| Accepted Name |
|---|
| lipoyl-dependent peroxiredoxin
|
| Reaction catalysed |
|---|
| a hydroperoxide + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[lipoyl-carrier protein] <=> an alcohol + H2O + N(6)-[(R)-lipoyl]-L-lysyl-[lipoyl-carrier protein] |
| 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.
- Two types of lipoyl-dependent peroxiredoxins have been reported from
bacteria.
- One type is the AhpC/AhpD system, originally described from
Mycobacterium tuberculosis.
- In that system, AhpC catalyzes reduction of the substrate, resulting
in an intramolecular disulfide.
- AhpD then forms an intermolecular disulfide cross-link with AhpC,
reducing it back to active state.
- AhpD is reduced in turn by lipoylated proteins.
- The second type, which has been characterized in Xylella fastidiosa,
consists of only one type of subunit, which interacts directly with
lipoylated proteins.
- Formerly EC 1.11.1.15.
|
| Cross-references |
|---|
| BRENDA | 1.11.1.28 |
| EC2PDB | 1.11.1.28 |
| ExplorEnz | 1.11.1.28 |
| PRIAM enzyme-specific profiles | 1.11.1.28 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.11.1.28 |
| IUBMB Enzyme Nomenclature | 1.11.1.28 |
| IntEnz | 1.11.1.28 |
| MEDLINE | Find literature relating to 1.11.1.28 |
| MetaCyc | 1.11.1.28 |
| Rhea expert-curated reactions | 1.11.1.28 |
| UniProtKB/Swiss-Prot |
| A0R1V9, AHPC_MYCS2 | P9WQB6, AHPC_MYCTO | P9WQB7, AHPC_MYCTU |
| C1F4K1, AHPD_ACIC5 | B8J9Z2, AHPD_ANAD2 | Q2IMQ8, AHPD_ANADE |
| A7HCA3, AHPD_ANADF | B4UA87, AHPD_ANASK | A8HQP5, AHPD_AZOC5 |
| B2IHZ4, AHPD_BEII9 | Q9ANL0, AHPD_BRADU | A5ENR3, AHPD_BRASB |
| A4YYT0, AHPD_BRASO | B2SAW2, AHPD_BRUA1 | Q2YKW2, AHPD_BRUA2 |
| A6X5N3, AHPD_BRUA4 | Q578J2, AHPD_BRUAB | A9MBZ4, AHPD_BRUC2 |
| Q8YCF2, AHPD_BRUME | A9WZ04, AHPD_BRUSI | Q8FVW4, AHPD_BRUSU |
| Q9A268, AHPD_CAUVC | B8GVX4, AHPD_CAUVN | C3PGV9, AHPD_CORA7 |
| Q6NGT4, AHPD_CORDI | C4LJ26, AHPD_CORK4 | B6IZ19, AHPD_COXB2 |
| A9KBI4, AHPD_COXBN | A9N917, AHPD_COXBR | Q83BM5, AHPD_COXBU |
| Q0RH96, AHPD_FRAAA | A8L1J2, AHPD_FRASN | A9H8D2, AHPD_GLUDA |
| Q0BUC5, AHPD_GRABC | Q0BXT2, AHPD_HYPNA | Q1IJ49, AHPD_KORVE |
| Q0AKM4, AHPD_MARMM | B0UAJ8, AHPD_METS4 | B8EJZ2, AHPD_METSB |
| A0QGI9, AHPD_MYCA1 | B1MJX0, AHPD_MYCA9 | P0A5N5, AHPD_MYCBO |
| A1KLC4, AHPD_MYCBP | C1AQZ5, AHPD_MYCBT | B2HD59, AHPD_MYCMM |
| Q73ZL4, AHPD_MYCPA | Q50441, AHPD_MYCS2 | A5U5C5, AHPD_MYCTA |
| P9WQB4, AHPD_MYCTO | P9WQB5, AHPD_MYCTU | A0PSD4, AHPD_MYCUA |
| Q5YT53, AHPD_NOCFA | A5VCB6, AHPD_RHIWR | B6IQZ3, AHPD_RHOCS |
| C0ZYQ9, AHPD_RHOE4 | Q07I00, AHPD_RHOP5 | Q20Y19, AHPD_RHOPB |
| Q02BZ5, AHPD_SOLUE | Q82IC5, AHPD_STRAW | Q7AKI6, AHPD_STRCO |
| B1W2G7, AHPD_STRGG | Q9X5V1, AHPD_STRVD |
|
