Ontology highlight
ABSTRACT:
SUBMITTER: Korolev S
PROVIDER: S-EPMC2792006 | biostudies-literature | 2002 Jan
REPOSITORIES: biostudies-literature
Korolev Sergey S Ikeguchi Yoshihiko Y Skarina Tatiana T Beasley Steven S Arrowsmith Cheryl C Edwards Aled A Joachimiak Andrzej A Pegg Anthony E AE Savchenko Alexei A
Nature structural biology 20020101 1
Polyamines are essential in all branches of life. Spermidine synthase (putrescine aminopropyltransferase, PAPT) catalyzes the biosynthesis of spermidine, a ubiquitous polyamine. The crystal structure of the PAPT from Thermotoga maritima (TmPAPT) has been solved to 1.5 A resolution in the presence and absence of AdoDATO (S-adenosyl-1,8-diamino-3-thiooctane), a compound containing both substrate and product moieties. This, the first structure of an aminopropyltransferase, reveals deep cavities for ...[more]