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Homospermidine synthase

From Wikipedia, the free encyclopedia
Homospermidine synthase
Identifiers
EC no.2.5.1.44
CAS no.76106-84-8
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
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NCBIproteins

Homospermidine synthase (EC 2.5.1.44) is an enzyme with systematic name putrescine:putrescine 4-aminobutyltransferase (ammonia-forming).[1] It was first characterised from Rhodopseudomonas viridis and catalyses two related chemical reactions. One converts two molecules of putrescine to one of sym-homospermidine, with ammonia as a byproduct:[2][3]

The other combines putrescine with spermidine to form sym-homospermidine and 1,3-propanediamine:[4]

The enzyme has been found in Acinetobacter tartarogenes and Lathyrus sativus.[5][6] There is evidence that it evolved from the enzyme deoxyhypusine synthase and that it is part of the biosynthetic pathway to pyrrolizidine alkaloids.[7] In many bacteria, it is an essential part of the metabolism of polyamines.[8]

References

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  1. ↑ Enzyme 2.5.1.44 at KEGG Pathway Database.
  2. ↑ Tait GH (February 1979). "The formation of homospermidine by an enzyme from Rhodopseudomonas viridis [proceedings]". Biochemical Society Transactions. 7 (1): 199–201. doi:10.1042/bst0070199. PMID 437275.
  3. ↑ Ober D, Tholl D, Martin W, Hartmann T (1996). "Homospermidine synthase of Rhodopseudomonas viridis: Substrate specificity and effects of the heterologously expressed enzyme on polyamine metabolism of Escherichia coli". J. Gen. Appl. Microbiol. 42 (5): 411–419. doi:10.2323/jgam.42.411.
  4. ↑ Böttcher F, Ober D, Hartmann T (1994). "Biosynthesis of pyrrolizidine alkaloids: putrescine and spermidine are essential substrates of enzymatic homospermidine formation". Can. J. Chem. 72 (1): 80–85. Bibcode:1994CaJCh..72...80B. doi:10.1139/v94-013.
  5. ↑ Yamamoto S, Nagata S, Kusaba K (July 1993). "Purification and characterization of homospermidine synthase in Acinetobacter tartarogenes ATCC 31105". Journal of Biochemistry. 114 (1): 45–9. doi:10.1093/oxfordjournals.jbchem.a124137. PMID 8407874.
  6. ↑ Srivenugopal KS, Adiga PR (August 1980). "Enzymic synthesis of sym-homospermidine in Lathyrus sativus (grass pea) seedlings". The Biochemical Journal. 190 (2): 461–4. doi:10.1042/bj1900461. PMC 1162113. PMID 7470060.
  7. ↑ Ober D, Hartmann T (December 1999). "Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine synthase". Proceedings of the National Academy of Sciences of the United States of America. 96 (26): 14777–82. Bibcode:1999PNAS...9614777O. doi:10.1073/pnas.96.26.14777. PMC 24724. PMID 10611289.
  8. ↑ Krossa, Sebastian; Faust, Annette; Ober, Dietrich; Scheidig, Axel J. (2016). "Comprehensive Structural Characterization of the Bacterial Homospermidine Synthase–an Essential Enzyme of the Polyamine Metabolism". Scientific Reports. 6 19501. doi:10.1038/srep19501. PMC 4725965. PMID 26776105.
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