Selenate reductase

Identifiers
EC no.| 1.97.1.9
Databases
IntEnz| IntEnz view
BRENDA| BRENDA entry
ExPASy| NiceZyme view
KEGG| KEGG entry
MetaCyc| metabolic pathway
PRIAM| profile
PDB structures| RCSB PDB PDBe PDBsum
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PubMed| articles
NCBI| proteins

In enzymology, a selenate reductase (EC 1.97.1.9) is an enzyme that catalyzes the chemical reaction

selenite + H2O + acceptor  ⇌ {\displaystyle \rightleftharpoons } selenate + reduced acceptor

The 3 substrates of this enzyme are selenite, H2O, and acceptor, whereas its two products are selenate and reduced acceptor.

This enzyme belongs to the family of oxidoreductases. The systematic name of this enzyme class is selenite:reduced acceptor oxidoreductase.

## References[edit]

* Schroder I, Rech S, Krafft T, Macy JM (1997). "Purification and characterization of the selenate reductase from Thauera selenatis". J. Biol. Chem. 272 (38): 23765–8. doi:10.1074/jbc.272.38.23765. PMID 9295321.
* Macy JM, Rech S, Auling G, Dorsch M, Stackebrandt E, Sly LI (1993). "Thauera selenatis gen. nov., sp. nov., a member of the beta subclass of Proteobacteria with a novel type of anaerobic respiration". Int. J. Syst. Bacteriol. 43 (1): 135–42. doi:10.1099/00207713-43-1-135. PMID 8427805.
* Krafft T, Bowen A, Theis F, Macy JM (2000). "Cloning and sequencing of the genes encoding the periplasmic-cytochrome B-containing selenate reductase of Thauera selenatis". DNA Seq. 10 (6): 365–77. doi:10.3109/10425170009015604. PMID 10826693.
* Stolz JF, Oremland RS (1999). "Bacterial respiration of arsenic and selenium". FEMS Microbiol. Rev. 23 (5): 615–27. doi:10.1111/j.1574-6976.1999.tb00416.x. PMID 10525169.

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Other oxidoreductases (EC 1.15–1.21)

1.15: Acting on superoxide as acceptor|

* Superoxide dismutase
* SOD1
* SOD2
* SOD3

1.16: Oxidizing metal ions|

* Ceruloplasmin
* (Methionine synthase) reductase

1.17: Acting on CH or CH2 groups|

* Xanthine oxidase
* Ribonucleotide reductase
* 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase
* 7-Hydroxymethyl chlorophyll a reductase

1.18: Acting on iron–sulfur proteins as donors|

* Nitrogenase

1.19: Acting on reduced flavodoxin as donor|

* Nitrogenase (flavodoxin)

1.20: Acting on phosphorus or arsenic in donors|

* Glutaredoxin
* GLRX
* GLRX2
* GLRX3
* GLRX5

1.21: Acting on X-H and Y-H to form an X-Y bond|

* Isopenicillin N synthase
* Columbamine oxidase
* Reticuline oxidase
* Sulochrin oxidase
* (+)-bisdechlorogeodin-forming
* (-)-bisdechlorogeodin-forming
* Aureusidin synthase
* Tetrahydrocannabinolic acid synthase
* Cannabidiolic acid synthase
* Dichlorochromopyrrolate synthase

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Enzymes

Activity|

* Active site
* Binding site
* Catalytic triad
* Oxyanion hole
* Enzyme promiscuity
* Diffusion-limited enzyme
* Cofactor
* Enzyme catalysis

Regulation|

* Allosteric regulation
* Cooperativity
* Enzyme inhibitor
* Enzyme activator

Classification|

* EC number
* Enzyme superfamily
* Enzyme family
* List of enzymes

Kinetics|

* Enzyme kinetics
* Eadie–Hofstee diagram
* Hanes–Woolf plot
* Lineweaver–Burk plot
* Michaelis–Menten kinetics

Types|

* EC1 Oxidoreductases (list)
* EC2 Transferases (list)
* EC3 Hydrolases (list)
* EC4 Lyases (list)
* EC5 Isomerases (list)
* EC6 Ligases (list)
* EC7 Translocases (list)

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