Structural highlights
3sm8 is a 1 chain structure with sequence from "bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , |
| Related: | 3nyc, 3nye, 3nyf |
| Gene: | dauA, PA3863, PAO1 ("Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Publication Abstract from PubMed
d-Arginine dehydrogenase (DADH) catalyzes the flavin-dependent oxidative deamination of d-arginine and other d-amino acids to the corresponding imino acids. The 1.07 A atomic-resolution structure of DADH crystallized with d-leucine unexpectedly revealed a covalent N(5) flavin adduct, instead of the expected iminoleucine product in the active site. This acyl adduct has been successfully reproduced by photoreduction of DADH in the presence of 4-methyl-2-oxopentanoic acid (ketoleucine). The iminoleucine may be released readily because of weak interactions in the binding site, in contrast to iminoarginine, converted to ketoleucine, which reacts with activated FAD to form the covalently linked acyl adduct.
Atomic-Resolution Structure of an N(5) Flavin Adduct in d-Arginine Dehydrogenase.,Fu G, Yuan H, Wang S, Gadda G, Weber IT Biochemistry. 2011 Jul 26;50(29):6292-4. Epub 2011 Jul 5. PMID:21707047[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fu G, Yuan H, Wang S, Gadda G, Weber IT. Atomic-Resolution Structure of an N(5) Flavin Adduct in d-Arginine Dehydrogenase. Biochemistry. 2011 Jul 26;50(29):6292-4. Epub 2011 Jul 5. PMID:21707047 doi:10.1021/bi200831a
