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Literature summary extracted from

  • Park, A.K.; Kim, I.S.; Jeon, B.W.; Roh, S.J.; Ryu, M.Y.; Baek, H.R.; Jo, S.W.; Kim, Y.S.; Park, H.; Lee, J.H.; Yoon, H.S.; Kim, H.W.
    Crystal structures of aldehyde deformylating oxygenase from Limnothrix sp. KNUA012 and Oscillatoria sp. KNUA011 (2016), Biochem. Biophys. Res. Commun., 477, 395-400 .
    View publication on PubMed

Application

EC Number Application Comment Organism
4.1.99.5 biofuel production the cyanobacterial aldehyde deformylating oxygenase (cADO) is a key enzyme that catalyzes the unusual deformylation of aliphatic aldehydes for alkane biosynthesis and can be applied to the production of biofuel in vitro and in vivo Limnothrix redekei
4.1.99.5 biofuel production the cyanobacterial aldehyde deformylating oxygenase (cADO) is a key enzyme that catalyzes the unusual deformylation of aliphatic aldehydes for alkane biosynthesis and can be applied to the production of biofuel in vitro and in vivo Oscillatoria sp. KNUA011

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.99.5 sequence comparisons Limnothrix redekei
4.1.99.5 sequence comparisons Oscillatoria sp. KNUA011

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.99.5 crystal structure determination and analysis Limnothrix redekei
4.1.99.5 crystal structure determination and analysis Oscillatoria sp. KNUA011

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.99.5 a long-chain aldehyde + O2 + 2 NADPH + 2 H+ Limnothrix redekei
-
 an alkane + formate + H2O + 2 NADP+
-
 ?
4.1.99.5 a long-chain aldehyde + O2 + 2 NADPH + 2 H+ Oscillatoria sp. KNUA011
-
 an alkane + formate + H2O + 2 NADP+
-
 ?
4.1.99.5 a long-chain aldehyde + O2 + 2 NADPH + 2 H+ Limnothrix redekei KNUA012
-
 an alkane + formate + H2O + 2 NADP+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.99.5 Limnothrix redekei A0A191T893
-
-
4.1.99.5 Limnothrix redekei KNUA012 A0A191T893
-
-
4.1.99.5 Oscillatoria sp. KNUA011 A0A191T887
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.99.5 a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
 Limnothrix redekei an alkane + formate + H2O + 2 NADP+
-
 ?
4.1.99.5 a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
 Oscillatoria sp. KNUA011 an alkane + formate + H2O + 2 NADP+
-
 ?
4.1.99.5 a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
 Limnothrix redekei KNUA012 an alkane + formate + H2O + 2 NADP+
-
 ?
4.1.99.5 additional information substrate binding site analysis Limnothrix redekei ?
-
 ?
4.1.99.5 additional information substrate binding site analysis Oscillatoria sp. KNUA011 ?
-
 ?
4.1.99.5 additional information substrate binding site analysis Limnothrix redekei KNUA012 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.99.5 More secondary structure element analysis. OsADO structure resembles ADO structures with active sites containing both metal co-factor and substrate Oscillatoria sp. KNUA011
4.1.99.5 More secondary structure element analysis. The LiADO structure resembles ADO structures with an empty active site Limnothrix redekei

Synonyms

EC Number Synonyms Comment Organism
4.1.99.5 aldehyde deformylating oxygenase
-
 Limnothrix redekei
4.1.99.5 aldehyde deformylating oxygenase
-
 Oscillatoria sp. KNUA011
4.1.99.5 LiADO
-
 Limnothrix redekei
4.1.99.5 OsADO
-
 Oscillatoria sp. KNUA011

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.99.5 37
-
 assay at Limnothrix redekei
4.1.99.5 37
-
 assay at Oscillatoria sp. KNUA011

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.99.5 7.4
-
 assay at Limnothrix redekei
4.1.99.5 7.4
-
 assay at Oscillatoria sp. KNUA011

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.99.5 NADPH
-
 Limnothrix redekei
4.1.99.5 NADPH
-
 Oscillatoria sp. KNUA011

General Information

EC Number General Information Comment Organism
4.1.99.5 additional information the enzyme structure consists of eight a-helices found in ferritin-like di-iron proteins. Residues Tyr21, Ile27, Val28, Phe67, Phe86, Phe87, Phe117, Ala118, Ala121, Tyr122, Try125, and Tyr184 contributing to substrate binding, and Glu32, Glu60, His63, Glu115, Glu144, and His147 participating in iron coordination. OsADO structure resembles ADO structures with active sites containing both metal co-factor and substrate, OsADO active site is fully occupied, helix 5 of OsADO with an iron bound in the active site is a long helix Oscillatoria sp. KNUA011
4.1.99.5 additional information the enzyme structure consists of eight a-helices found in ferritin-like di-iron proteins. Residues Tyr21, Ile27, Val28, Phe67, Phe86, Phe87, Phe117, Ala118, Ala121, Tyr122, Try125, and Tyr184 contributing to substrate binding, and Glu32, Glu60, His63, Glu115, Glu144, and His147 participating in iron coordination. The LiADO structure resembles ADO structures with an empty active site, the LiADO active site is vacant of iron and substrates, helix 5 of LiADO, which lacks iron in the active site, presents two conformations (one long and two short helices), indicating that an equilibrium exists between the two states in solution Limnothrix redekei
4.1.99.5 physiological function the cyanobacterial aldehyde deformylating oxygenase (cADO) is a key enzyme that catalyzes the unusual deformylation of aliphatic aldehydes for alkane biosynthesis Limnothrix redekei
4.1.99.5 physiological function the cyanobacterial aldehyde deformylating oxygenase (cADO) is a key enzyme that catalyzes the unusual deformylation of aliphatic aldehydes for alkane biosynthesis Oscillatoria sp. KNUA011