Acireductone dioxygenase (iron(II)-requiring)

acireductone dioxygenase [iron(II)-requiring]
Identifiers
EC no.	1.13.11.54
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
Search PMC articles PubMed articles NCBI proteins

Acireductone dioxygenase [iron(II)-requiring] (EC 1.13.11.54) is an enzyme that catalyzes the chemical reaction

1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O₂${\displaystyle \rightleftharpoons }$ 4-(methylthio)-2-oxobutanoate + formate

Thus, the two substrates of this enzyme are 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one and oxygen, whereas its two products are 4-methylthio-2-oxobutanoate and formate.

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-forming). Other names in common use include ARD', 2-hydroxy-3-keto-5-thiomethylpent-1-ene dioxygenase (ambiguous), acireductone dioxygenase (ambiguous), E-2', and E-3 dioxygenase. This enzyme participates in methionine metabolism.

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2HJI.

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): 1193–5. 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): 287–8. doi:10.1023/A:1008396624784. PMID   10481280. S2CID   36731035.
• Dai Y, Pochapsky TC, Abeles RH (2001). "Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae". Biochemistry. 40 (21): 6379–87. 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): 6761–9. 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): 966–72. doi:10.1038/nsb863. PMID   12402029. S2CID   38098047.