“Adenylyl-sulfate reductase (thioredoxin)”的意思、由来-开放百科全书

词条

Adenylyl-sulfate reductase (thioredoxin)

释义

Structural studies
References

{{enzyme
| Name = adenylyl-sulfate reductase (thioredoxin)
| EC_number = 1.8.4.10
| CAS_number =
| IUBMB_EC_number = 1/8/4/10
| GO_code = 0043866
| image =
| width =
| caption =
}}Adenylyl-sulfate reductase (thioredoxin) ({{EC number|1.8.4.10}}) is an enzyme that catalyzes the chemical reaction

AMP + sulfite + thioredoxin disulfide 5'-adenylyl sulfate + thioredoxin

The 3 substrates of this enzyme are adenosine monophosphate, sulfite, and thioredoxin disulfide, whereas its two products are 5'-adenylyl 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 AMP,sulfite:thioredoxin-disulfide oxidoreductase (adenosine-5'-phosphosulfate-forming). This enzyme is also called thioredoxin-dependent 5'-adenylylsulfate reductase.

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code {{PDB link|2GOY}}.

References

{{cite journal | vauthors = Bick JA, Dennis JJ, Zylstra GJ, Nowack J, Leustek T | date = 2000 | title = Identification of a New Class of 5′-Adenylylsulfate (APS) Reductases from Sulfate-Assimilating Bacteria | journal = J. Bacteriol. | volume = 182 | pages = 135–42 | pmid = 10613872 | doi = 10.1128/JB.182.1.135-142.2000 | issue = 1 | pmc = 94249 }}
{{cite journal | vauthors = Abola AP, Willits MG, Wang RC, Long SR | date = 1999 | title = Reduction of Adenosine-5′-Phosphosulfate Instead of 3′-Phosphoadenosine-5′-Phosphosulfate in Cysteine Biosynthesis by Rhizobium meliloti and Other Members of the Family Rhizobiaceae | journal = J. Bacteriol. | volume = 181 | pages = 5280–7 | pmid = 10464198 | issue = 17 | pmc = 94033 }}
{{cite journal | vauthors = Williams SJ, Senaratne RH, Mougous JD, Riley LW, Bertozzi CR | date = 2002 | title = 5'-adenosinephosphosulfate lies at a metabolic branch point in mycobacteria | journal = J. Biol. Chem. | volume = 277 | pages = 32606–15 | pmid = 12072441 | doi = 10.1074/jbc.M204613200 | issue = 36 }}
{{cite journal | vauthors = Neumann S, Wynen A, Truper HG, Dahl C | date = 2000 | title = Characterization of the cys gene locus from Allochromatium vinosum indicates an unusual sulfate assimilation pathway | journal = Mol. Biol. Rep. | volume = 27 | pages = 27–33 | pmid = 10939523 | doi = 10.1023/A:1007058421714 | issue = 1 }}

2 : EC 1.8.4|Enzymes of known structure

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