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Spermidine Synthase
From Proteopedia
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Polyamines are essential in all branches of life. Spermidine synthase (putrescine aminopropyltransferase, PAPT) catalyzes the biosynthesis of spermidine, a ubiquitous polyamine. | Polyamines are essential in all branches of life. Spermidine synthase (putrescine aminopropyltransferase, PAPT) catalyzes the biosynthesis of spermidine, a ubiquitous polyamine. | ||
[[1inl]] - The crystal structure of the PAPT from Thermotoga maritima (TmPAPT) has been solved to 1.5 A resolution. | [[1inl]] - The crystal structure of the PAPT from Thermotoga maritima (TmPAPT) has been solved to 1.5 A resolution. | ||
| - | The structure of TmPAPT in a complex with adoDATO ([[1jq3]]) can also be found on this site. | + | The structure of TmPAPT in a complex with adoDATO ([[1jq3]]) can also be found on this site. |
| + | Created with the participation of [[User:Lindsey Butler|Lindsey Butler]]. | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 07:03, 5 June 2012
Image:1inl.png
Spermidine synthase 1inl
Under construction!
Polyamines are essential in all branches of life. Spermidine synthase (putrescine aminopropyltransferase, PAPT) catalyzes the biosynthesis of spermidine, a ubiquitous polyamine.
1inl - The crystal structure of the PAPT from Thermotoga maritima (TmPAPT) has been solved to 1.5 A resolution.
The structure of TmPAPT in a complex with adoDATO (1jq3) can also be found on this site.
Created with the participation of Lindsey Butler.
