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Title: Complexes of Thermotoga maritima S-adenosylmethionine decarboxylase provide insights into substrate specificity

Abstract

The polyamines putrescine, spermidine and spermine are ubiquitous aliphatic cations and are essential for cellular growth and differentiation. S-Adenosylmethionine decarboxylase (AdoMetDC) is a critical pyruvoyl-dependent enzyme in the polyamine-biosynthetic pathway. The crystal structures of AdoMetDC from humans and plants and of the AdoMetDC proenzyme from Thermotoga maritima have been obtained previously. Here, the crystal structures of activated T. maritima AdoMetDC (TmAdoMetDC) and of its complexes with S-adenosylmethionine methyl ester and 5{prime}-deoxy-5{prime}-dimethylthioadenosine are reported. The results demonstrate for the first time that TmAdoMetDC autoprocesses without the need for additional factors and that the enzyme contains two complete active sites, both of which use residues from both chains of the homodimer. The complexes provide insights into the substrate specificity and ligand binding of AdoMetDC in prokaryotes. The conservation of the ligand-binding mode and the active-site residues between human and T. maritima AdoMetDC provides insight into the evolution of AdoMetDC.

Authors:
; ; ; ;
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
USDOE
OSTI Identifier:
1002475
Resource Type:
Journal Article
Journal Name:
Acta Crystallogr. D
Additional Journal Information:
Journal Volume: 66; Journal Issue: (2) ; 02, 2010
Country of Publication:
United States
Language:
ENGLISH
Subject:
36 MATERIALS SCIENCE; CATIONS; CHAINS; CRYSTAL STRUCTURE; DECARBOXYLASES; ENZYMES; ESTERS; PUTRESCINE; RESIDUES; SPECIFICITY; SPERMIDINE; SPERMINE; SUBSTRATES

Citation Formats

Bale, Shridhar, Baba, Kavita, McCloskey, Diane E, Pegg, Anthony E, and Ealick, Steven E. Complexes of Thermotoga maritima S-adenosylmethionine decarboxylase provide insights into substrate specificity. United States: N. p., 2010. Web. doi:10.1107/S090744490904877X.
Bale, Shridhar, Baba, Kavita, McCloskey, Diane E, Pegg, Anthony E, & Ealick, Steven E. Complexes of Thermotoga maritima S-adenosylmethionine decarboxylase provide insights into substrate specificity. United States. https://doi.org/10.1107/S090744490904877X
Bale, Shridhar, Baba, Kavita, McCloskey, Diane E, Pegg, Anthony E, and Ealick, Steven E. 2010. "Complexes of Thermotoga maritima S-adenosylmethionine decarboxylase provide insights into substrate specificity". United States. https://doi.org/10.1107/S090744490904877X.
@article{osti_1002475,
title = {Complexes of Thermotoga maritima S-adenosylmethionine decarboxylase provide insights into substrate specificity},
author = {Bale, Shridhar and Baba, Kavita and McCloskey, Diane E and Pegg, Anthony E and Ealick, Steven E},
abstractNote = {The polyamines putrescine, spermidine and spermine are ubiquitous aliphatic cations and are essential for cellular growth and differentiation. S-Adenosylmethionine decarboxylase (AdoMetDC) is a critical pyruvoyl-dependent enzyme in the polyamine-biosynthetic pathway. The crystal structures of AdoMetDC from humans and plants and of the AdoMetDC proenzyme from Thermotoga maritima have been obtained previously. Here, the crystal structures of activated T. maritima AdoMetDC (TmAdoMetDC) and of its complexes with S-adenosylmethionine methyl ester and 5{prime}-deoxy-5{prime}-dimethylthioadenosine are reported. The results demonstrate for the first time that TmAdoMetDC autoprocesses without the need for additional factors and that the enzyme contains two complete active sites, both of which use residues from both chains of the homodimer. The complexes provide insights into the substrate specificity and ligand binding of AdoMetDC in prokaryotes. The conservation of the ligand-binding mode and the active-site residues between human and T. maritima AdoMetDC provides insight into the evolution of AdoMetDC.},
doi = {10.1107/S090744490904877X},
url = {https://www.osti.gov/biblio/1002475}, journal = {Acta Crystallogr. D},
number = (2) ; 02, 2010,
volume = 66,
place = {United States},
year = {Fri Jun 25 00:00:00 EDT 2010},
month = {Fri Jun 25 00:00:00 EDT 2010}
}