phosphoadenylyl-sulfate reductase (thioredoxin) | |||||||||
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Identifiers | |||||||||
EC no. | 1.8.4.8 | ||||||||
CAS no. | 9068-63-7 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a phosphoadenylyl-sulfate reductase (thioredoxin) (EC 1.8.4.8) is an enzyme that catalyzes the chemical reaction
The 3 substrates of this enzyme are adenosine 3',5'-bisphosphate, sulfite, and thioredoxin disulfide, whereas its two products are 3'-phosphoadenylyl sulfate and thioredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is adenosine 3',5'-bisphosphate,sulfite:thioredoxin-disulfide oxidoreductase (3'-phosphoadenosine-5'-phosphosulfate-forming). Other names in common use include PAPS reductase, thioredoxin-dependent, PAPS reductase, thioredoxin:adenosine 3'-phosphate 5'-phosphosulfate reductase, 3'-phosphoadenylylsulfate reductase, thioredoxin:3'-phospho-adenylylsulfate reductase, phosphoadenosine-phosphosulfate reductase, adenosine 3',5'-bisphosphate,sulfite:oxidized-thioredoxin, and oxidoreductase (3'-phosphoadenosine-5'-phosphosulfate-forming). This enzyme participates in sulfur metabolism.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1ILO, 1WMJ, and 2O8V.
Sulfur assimilation is the process by which living organisms incorporate sulfur into their biological molecules. In plants, sulfate is absorbed by the roots and then be transported to the chloroplasts by the transipration stream where the sulfur are reduced to sulfide with the help of a series of enzymatic reactions. Furthermore, the reduced sulfur is incorporated into cysteine, an amino acid that is a precursor to many other sulfur-containing compounds. In animals, sulfur assimilation occurs primarily through the diet, as animals cannot produce sulfur-containing compounds directly. Sulfur is incorporated into amino acids such as cysteine and methionine, which are used to build proteins and other important molecules. Besides, With the rapid development of economy, the increase emission of sulfur results in environmental issues, such as acid rain and hydrogen sulfilde.
3′-Phosphoadenosine-5′-phosphosulfate (PAPS) is a derivative of adenosine monophosphate (AMP) that is phosphorylated at the 3′ position and has a sulfate group attached to the 5′ phosphate. It is the most common coenzyme in sulfotransferase reactions and hence part of sulfation pathways. It is endogenously synthesized by organisms via the phosphorylation of adenosine 5′-phosphosulfate (APS), an intermediary metabolite. In humans such reaction is performed by bifunctional 3′-phosphoadenosine 5′-phosphosulfate synthases using ATP as the phosphate donor.
Adenylyl-sulfate reductase is an enzyme that catalyzes the chemical reaction of the reduction of adenylyl-sulfate/adenosine-5'-phosphosulfate (APS) to sulfite through the use of an electron donor cofactor. The products of the reaction are AMP and sulfite, as well as an oxidized electron donor cofactor.
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Adenylyl-sulfate reductase (thioredoxin) is an enzyme that catalyzes the chemical reaction
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