2o06: Difference between revisions

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[[Image:2o06.~~jpg~~|left|200px]]

[[Image:2o06.png|left|200px]]

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~~'''~~Human spermidine synthase~~'''~~

===Human spermidine synthase===

~~==Overview==~~

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~~Aminopropyltransferases transfer aminopropyl groups from decarboxylated S-adenosylmethionine to amine acceptors~~, ~~forming polyamines. Structural and biochemical studies have been carried out with the human spermidine synthase~~, ~~which is highly specific for putrescine as~~ the ~~amine acceptor, and~~ the ~~Thermotoga maritima spermidine synthase~~, ~~which prefers putrescine but~~ is ~~more tolerant of other substrates. Comparison of the structures of the human spermidine synthase with both substrates and products with~~ the ~~known structure of T~~. ~~maritima spermidine synthase complexed to a multisubstrate analogue inhibitor and analysis of the properties of site~~-directed mutants provide a general mechanistic hypothesis for the aminopropyl transfer reaction. The studies also provide a structural basis for the specificity of the spermidine synthase subclass of the aminopropyltransferase family.

The line below this paragraph, {{ABSTRACT_PUBMED_17585781}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17585781 is the PubMed ID number.

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==About this Structure==

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[[Category: Structural genomic]]

[[Category: Structural genomics consortium]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 10~~:08:31 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:38:34 2008''

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-[[Image:2o06.jpg|left|200px]]
+{{Seed}}
+[[Image:2o06.png|left|200px]]
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 {{STRUCTURE_2o06|  PDB=2o06  |  SCENE=  }}
-'''Human spermidine synthase'''
+===Human spermidine synthase===
-==Overview==
+<!--
-Aminopropyltransferases transfer aminopropyl groups from decarboxylated S-adenosylmethionine to amine acceptors, forming polyamines. Structural and biochemical studies have been carried out with the human spermidine synthase, which is highly specific for putrescine as the amine acceptor, and the Thermotoga maritima spermidine synthase, which prefers putrescine but is more tolerant of other substrates. Comparison of the structures of the human spermidine synthase with both substrates and products with the known structure of T. maritima spermidine synthase complexed to a multisubstrate analogue inhibitor and analysis of the properties of site-directed mutants provide a general mechanistic hypothesis for the aminopropyl transfer reaction. The studies also provide a structural basis for the specificity of the spermidine synthase subclass of the aminopropyltransferase family.
+The line below this paragraph, {{ABSTRACT_PUBMED_17585781}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17585781 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17585781}}
 ==About this Structure==
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 [[Category: Structural genomic]]
 [[Category: Structural genomics consortium]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 10:08:31 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:38:34 2008''