Article

N1-aminopropylagmatine, a new polyamine produced as a key intermediate in polyamine biosynthesis of an extreme thermophile, Thermus thermophilus. J Biol Chem

Josai University, Saitama, Saitama, Japan
Journal of Biological Chemistry (Impact Factor: 4.57). 09/2005; 280(34):30073-82. DOI: 10.1074/jbc.M413332200
Source: PubMed

ABSTRACT

In the extreme thermophile Thermus thermophilus, a disruption mutant of a gene homologous to speB (coding for agmatinase = agmatine ureohydrolase) accumulated N1-aminopropylagmatine (N8-amidino-1,8-diamino-4-azaoctane, N8-amidinospermidine), a new compound, whereas all other polyamines produced by the wild-type strain were absent from the cells. Double disruption of speB and speE (polyamine aminopropyltransferase) resulted in the disappearance of N1-aminopropylagmatine and the accumulation of agmatine. These results suggested the following. 1) N1-Aminopropylagmatine is produced from agmatine by the action of an enzyme coded by speE. 2) N1-Aminopropylagmatine is a metabolic intermediate in the biosynthesis of unique polyamines found in the thermophile. 3) N1-Aminopropylagmatine is a substrate of the SpeB homolog. They further suggest a new biosynthetic pathway in T. thermophilus, by which polyamines are formed from agmatine via N1-aminopropylagmatine. To confirm our speculation, we purified the expression product of the speB homolog and confirmed that the enzyme hydrolyzes N1-aminopropylagmatine to spermidine but does not act on agmatine.

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Available from: Yusuke Terui, Dec 22, 2015
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    • "Our metabolic studies have produced data that indicate an alternative route for polyamine synthesis. The common bacterial spermidine intermediate, putrescine, was not detected in any condition (detection limit for putrescine: 0.1 uM), which suggests that spermidine synthesis might be analogous to routes described in other extremophiles (Ohnuma et al. 2005). "
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    • "Thermus thermophilus has only one ACL5 gene homolog, SpeE, and this gene is assigned to encode bifunctional triamine/agmatine aminopropyltransferase (TAAPT; Ohnuma et al. 2011). Both bacterial and archaeal thermophiles have recently been shown to possess a unique pathway to synthesize spermidine in which agmatine is converted by TAAPT to N 1 -propylagmatine which is then hydrolyzed to form spermidine (Ohnuma et al. 2005, Morimoto et al. 2010). An ACL5-like TAAPT gene is also present in cyanobacteria . "
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    • "It is thus very likely that the prokaryotic sequences conforming this clade are the enzymes responsible for the synthesis of thermospermine , and they are not SPDS. The absence of SPDS activity in these prokaryotes is not surprising, given that, at least in T. thermophilus, spermidine is synthesized from N1-aminopropylagmatine and not from putrescine (Ohnuma et al. 2005). A subgroup of prokaryotic SPDS-related sequences , that contains a sequence of a cadaverine aminopropyltransferase from Pyrococcus furiosus (Cacciapuoti et al. 2007), is clearly separated from its paraphyletic SPDS, indicating that it can also be a group of sequences loosely annotated as SPDS (fig. "
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