Trypanosoma brucei S-adenosylmethionine decarboxylase N terminus is essential for allosteric activation by the regulatory subunit prozyme

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Background: Trypanosoma brucei S-adenosylmethionine decarboxylase (AdoMetDC) is activated by heterodimerization with a catalytically dead paralog, prozyme. Results: Trypanosomatid-specific residues in the AdoMetDC N terminus are essential for prozyme-mediated activation but not for heterodimerization. Conclusion: AdoMetDC activation likely involves a conformational change of the N-terminal peptide. Significance: Development of conformationally sensitive AdoMetDC inhibitors may provide a species-selective mechanism to inhibit trypanosomatid AdoMetDCs.

Original languageEnglish (US)
Pages (from-to)5232-5240
Number of pages9
JournalJournal of Biological Chemistry
Volume288
Issue number7
DOIs
StatePublished - Feb 15 2013

Fingerprint

Adenosylmethionine Decarboxylase
Trypanosoma brucei brucei
Chemical activation
Peptides

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

@article{1b72c0ece8514198821911086a076836,
title = "Trypanosoma brucei S-adenosylmethionine decarboxylase N terminus is essential for allosteric activation by the regulatory subunit prozyme",
abstract = "Background: Trypanosoma brucei S-adenosylmethionine decarboxylase (AdoMetDC) is activated by heterodimerization with a catalytically dead paralog, prozyme. Results: Trypanosomatid-specific residues in the AdoMetDC N terminus are essential for prozyme-mediated activation but not for heterodimerization. Conclusion: AdoMetDC activation likely involves a conformational change of the N-terminal peptide. Significance: Development of conformationally sensitive AdoMetDC inhibitors may provide a species-selective mechanism to inhibit trypanosomatid AdoMetDCs.",
author = "Nahir Velez and Brautigam, {Chad A} and Phillips, {Margaret A}",
year = "2013",
month = "2",
day = "15",
doi = "10.1074/jbc.M112.442475",
language = "English (US)",
volume = "288",
pages = "5232--5240",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "7",

}

TY - JOUR

T1 - Trypanosoma brucei S-adenosylmethionine decarboxylase N terminus is essential for allosteric activation by the regulatory subunit prozyme

AU - Velez, Nahir

AU - Brautigam, Chad A

AU - Phillips, Margaret A

PY - 2013/2/15

Y1 - 2013/2/15

N2 - Background: Trypanosoma brucei S-adenosylmethionine decarboxylase (AdoMetDC) is activated by heterodimerization with a catalytically dead paralog, prozyme. Results: Trypanosomatid-specific residues in the AdoMetDC N terminus are essential for prozyme-mediated activation but not for heterodimerization. Conclusion: AdoMetDC activation likely involves a conformational change of the N-terminal peptide. Significance: Development of conformationally sensitive AdoMetDC inhibitors may provide a species-selective mechanism to inhibit trypanosomatid AdoMetDCs.

AB - Background: Trypanosoma brucei S-adenosylmethionine decarboxylase (AdoMetDC) is activated by heterodimerization with a catalytically dead paralog, prozyme. Results: Trypanosomatid-specific residues in the AdoMetDC N terminus are essential for prozyme-mediated activation but not for heterodimerization. Conclusion: AdoMetDC activation likely involves a conformational change of the N-terminal peptide. Significance: Development of conformationally sensitive AdoMetDC inhibitors may provide a species-selective mechanism to inhibit trypanosomatid AdoMetDCs.

UR - http://www.scopus.com/inward/record.url?scp=84874054287&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84874054287&partnerID=8YFLogxK

U2 - 10.1074/jbc.M112.442475

DO - 10.1074/jbc.M112.442475

M3 - Article

C2 - 23288847

AN - SCOPUS:84874054287

VL - 288

SP - 5232

EP - 5240

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 7

ER -