ENZYME entry: EC 1.8.99.5
Accepted Name |
Dissimilatory sulfite reductase.
|
Alternative Name(s) |
Siroheme sulfite reductase. |
Reaction catalysed |
- Hydrogen sulfide + a [DsrC protein]-disulfide + 2 acceptor + 3 H(2)O <=> sulfite + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H(+)
- A [DsrC protein]-S-sulfanyl-L-cysteine + 3 acceptor + 3 H(2)O <=> sulfite + a [DsrC protein]-disulfide + 3 reduced acceptor + 2 H(+)
|
Cofactor(s) |
Siroheme.
|
Comment(s) |
- The enzyme is essential in prokaryotic sulfur-based energy
metabolism, including sulfate/sulfite reducing organisms, sulfur-
oxidizing bacteria, and organosulfonate reducers.
- In sulfur reducers it catalyzes the reduction of sulfite to sulfide,
while in sulfur oxidizers it catalyzes the opposite reaction.
- The reaction involves the small protein DsrC, which is present in all
the organisms that contain dissimilatory sulfite reductase.
- During the process an intramolecular disulfide bond is formed between
two L-cysteine residues of DsrC.
- This disulfide can be reduced by a number of proteins including DsrK
and TcmB.
- This enzyme is different from EC 1.8.1.2 and EC 1.8.7.1, which are
involved in sulfate assimilation.
|
Cross-references |
BRENDA | 1.8.99.5 |
EC2PDB | 1.8.99.5 |
ExplorEnz | 1.8.99.5 |
PRIAM enzyme-specific profiles | 1.8.99.5 |
KEGG Ligand Database for Enzyme Nomenclature | 1.8.99.5 |
IUBMB Enzyme Nomenclature | 1.8.99.5 |
IntEnz | 1.8.99.5 |
MEDLINE | Find literature relating to 1.8.99.5 |
MetaCyc | 1.8.99.5 |
Rhea expert-curated reactions | 1.8.99.5 |
UniProtKB/Swiss-Prot |
|
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