| Accepted Name |
|---|
| NADH-dependent peroxiredoxin
|
| Alternative Name(s) |
|---|
| alkyl hydroperoxide reductase |
| Reaction catalysed |
|---|
| a hydroperoxide + H(+) + NADH <=> an alcohol + H2O + NAD(+) |
| Comment(s) |
|---|
- Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant
proteins.
- They can be divided into three classes: typical 2-Cys, atypical 2-Cys
and 1-Cys peroxiredoxins.
- The peroxidase reaction comprises two steps centered around a redox-
active cysteine called the peroxidatic cysteine.
- All three peroxiredoxin classes have the first step in common,
in which the peroxidatic cysteine attacks the peroxide substrate and
is oxidized to S-hydroxycysteine (a sulfenic acid).
- The second step of the peroxidase reaction, the regeneration of
cysteine from S-hydroxycysteine, distinguishes the three
peroxiredoxin classes.
- For typical 2-Cys Prxs, in the second step, the peroxidatic
S-hydroxycysteine from one subunit is attacked by the 'resolving'
cysteine located in the C-terminus of the second subunit, to form an
intersubunit disulfide bond, which is then reduced by one of several
cell-specific thiol-containing reductants completing the catalytic
cycle.
- In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its
resolving cysteine are in the same polypeptide, so their reaction
forms an intrachain disulfide bond.
- The 1-Cys Prxs conserve only the peroxidatic cysteine, so its
regeneration involves direct interaction with a reductant molecule.
- This bacterial peroxiredoxin differs from most other forms by
comprising two types of subunits.
- One subunit (AhpC) is a typical 2-Cys peroxiredoxin.
- Following the reduction of the substrate, one AhpC subunit forms a
disulfide bond with an identical unit.
- The disulfide bond is reduced by the second type of subunit (AhpF).
- This second subunit is a flavin-containing protein that uses
electrons from NADH to reduce the cysteine residues on the
AhpC subunits back to their active state.
- Formerly EC 1.11.1.15.
|
| Cross-references |
|---|
| BRENDA | 1.11.1.26 |
| EC2PDB | 1.11.1.26 |
| ExplorEnz | 1.11.1.26 |
| PRIAM enzyme-specific profiles | 1.11.1.26 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.11.1.26 |
| IUBMB Enzyme Nomenclature | 1.11.1.26 |
| IntEnz | 1.11.1.26 |
| MEDLINE | Find literature relating to 1.11.1.26 |
| MetaCyc | 1.11.1.26 |
| Rhea expert-curated reactions | 1.11.1.26 |
| UniProtKB/Swiss-Prot |
| P82954, AHPC_ACICA | K0J4Q8, AHPC_AMPXN | P80239, AHPC_BACSU |
| P57279, AHPC_BUCAI | Q8K9W0, AHPC_BUCAP | Q89AS1, AHPC_BUCBP |
| P83117, AHPC_DELAC | P0AE10, AHPC_ECO57 | P0AE09, AHPC_ECOL6 |
| P0AE08, AHPC_ECOLI | P26830, AHPC_FERAY | P56876, AHPC_HELPJ |
| P21762, AHPC_HELPY | Q02UU0, AHPC_PSEAB | P72314, AHPC_RHORU |
| P0A252, AHPC_SALTI | P0A251, AHPC_SALTY | P0AE11, AHPC_SHIFL |
| Q2FJN4, AHPC_STAA3 | P0A0B7, AHPC_STAA8 | Q2YVK2, AHPC_STAAB |
| Q5HIR5, AHPC_STAAC | P0A0B5, AHPC_STAAM | P99074, AHPC_STAAN |
| Q6GJR7, AHPC_STAAR | Q6GC91, AHPC_STAAS | P0A0B6, AHPC_STAAW |
| Q5HRY1, AHPC_STAEQ | Q8CMQ2, AHPC_STAES | Q4L376, AHPC_STAHJ |
| Q49UT8, AHPC_STAS1 |
|
