99489

763008

sitting drop vapor diffusion method, using 5–10%(w/v) PEG 8000, 100 mM sodium dihydrogen phosphate (or 100 mM potassium dihydrogen phosphate), 100 mM sodium acetate (pH 4.7)

Sus scrofa

-

723870