D-amino-acid oxidase
Named enzymes, including the metabolising cytochromes and the monoamine oxidases.
- Measurements
- 1
- Compounds
- 1
- Binding constants
- 0
- Median pX
- —
I · Identity
What this target is
Its function as UniProt states it, where in a cell the protein is found, and which cell types and tissues transcribe its gene.
D-amino-acid oxidase
Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity16616139,17088322,17303072,18544534,20368421,20567862,20603179,22203986,23219954,23391306,25030849,25701391,29274788,29326945,30938755,31799256,32730563,33484270,34041270,37558109,38035964. Required to catabolize D-amino acids synthesized endogenously, of gastrointestinal bacterial origin or obtained from the diet, and to use these as nutrients (By similarity). Regulates the level of D-amino acid neurotransmitters in the brain, such as D-serine, a co-agonist of N-methyl D-aspartate (NMDA) receptors, and may modulate synaptic transmission17303072. Catalyzes the first step of the racemization of D-DOPA to L-DOPA, for possible use in an alternative dopamine biosynthesis pathway17303072. Also catalyzes the first step of the chiral inversion of N(gamma)-nitro-D-arginine methyl ester (D-NNA) to its L-enantiomer L-NNA that acts as a nitric oxide synthase inhibitor (By similarity). The hydrogen peroxide produced in the reaction provides protection against microbial infection; it contributes to the oxidative killing activity of phagocytic leukocytes and protects against bacterial colonization of the small intestine (By similarity). Enzyme secreted into the lumen of the intestine may not be catalytically active and could instead be proteolytically cleaved into peptides with antimicrobial activity (By similarity). The hydrogen peroxide produced in the reaction may also play a role in promoting cellular senescence in response to DNA damage30659069. Could act as a detoxifying agent which removes D-amino acids accumulated during aging17303072
Quoted from UniProt’s FUNCTION annotation for P14920 (reviewed). The superscript numbers are UniProt’s own PubMed citations, kept in the sentence and in order, each linking to the paper it names.
What it acts with
STRING’s highest-confidence human functional partners. The combined score mixes several kinds of evidence, so each channel is shown separately — a partner supported by experiment is a different claim from one supported only by text mining, and for a receptor this is where its coupling appears as evidence rather than as assertion.
Where it sits in the cell
UniProt, curated Peroxisome matrix · Cytoplasm, cytosol · Presynaptic active zone · Secreted
Expression by cell type
Single cell type RNA, the 2 highest of those the Human Protein Atlas reports for this gene. Transcript, not protein, and a cell type rather than a tissue.
- Bergmann glia132.8 nCPM
- Hepatocytes53 nCPM
Expression by tissue
The tissues this gene is enriched in, by consensus RNA. A tissue absent from this list is one the Atlas does not call specific for this gene, which is not the same as absent from it.
- liver139.9 nTPM
- kidney84.2 nTPM
- brain48.2 nTPM
IV · Evidence
Every measurement at this target
Each row links to the ChEMBL assay it came from.
Functional readouts 1
IC₅₀, EC₅₀, AC₅₀ and potency. Assay-dependent, and not interchangeable with a binding constant.
| Target | Class | Type | Value (nM) | pX | Organism | Assay |
|---|---|---|---|---|---|---|
| D-amino-acid oxidase | Enzymes | IC50 | — no normalized value | — value does not convert to pX | Sus scrofa | CHEMBL964475 |