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CATH Superfamily 3.50.50.60

FAD/NAD(P)-binding domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
FAD/NAD(P)-binding domain
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 150: Polyamine oxidase 1

There are 4 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Polyamine oxidase (propane-1,3-diamine-forming). [EC: 1.5.3.14]
Spermidine + O(2) + H(2)O = propane-1,3-diamine + 4-aminobutanal + H(2)O(2).
  • As the products of the reaction cannot be converted directly to other polyamines, this class of polyamine oxidases is considered to be involved in the terminal catabolism of polyamines.
  • Catalyzes less efficiently the oxidation of N(1)-acetylspermine and spermine.
  • Differs in specificity from EC 1.5.3.13, EC 1.5.3.15, EC 1.5.3.16 and EC 1.5.3.17.
  • Formerly EC 1.5.3.11, EC 1.5.3.n6, EC 1.5.3.n7, EC 1.5.3.n8 and EC 1.5.3.n9.
 1 O64411
Non-specific polyamine oxidase. [EC: 1.5.3.17]
(1) Spermine + O(2) + H(2)O = spermidine + 3-aminopropanal + H(2)O(2). (2) Spermidine + O(2) + H(2)O = putrescine + 3-aminopropanal + H(2)O(2). (3) N(1)-acetylspermine + O(2) + H(2)O = spermidine + 3-acetamidopropanal + H(2)O(2). (4) N(1)-acetylspermidine + O(2) + H(2)O = putrescine + 3-acetamidopropanal + H(2)O(2).
  • The non-specific polyamine oxidases may differ from each other considerably.
  • The enzyme from Saccharomyces cerevisiae shows a rather broad specificity and also oxidizes N(8)-acetylspermidine.
  • The enzyme from Ascaris suum shows high activity with spermine and spermidine, but also oxidizes norspermine.
  • The enzyme from Arabidopsis thaliana shows high activity with spermidine, but also oxidizes other polyamines.
  • The specific polyamine oxidases are classified as EC 1.5.3.13, EC 1.5.3.14, EC 1.5.3.15 and EC 1.5.3.16.
  • Formerly EC 1.5.3.11, EC 1.5.3.n1, EC 1.5.3.n2 and EC 1.5.3.n4.
 1 Q9FNA2
N(8)-acetylspermidine oxidase (propane-1,3-diamine-forming). [EC: 1.5.3.15]
N(8)-acetylspermidine + O(2) + H(2)O = propane-1,3-diamine + 4-acetamidobutanal + H(2)O(2).
  • Also active with N(1)-acetylspermine, weak activity with N(1),N(12)- diacetylspermine.
  • No activity with diaminopropane, putrescine, cadaverine, diaminohexane, norspermidine, spermine and spermidine.
  • Absence of monoamine oxidase (EC 1.4.3.4) activity.
  • Differs in specificity from EC 1.5.3.13, EC 1.5.3.14, EC 1.5.3.16 and EC 1.5.3.17.
  • Formerly EC 1.5.3.11, EC 1.5.3.n6, EC 1.5.3.n7, EC 1.5.3.n8 and EC 1.5.3.n9.
 1 O64411
Spermine oxidase. [EC: 1.5.3.16]
Spermine + O(2) + H(2)O = spermidine + 3-aminopropanal + H(2)O(2).
  • The enzyme from Arabidopsis thaliana (AtPAO1) oxidizes norspermine to norspermidine with high efficiency.
  • The mammalian enzyme, encoded by the SMOX gene, is a cytosolic enzyme that catalyzes the oxidation of spermine at the exo (three-carbon) side of the tertiary amine.
  • No activity with spermidine.
  • Weak activity with N(1)-acetylspermine.
  • Differs in specificity from EC 1.5.3.13, EC 1.5.3.14, EC 1.5.3.15 and EC 1.5.3.17.
  • Formerly EC 1.5.3.11, EC 1.5.3.n1, EC 1.5.3.n2, EC 1.5.3.n3 and EC 1.5.3.n5.
 1 Q9FNA2