Aldehyde dehydrogenase (FAD-independent) | |||||||||
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Identifiers | |||||||||
EC no. | 1.2.99.7 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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In enzymology, an aldehyde dehydrogenase (FAD-independent) (EC 1.2.99.7) is an enzyme that catalyzes the chemical reaction
The 3 substrates of this enzyme are aldehyde, H2O, and acceptor, whereas its two products are carboxylate and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with other acceptors. The systematic name of this enzyme class is aldehyde:acceptor oxidoreductase (FAD-independent). Other names in common use include aldehyde oxidase, aldehyde oxidoreductase, Mop, and AORDd.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1ZCS.
Dithiolene metal complexes are complexes containing 1,2-dithiolene ligands. 1,2-Dithiolene ligands, a particular case of 1,2-dichalcogenolene species along with 1,2-diselenolene derivatives, are unsaturated bidentate ligand wherein the two donor atoms are sulfur. 1,2-Dithiolene metal complexes are often referred to as "metal dithiolenes", "metallodithiolenes" or "dithiolene complexes". Most molybdenum- and tungsten-containing proteins have dithiolene-like moieties at their active sites, which feature the so-called molybdopterin cofactor bound to the Mo or W.
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