| Structural highlights
Function
OXDD_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 PubMed
The 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
- ↑ Takahashi S, Takahashi T, Kera Y, Matsunaga R, Shibuya H, Yamada RH. Cloning and expression in Escherichia coli of the D-aspartate oxidase gene from the yeast Cryptococcus humicola and characterization of the recombinant enzyme. J Biochem. 2004 Apr;135(4):533-40. PMID:15115779 doi:10.1093/jb/mvh068
- ↑ Takahashi S, Kakuichi T, Fujii K, Kera Y, Yamada RH. Physiological role of D-aspartate oxidase in the assimilation and detoxification of D-aspartate in the yeast Cryptococcus humicola. Yeast. 2005 Nov;22(15):1203-12. PMID:16278929 doi:10.1002/yea.1303
- ↑ Takahashi S, Shimada K, Nozawa S, Goto M, Abe K, Kera Y. Possible role of a histidine residue in the substrate specificity of yeast d-aspartate oxidase. J Biochem. 2016 Mar;159(3):371-8. PMID:26519738 doi:10.1093/jb/mvv108
- ↑ Yamada R, Ujiie H, Kera Y, Nakase T, Kitagawa K, Imasaka T, Arimoto K, Takahashi M, Matsumura Y. Purification and properties of D-aspartate oxidase from Cryptococcus humicolus UJ1. Biochim Biophys Acta. 1996 May 23;1294(2):153-8. PMID:8645733 doi:10.1016/0167-4838(96)00012-x
- ↑ Takahashi S, Kakuichi T, Fujii K, Kera Y, Yamada RH. Physiological role of D-aspartate oxidase in the assimilation and detoxification of D-aspartate in the yeast Cryptococcus humicola. Yeast. 2005 Nov;22(15):1203-12. PMID:16278929 doi:10.1002/yea.1303
- ↑ Goto M, Nonaka R, Mizobuchi T, Imanishi D, Takahashi S. Crystal structure of D-aspartate oxidase from Cryptococcus humicola UJ1. Acta Crystallogr F Struct Biol Commun. 2025 Oct 1. PMID:40970329 doi:10.1107/S2053230X25008192
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