9vpf | pdb_00009vpf
Crystal structure of D-aspartate oxidase from Cryptococcus humicola UJ1.
Structural highlights
FunctionOXDD_VANHU Selectively catalyzes the oxidative deamination of acidic amino acids (PubMed:15115779, PubMed:26519738, PubMed:8645733, Ref.4). Protects the organism from the toxicity of D-amino acids (PubMed:16278929). Enables the organism to utilize D-amino acids as a source of nutrients (PubMed:16278929). Enables the organism to utilize D-aspartate as a source of nitrogen and carbon (PubMed:16278929).[1] [2] [3] [4] [5] Publication Abstract from PubMedThe enzyme D-aspartate oxidase (DDO) oxidizes acidic D-amino acids using the coenzyme flavin adenine dinucleotide to generate the corresponding alpha-keto acids and ammonia. DDO differs from D-amino-acid oxidase (DAAO), which acts on neutral and basic D-amino acids. Although the enzymatic properties of DDO have been characterized in several species, the structure of DDO had remained unclear. The structure of DDO derived from Cryptococcus humicola strain UJ1 (chDDO) was determined by X-ray crystallography at 1.70 A resolution. While the three-dimensional structures of DAAOs are known to be homodimers, chDDO forms a homotetramer. This difference was found to be caused by the deletion of one loop and the insertion of two loops. Crystal structure of D-aspartate oxidase from Cryptococcus humicola UJ1.,Goto M, Nonaka R, Mizobuchi T, Imanishi D, Takahashi S Acta Crystallogr F Struct Biol Commun. 2025 Oct 1. doi: , 10.1107/S2053230X25008192. PMID:40970329[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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