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CATH Superfamily 1.10.630.10

Cytochrome P450

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:

"
Cytochrome P450
".

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 37: Cytochrome P450 9

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
Valine N-monooxygenase. [EC: 1.14.14.38]
L-valine + 2 O(2) + 2 [reduced NADPH--hemoprotein reductase] = (E)-2- methylpropanal oxime + 2 [oxidized NADPH--hemoprotein reductase] + CO(2) + 3 H(2)O.
  • This enzyme catalyzes two successive N-hydroxylations of L-valine, the committed step in the biosynthesis of the cyanogenic glucoside linamarin in Manihot esculenta (cassava).
  • The product of the two hydroxylations, N,N-dihydroxy-L-valine, is labile and undergoes dehydration and decarboxylation that produce the (E) isomer of the oxime.
  • It is still not known whether the decarboxylation is spontaneous or catalyzed by the enzyme.
  • The enzyme can also accept L-isoleucine as substrate, with a lower activity.
  • It is different from EC 1.14.14.39.
  • Formerly EC 1.14.13.117.
 8 A0A2C9UQJ0 A0A2C9UQJ0 A0A2C9UW86 A0A2C9UW86 Q9M7B7 Q9M7B7 Q9M7B8 Q9M7B8
Tryptophan N-monooxygenase. [EC: 1.14.14.156]
L-tryptophan + 2 [reduced NADPH--hemoprotein reductase] + 2 O(2) = (E)- indol-3-ylacetaldoxime + 2 [oxidized NADPH--hemoprotein reductase] + CO(2) + 3 H(2)O.
  • A cytochrome P450 (heme-thiolate) protein from the plant Arabidopsis thaliana.
  • This enzyme catalyzes two successive N-hydroxylations of L-tryptophan, the first steps in the biosynthesis of both auxin and the indole alkaloid phytoalexin camalexin.
  • The product of the two hydroxylations, N,N-dihydroxy-L-tryptophan, is extremely labile and dehydrates spontaneously.
  • The dehydrated product is then subject to a decarboxylation that produces an oxime.
  • It is still not known whether the decarboxylation is spontaneous or catalyzed by the enzyme.
  • Formerly EC 1.14.13.125 and EC 1.14.13.n2.
 5 A0A178W1U6 A0A178W1U6 O81346 Q501D8 Q501D8
Isoleucine N-monooxygenase. [EC: 1.14.14.39]
L-isoleucine + 2 O(2) + 2 [reduced NADPH--hemoprotein reductase] = (1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH--hemoprotein reductase] + CO(2) + 3 H(2)O.
  • This enzyme, found in plants, catalyzes two successive N-hydroxylations of L-isoleucine, the committed step in the biosynthesis of the cyanogenic glucoside lotaustralin.
  • The product of the two hydroxylations, N,N-dihydroxy-L-isoleucine, is labile and undergoes dehydration followed by decarboxylation, producing the oxime.
  • It is still not known whether the decarboxylation is spontaneous or catalyzed by the enzyme.
  • The enzyme can also accept L-valine, but with a lower activity.
  • Cf. EC 1.14.14.38, valine N-monooxygenase.
  • Formerly EC 1.4.13.117.
 2 Q6J540 Q6J541
Homomethionine N-monooxygenase. [EC: 1.14.14.42]
An L-polyhomomethionine + 2 O(2) + 2 [reduced NADPH--hemoprotein reductase] = an omega-(methylthio)-(E)-alkanal oxime + CO(2) + 3 H(2)O + 2 [oxidized NADPH--hemoprotein reductase].
  • Involved in methionine-derived aliphatic glucosinolates biosynthesis.
  • It catalyzes two successive N-hydroxylations, which are followed by dehydration and decarboxylation.
  • CYP79F1 from Arabidopsis thaliana can metabolize homo-, di-, tri-, tetra-, penta-, and hexahomomethionine to their corresponding aldoximes, while CYP79F2 from the same plant can only metabolize penta- and hexahomomethionine.
  • Formerly EC 1.14.13.n5 and EC 1.14.13.n6.
 2 Q949U1 Q9FUY7