3anx | pdb_00003anx
From Proteopedia
Crystal structure of triamine/agmatine aminopropyltransferase (SPEE) from thermus thermophilus, complexed with MTA
Template:ABSTRACT PUBMED 21458463
Function
[SPEE_THET8] Catalyzes the production of spermidine from putrescine and decarboxylated S-adenosylmethionine (dcSAM), which serves as an aminopropyl donor. Has broad substrate specificity. Is also active with agmatine and norspermidine. Has lower activity with homospermidine, mitsubishine and thermine.[1]
About this Structure
3anx is a 2 chain structure with sequence from Thet8. Full crystallographic information is available from OCA.
Reference
- Ohnuma M, Ganbe T, Terui Y, Niitsu M, Sato T, Tanaka N, Tamakoshi M, Samejima K, Kumasaka T, Oshima T. Crystal structures and enzymatic properties of a triamine/agmatine aminopropyltransferase from Thermus thermophilus. J Mol Biol. 2011 May 20;408(5):971-86. Epub 2011 Mar 31. PMID:21458463 doi:https://dx.doi.org/10.1016/j.jmb.2011.03.025
- ↑ Ohnuma M, Ganbe T, Terui Y, Niitsu M, Sato T, Tanaka N, Tamakoshi M, Samejima K, Kumasaka T, Oshima T. Crystal structures and enzymatic properties of a triamine/agmatine aminopropyltransferase from Thermus thermophilus. J Mol Biol. 2011 May 20;408(5):971-86. Epub 2011 Mar 31. PMID:21458463 doi:https://dx.doi.org/10.1016/j.jmb.2011.03.025
