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Literature summary extracted from

  • Khara, B.; Menon, N.; Levy, C.; Mansell, D.; Das, D.; Marsh, E.N.; Leys, D.; Scrutton, N.S.
    Production of propane and other short-chain alkanes by structure-based engineering of ligand specificity in aldehyde-deformylating oxygenase (2013), ChemBioChem, 14, 1204-1208.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.99.5 recombinant expression of mutants V41Y and A134F Prochlorococcus marinus

Protein Variants

EC Number Protein Variants Comment Organism
4.1.99.5 A134F site-directed mutagenesis, the mutant has the same global architecture as wild-type enzyme, the mutant shows highly reduced activity with the majority of long-chain aldehyde substrates tested. the A134F variant displays an approximate fourfold increase in the rate of butanal consumption and approximately sixfold increase in pentanal consumption compared to wild-type enzyme, the mutant generates enhanced levels of propane production in whole-cell biotransformations compared to wild-type cADO Prochlorococcus marinus
4.1.99.5 additional information alteration of the enzyme's substrate specificity by engineering of active site residues involved in substrate binding, residues V41 and A134, adjacent to the C9 position of the ligand, might influence fatty acid binding, overview Prochlorococcus marinus
4.1.99.5 V41Y site-directed mutagenesis, the mutant has the same global architecture as wild-type enzyme, the mutant shows highly reduced activity with the majority of long-chain aldehyde substrates tested Prochlorococcus marinus
4.1.99.5 V41Y/A134F site-directed mutagenesis, the double mutant shows reduced activity with long-chain aldehyde substrates and increased activity with short-chain aldehyde substrates like the single mutants Prochlorococcus marinus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.99.5 Fe2+ di-iron centre, coordinated by two histidine residues and four carboxylates from glutamate side chains Prochlorococcus marinus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.99.5 additional information Prochlorococcus marinus natural specificity of cADO to favour reactivity against short-chain over long-chain aldehydes ?
-
 ?
4.1.99.5 additional information Prochlorococcus marinus MIT9313 natural specificity of cADO to favour reactivity against short-chain over long-chain aldehydes ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.99.5 Prochlorococcus marinus
-
-
-
4.1.99.5 Prochlorococcus marinus MIT9313
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.99.5 recombinant enzyme mutants V41Y and A134F to homogeneity Prochlorococcus marinus

Reaction

EC Number Reaction Comment Organism Reaction ID
4.1.99.5 octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+ mechanism of the unusual iron-catalysed decarbonylation reaction Prochlorococcus marinus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.99.5 butanal + O2 + 2 NADH + 2 H+ with reducing system NADH/phenazine methosulfate Prochlorococcus marinus propane + formate + H2O + 2 NAD+ GC-MS poduct analysis ?
4.1.99.5 butanal + O2 + 2 NADH + 2 H+ with reducing system NADH/phenazine methosulfate Prochlorococcus marinus MIT9313 propane + formate + H2O + 2 NAD+ GC-MS poduct analysis ?
4.1.99.5 additional information natural specificity of cADO to favour reactivity against short-chain over long-chain aldehydes Prochlorococcus marinus ?
-
 ?
4.1.99.5 additional information natural specificity of cADO to favour reactivity against short-chain over long-chain aldehydes Prochlorococcus marinus MIT9313 ?
-
 ?
4.1.99.5 octadecanal + O2 + 2 NADH + 2 H+ with reducing system NADH/phenazine methosulfate Prochlorococcus marinus heptadecane + formate + H2O + 2 NAD+ GC-MS poduct analysis ?
4.1.99.5 octadecanal + O2 + 2 NADH + 2 H+ with reducing system NADH/phenazine methosulfate Prochlorococcus marinus MIT9313 heptadecane + formate + H2O + 2 NAD+ GC-MS poduct analysis ?
4.1.99.5 pentanal + O2 + 2 NADH + 2 H+ with reducing system NADH/phenazine methosulfate Prochlorococcus marinus butane + formate + H2O + 2 NAD+ GC-MS poduct analysis ?
4.1.99.5 pentanal + O2 + 2 NADH + 2 H+ with reducing system NADH/phenazine methosulfate Prochlorococcus marinus MIT9313 butane + formate + H2O + 2 NAD+ GC-MS poduct analysis ?

Synonyms

EC Number Synonyms Comment Organism
4.1.99.5 ADO
-
 Prochlorococcus marinus
4.1.99.5 aldehyde-deformylating oxygenase
-
 Prochlorococcus marinus
4.1.99.5 cADO
-
 Prochlorococcus marinus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.99.5 37
-
 assay at Prochlorococcus marinus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.99.5 7.2
-
 assay at Prochlorococcus marinus

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.99.5 NADH
-
 Prochlorococcus marinus

General Information

EC Number General Information Comment Organism
4.1.99.5 additional information the enzyme shows a mainly alpha helical architecture, with a ferritin-like four-helix bundle. The latter contains the di-iron centre, coordinated by two histidine residues and four carboxylates from glutamate side chains. Substrates access the active site through a tunnel-like hydrophobic pocket. Active site structure analysis from crystal structure, PDB ID 20C5 Prochlorococcus marinus