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Literature summary extracted from

  • Zhang, L.; Liang, Y.; Wu, W.; Tan, X.; Lu, X.
    Microbial synthesis of propane by engineering valine pathway and aldehyde-deformylating oxygenase (2016), Biotechnol. Biofuels, 9, 80 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.99.5 gene PMT1231, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain BW25113(DE3) DELTA13 Prochlorococcus marinus

Protein Variants

EC Number Protein Variants Comment Organism
4.1.99.5 I127G site-directed mutagenesis, increased activity compared to wild-type Prochlorococcus marinus
4.1.99.5 I127G/A48G site-directed mutagenesis, increased activity compared to wild-type Prochlorococcus marinus
4.1.99.5 additional information screening for Prochlorococcus marinus enzyme ADO mutants generated by engineering the active center to accommodate branched-chain isobutyraldehyde, identification of two ADO mutants, I127G and I127G/A48G, which exhibit higher catalytic activity for isobutyraldehyde and 3fold improved propane productivity compared to wild-type, propane biosynthesis generation 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 a long-chain aldehyde + O2 + 2 NADPH + 2 H+ Prochlorococcus marinus
-
 an alkane + formate + H2O + 2 NADP+
-
 ?
4.1.99.5 a long-chain aldehyde + O2 + 2 NADPH + 2 H+ Prochlorococcus marinus MIT 9313
-
 an alkane + formate + H2O + 2 NADP+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.99.5 Prochlorococcus marinus Q7V6D4
-
-
4.1.99.5 Prochlorococcus marinus MIT 9313 Q7V6D4
-
-

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+
-
 Prochlorococcus marinus an alkane + formate + H2O + 2 NADP+
-
 ?
4.1.99.5 a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
 Prochlorococcus marinus MIT 9313 an alkane + formate + H2O + 2 NADP+
-
 ?
4.1.99.5 isobutyraldehyde + O2 + 2 NADPH + 2 H+ low activity with the wild-type enzyme, but increased activity with enzyme mutants I127G and I127G/A48G Prochlorococcus marinus propane + formate + H2O + 2 NADP+
-
 ?
4.1.99.5 isobutyraldehyde + O2 + 2 NADPH + 2 H+ low activity with the wild-type enzyme, but increased activity with enzyme mutants I127G and I127G/A48G Prochlorococcus marinus MIT 9313 propane + formate + H2O + 2 NADP+
-
 ?

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 PMT1231
-
 Prochlorococcus marinus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.99.5 25
-
 assay at Prochlorococcus marinus

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.99.5 NADPH
-
 Prochlorococcus marinus

General Information

EC Number General Information Comment Organism
4.1.99.5 physiological function enzyme ADO natively catalyzes the conversion of long-chain aldehydes into corresponding alkanes. To convert short-chain isobutyraldehyde into propane efficiently, the substrate specificity of ADO has to be modified for the utilization of the short-chain aldehydes Prochlorococcus marinus