Structure of prokaryotic polyamine deacetylase reveals evolutionary functional relationships with eukaryotic histone deacetylases

Biochemistry

Volumn 50, Issue 11, 2011, Pages 1808-1817

  Lombardi, Patrick M ^a   Angell, Heather D ^a   Whittington, Douglas A ^a,c   Flynn, Erin F ^a   Rajashankar, Kanagalaghatta R ^b   Christianson, David W ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b Cornell University ^*  (United States)

^c AMGEN INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; AMIDOHYDROLASE; CELL-CYCLE PROGRESSION; DEACETYLASE; DEACETYLATION; DIMER INTERFACE; FLEXIBLE SUBSTRATE; FUNCTIONAL RELATIONSHIP; HISTONE DEACETYLASES; HYDROXAMATE; INACTIVE MUTANTS; POLYAMINES; SMALL MOLECULES; TRANSITION-STATE ANALOGUES;

ACETYLATION; DIMERIZATION; DIMERS; NUCLEIC ACIDS;

GENE EXPRESSION;

ACETYLPOLYAMINE AMIDOHYDROLASE; HISTONE DEACETYLASE; HISTONE DEACETYLASE LIKE AMIDOHYDROLASE; HISTONE DEACETYLASE LIKE PROTEIN; N CYCLOHEXYL 3 AMINOPROPANESULFONIC ACID; OLIGOMER; POLYAMINE; POLYAMINE DEACETYLASE; UNCLASSIFIED DRUG;

ARTICLE; CRYSTAL STRUCTURE; DIMERIZATION; ENZYME ACTIVITY; ENZYME STRUCTURE; EUKARYOTE; PRIORITY JOURNAL; PROKARYOTE; SITE DIRECTED MUTAGENESIS;

AMINOHYDROLASES; BACTERIA; CATALYSIS; DIMERIZATION; EUKARYOTA; EVOLUTION, MOLECULAR; HISTONE DEACETYLASES; LIGANDS; POLYAMINES;

EUKARYOTA; MYCOPLANA RAMOSA; PROKARYOTA;

EID: 79952790219     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101859k     Document Type: Article

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