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Results 1 - 10 of 56 > >>
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EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.5749051 Role of cysteine residues in the structure, stability, and alkane producing activity of cyanobacterial aldehyde deformylating oxygenase PLoS ONE 10 e0122217 2015 Nostoc punctiforme 25837679
Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.5749051 Role of cysteine residues in the structure, stability, and alkane producing activity of cyanobacterial aldehyde deformylating oxygenase PLoS ONE 10 e0122217 2015 Nostoc punctiforme ATCC 29133 / PCC 73102 25837679
Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.5748032 Conversion of aldehyde to alkane by a peroxoiron(III) complex a functional model for the cyanobacterial aldehyde-deformylating oxygenase J. Am. Chem. Soc. 137 7686-7691 2015 Prochlorococcus marinus 26030345
Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.5748032 Conversion of aldehyde to alkane by a peroxoiron(III) complex a functional model for the cyanobacterial aldehyde-deformylating oxygenase J. Am. Chem. Soc. 137 7686-7691 2015 Prochlorococcus marinus MIT 9313 26030345
Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.5748027 Rapid reduction of the diferric-peroxyhemiacetal intermediate in aldehyde-deformylating oxygenase by a cyanobacterial ferredoxin evidence for a free-radical mechanism J. Am. Chem. Soc. 137 11695-11709 2015 Nostoc punctiforme 26284355
Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.5748027 Rapid reduction of the diferric-peroxyhemiacetal intermediate in aldehyde-deformylating oxygenase by a cyanobacterial ferredoxin evidence for a free-radical mechanism J. Am. Chem. Soc. 137 11695-11709 2015 Nostoc punctiforme ATCC 29133 / PCC 73102 26284355
Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.5747409 Identification of residues important for the activity of aldehyde-deformylating oxygenase through investigation into the structure-activity relationship BMC Biotechnol. 17 31-39 2017 Synechococcus elongatus PCC 7942 = FACHB-805 28302170
Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.5747409 Identification of residues important for the activity of aldehyde-deformylating oxygenase through investigation into the structure-activity relationship BMC Biotechnol. 17 31-39 2017 Synechocystis sp. PCC 6803 28302170
Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.5747409 Identification of residues important for the activity of aldehyde-deformylating oxygenase through investigation into the structure-activity relationship BMC Biotechnol. 17 31-39 2017 Synechococcus elongatus PCC 7942 = FACHB-805 R2 28302170
Display the word mapDisplay the reaction diagram Show all sequences 4.1.99.5746976 Crystal structures of aldehyde deformylating oxygenase from Limnothrix sp. KNUA012 and Oscillatoria sp. KNUA011 Biochem. Biophys. Res. Commun. 477 395-400 2016 Oscillatoria sp. KNUA011 27329814
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