3q9c: Difference between revisions

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[[Image:3q9c.png|left|200px]]
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{{STRUCTURE_3q9c|  PDB=3q9c  |  SCENE=  }}  
{{STRUCTURE_3q9c|  PDB=3q9c  |  SCENE=  }}  
===Crystal Structure of H159A APAH complexed with N8-acetylspermidine===
===Crystal Structure of H159A APAH complexed with N8-acetylspermidine===
{{ABSTRACT_PUBMED_21268586}}


 
==Function==
<!--
[[http://www.uniprot.org/uniprot/APHA_MYCRA APHA_MYCRA]] Acts on many types of acetylpolyamines. Has high affinity towards acetylputrescine, acetylcadaverine, acetylspermidine, and acetylspermine. Acts on L-Lys-(epsilon-acetyl)-coumarin, but has very low activity towards acetylated peptides.
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{{ABSTRACT_PUBMED_21268586}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
<ref group="xtra">PMID:21268586</ref><references group="xtra"/>
<ref group="xtra">PMID:021268586</ref><references group="xtra"/><references/>
[[Category: Mycoplana ramosa]]
[[Category: Mycoplana ramosa]]
[[Category: Christianson, D W.]]
[[Category: Christianson, D W.]]
[[Category: Lombardi, P M.]]
[[Category: Lombardi, P M.]]
[[Category: Arginase fold]]
[[Category: Deacetylase]]
[[Category: Hdac]]
[[Category: Hydrolase]]
[[Category: Polyamine]]

Revision as of 08:22, 8 May 2013

Template:STRUCTURE 3q9c

Crystal Structure of H159A APAH complexed with N8-acetylspermidine

Template:ABSTRACT PUBMED 21268586

Function

[APHA_MYCRA] Acts on many types of acetylpolyamines. Has high affinity towards acetylputrescine, acetylcadaverine, acetylspermidine, and acetylspermine. Acts on L-Lys-(epsilon-acetyl)-coumarin, but has very low activity towards acetylated peptides.

About this Structure

3q9c is a 12 chain structure with sequence from Mycoplana ramosa. Full crystallographic information is available from OCA.

Reference

  1. Lombardi PM, Angell HD, Whittington DA, Flynn EF, Rajashankar KR, Christianson DW. Structure of Prokaryotic Polyamine Deacetylase Reveals Evolutionary Functional Relationships with Eukaryotic Histone Deacetylases . Biochemistry. 2011 Jan 26. PMID:21268586 doi:10.1021/bi101859k

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