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CATH Superfamily 2.170.150.20

Peptide methionine sulfoxide reductase.

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:

"
Peptide methionine sulfoxide reductase.
".

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.

Superfamily EC Annotations

Note: the EC figure is not being displayed for this superfamily as there are more than 100 different EC terms.

There are 3 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
Peptide-methionine (R)-S-oxide reductase. [EC: 1.8.4.12]
Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L- methionine (R)-S-oxide + thioredoxin.
  • The reaction occurs in the reverse direction to that shown above.
  • Exhibits high specificity for reduction of the R-form of methionine S-oxide, with higher activity being observed with L-methionine S-oxide than with D-methionine S-oxide.
  • While both free and protein-bound methionine (R)-S-oxide act as substrates, the activity with the peptide-bound form is far greater.
  • Plays a role in preventing oxidative-stress damage caused by reactive oxygen species by reducing the oxidized form of methionine back to methionine and thereby reactivating peptides that had been damaged.
  • The reaction proceeds via a sulfenic-acid intermediate.
  • For MsrB2 and MsrB3, thioredoxin is a poor reducing agent but thionein works well.
 707 A0A009GDB5 A0A009ILK8 A0A009JH87 A0A009PZP3 A0A009S9P1 A0A009TCB6 A0A028ALC6 A0A028EBT4 A0A029HZ70 A0A029ITD8
(697 more...)
Peptide-methionine (S)-S-oxide reductase. [EC: 1.8.4.11]
(1) Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L- methionine (S)-S-oxide + thioredoxin. (2) L-methionine + thioredoxin disulfide + H(2)O = L-methionine (S)-S- oxide + thioredoxin.
  • The reaction occurs in the reverse direction to that shown above.
  • Exhibits high specificity for the reduction of the S-form of L-methionine S-oxide, acting faster on the residue in a peptide than on the free amino acid.
  • On the free amino acid, it can also reduce D-methionine (S)-S-oxide but more slowly.
  • Plays a role in preventing oxidative-stress damage caused by reactive oxygen species by reducing the oxidized form of methionine back to methionine and thereby reactivating peptides that had been damaged.
  • The reaction proceeds via a sulfenic-acid intermediate.
  • Formerly EC 1.8.4.6.
 45 A0A064C3V2 A0A0H2ZLK9 A0A0H2ZP44 A0A0H3BKX2 A0A0H5DMG2 A0A0H6EDV0 A0A0K9UQ55 A0A0Y6G043 A0A158LNN5 A0A1C7BX06
(35 more...)
L-methionine (R)-S-oxide reductase. [EC: 1.8.4.14]
L-methionine + thioredoxin disulfide + H(2)O = L-methionine (R)-S-oxide + thioredoxin.
  • Unlike EC 1.8.4.12 this enzyme cannot use peptide-bound methionine (R)-S-oxide as a substrate.
  • Differs from EC 1.8.4.13, in that L-methionine (S)-S-oxide is not a substrate.
  • Formerly EC 1.8.4.5.
 17 A0A2J8W0M2 A1E952 H2QZL3 M5FMU9 Q3MHL9 Q4FZX5 Q52KJ8 Q5R869 Q5R930 Q6NW52
(7 more...)