Structural highlights
3q9b is a 12 chain structure with sequence from Mycoplana ramosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
|
| Method: | X-ray diffraction, Resolution 2.25Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
APAH_MYCRA Involved in polyamine metabolism. Catalyzes the deacetylation of various acetylated polyamines such as N-acetylputrescine, N-acetylcadaverine, N(1)-acetylspermine, N(1)-acetylspermidine and N(8)-acetylspermidine (PubMed:8824626, PubMed:3207420). In vitro, is also able to deacetylate L-Lys(epsilon-acetyl)coumarin, but has very low activity towards the larger tetrapeptide N-acetyl-L-Arg-L-His-L-Lys(epsilon-acetyl)-L-Lys(epsilon-acetyl)coumarin (PubMed:21268586).[1] [2] [3]
References
- ↑ Lombardi PM, Angell HD, Whittington DA, Flynn EF, Rajashankar KR, Christianson DW. Structure of Prokaryotic Polyamine Deacetylase Reveals Evolutionary Functional Relationships with Eukaryotic Histone Deacetylases . Biochemistry. 2011 Jan 26. PMID:21268586 doi:10.1021/bi101859k
- ↑ Fujishiro K, Ando M, Uwajima T. Crystallization and some properties of acetylpolyamine amidohydrolase from Mycoplana bullata. Biochem Biophys Res Commun. 1988 Dec 30;157(3):1169-74. PMID:3207420 doi:10.1016/s0006-291x(88)80997-5
- ↑ Sakurada K, Ohta T, Fujishiro K, Hasegawa M, Aisaka K. Acetylpolyamine amidohydrolase from Mycoplana ramosa: gene cloning and characterization of the metal-substituted enzyme. J Bacteriol. 1996 Oct;178(19):5781-6. PMID:8824626 doi:10.1128/jb.178.19.5781-5786.1996
