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Literature summary for 4.1.99.5 extracted from

  • Li, N.; Chang, W.C.; Warui, D.M.; Booker, S.J.; Krebs, C.; Bollinger, J.M.
    Evidence for only oxygenative cleavage of aldehydes to alk(a/e)nes and formate by cyanobacterial aldehyde decarbonylases (2012), Biochemistry, 51, 7908-7916.
    View publication on PubMed
Search for more literature for 4.1.99.5

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) Prochlorococcus marinus

Organism

Organism UniProt Comment Textmining
Prochlorococcus marinus
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
heptanal + O2 + 2 NAD(P)H + 2 H+ with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase Prochlorococcus marinus hexane + formate + H2O + 2 NAD(P)+
-
 ?
additional information the enzyme catalyzes the conversion of Cn fatty aldehydes to formate and the corresponding Cn-1 alk(a/e)nes. This apparently hydrolytic reaction is actually a cryptically redox oxygenation process, in which one O-atom is incorporated from O2 into formate and a protein-based reducing system (NADPH, ferredoxin, and ferredoxin reductase) provides all four electrons needed for the complete reduction of O2, absolute O2 requirement for formate production Prochlorococcus marinus ?
-
 ?
octadecanal + O2 + 2 NADH + 2 H+ with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase Prochlorococcus marinus heptadecane + formate + H2O + 2 NAD+
-
 ?

Synonyms

Synonyms Comment Organism
cyanobacterial aldehyde decarbonylase
-
 Prochlorococcus marinus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at Prochlorococcus marinus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Prochlorococcus marinus

General Information

General Information Comment Organism
additional information the definitive reaffirmation of the oxygenative nature of the reaction implies that the enzyme, initially designated as aldehyde decarbonylase when the C1-derived coproduct is thought to be carbon monoxide rather than formate, should be redesignated as aldehyde-deformylating oxygenase, ADO Prochlorococcus marinus