Ontology highlight
ABSTRACT:
SUBMITTER: Seckute J
PROVIDER: S-EPMC3267948 | biostudies-literature | 2011 Nov
REPOSITORIES: biostudies-literature
Sečkutė Jolita J McCloskey Diane E DE Thomas H Jeanette HJ Secrist John A JA Pegg Anthony E AE Ealick Steven E SE
Protein science : a publication of the Protein Society 20110915 11
Aminopropyltransferases are essential enzymes that form polyamines in eukaryotic and most prokaryotic cells. Spermidine synthase (SpdS) is one of the most well-studied enzymes in this biosynthetic pathway. The enzyme uses decarboxylated S-adenosylmethionine and a short-chain polyamine (putrescine) to make a medium-chain polyamine (spermidine) and 5'-deoxy-5'-methylthioadenosine as a byproduct. Here, we report a new spermidine synthase inhibitor, decarboxylated S-adenosylhomocysteine (dcSAH). The ...[more]