Query author contributions in Reactome
Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.
If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.
Details on Person The reactions catalyzed by aminopropyl-transferases annotate...
| Class:Id | Summation:353137 |
|---|---|
| _displayName | The reactions catalyzed by aminopropyl-transferases annotate... |
| _timestamp | 2008-06-12 17:29:13 |
| created | [InstanceEdit:353141] Gopinathrao, G, 2008-06-11 18:57:00 |
| literatureReference | [LiteratureReference:351205] Polyamines: metabolism and implications in human diseases |
| modified | [InstanceEdit:353147] Gopinathrao, G, 2008-06-11 18:57:22 [InstanceEdit:353581] Gopinathrao, G, 2008-06-12 17:22:59 [InstanceEdit:353592] Gopinathrao, G, 2008-06-12 17:29:12 |
| text | The reactions catalyzed by aminopropyl-transferases annotated above are generally irreversible. But spermine and spermidine can be recycled respectively into spermidine and putrescine. These events require the formation of N-acetylated intermediates, N1-acetylspermine and N1-acetylspermidine catalyzed by a cytosolic acetyl-CoA:spermidine/spermine N1-acetyl-tranferase (SSAT) enzyme. Subsequently, polyamine-oxidase (PAO), a FAD enzyme present in the peroxysomes, yields a polyamine with release of an aldehyde (3-acetamindopropanal) and H2O2. In addition, SMOX, a FAD-dependent, polyamine oxidase (PAOh1/SMO) that can efficiently use spermine as a substrate and is involved in interconversion reactions. |
| (summation) | [Pathway:351200] Interconversion of polyamines [Homo sapiens] |
| [Change default viewing format] | |
No pathways have been reviewed or authored by The reactions catalyzed by aminopropyl-transferases annotate... (353137)
