To install click the Add extension button. That's it.

The source code for the WIKI 2 extension is being checked by specialists of the Mozilla Foundation, Google, and Apple. You could also do it yourself at any point in time.

4,5
Kelly Slayton
Congratulations on this excellent venture… what a great idea!
Alexander Grigorievskiy
I use WIKI 2 every day and almost forgot how the original Wikipedia looks like.
Live Statistics
English Articles
Improved in 24 Hours
Added in 24 Hours
What we do. Every page goes through several hundred of perfecting techniques; in live mode. Quite the same Wikipedia. Just better.
.
Leo
Newton
Brights
Milds

Acireductone dioxygenase (Ni2+-requiring)

From Wikipedia, the free encyclopedia

Acireductone dioxygenase (Ni2+-requiring) (EC 1.13.11.53) is an enzyme that catalyzes the chemical reaction

1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 3-(methylthio)propanoate + formate + CO

Thus, the two substrates of this enzyme are 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one and oxygen, whereas its 3 products are 3-(methylthio)propanoate, formate, and carbon monoxide.

This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one:oxygen oxidoreductase (formate- and CO-forming). Other names in common use include ARD, 2-hydroxy-3-keto-5-thiomethylpent-1-ene dioxygenase (ambiguous), acireductone dioxygenase (ambiguous), and E-2. This enzyme participates in methionine metabolism.

References

  • Wray JW, Abeles RH (1993). "A bacterial enzyme that catalyzes formation of carbon monoxide". J. Biol. Chem. 268 (29): 21466–9. doi:10.1016/S0021-9258(20)80559-6. PMID 8407993.
  • Wray JW, Abeles RH (1995). "The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases". J. Biol. Chem. 270 (7): 3147–53. doi:10.1074/jbc.270.7.3147. PMID 7852397.
  • Furfine ES, Abeles RH (1988). "Intermediates in the conversion of 5'-S-methylthioadenosine to methionine in Klebsiella pneumoniae". J. Biol. Chem. 263 (20): 9598–606. doi:10.1016/S0021-9258(19)81558-2. PMID 2838472.
  • Dai Y, Wensink PC, Abeles RH (1999). "One protein, two enzymes". J. Biol. Chem. 274 (3): 1193–1195. doi:10.1074/jbc.274.3.1193. PMID 9880484.
  • Mo H, Dai Y, Pochapsky SS, Pochapsky TC (1999). "1H, 13C and 15N NMR assignments for a carbon monoxide generating metalloenzyme from Klebsiella pneumoniae". J. Biomol. NMR. 14 (3): 287–288. doi:10.1023/A:1008396624784. PMID 10481280.
  • Dai Y, Pochapsky TC, Abeles RH (2001). "Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae". Biochemistry. 40 (21): 6379–6387. doi:10.1021/bi010110y. PMID 11371200.
  • Al-Mjeni F, Ju T, Pochapsky TC, Maroney MJ (2002). "XAS investigation of the structure and function of Ni in acireductone dioxygenase". Biochemistry. 41 (21): 6761–6769. doi:10.1021/bi012209a. PMID 12022880.
  • Pochapsky TC, Pochapsky SS, Ju T, Mo H, Al-Mjeni F, Maroney MJ (2002). "Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae". Nat. Struct. Biol. 9 (12): 966–972. doi:10.1038/nsb863. PMID 12402029.
This page was last edited on 27 March 2024, at 18:58
Basis of this page is in Wikipedia. Text is available under the CC BY-SA 3.0 Unported License. Non-text media are available under their specified licenses. Wikipedia® is a registered trademark of the Wikimedia Foundation, Inc. WIKI 2 is an independent company and has no affiliation with Wikimedia Foundation.