Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.1.99.5 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
Search for more literature for 4.1.99.5

Cloned(Commentary)

Cloned (Comment) Organism
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

Protein Variants Comment Organism
I127G site-directed mutagenesis, increased activity compared to wild-type Prochlorococcus marinus
I127G/A48G site-directed mutagenesis, increased activity compared to wild-type Prochlorococcus marinus
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
a long-chain aldehyde + O2 + 2 NADPH + 2 H+ Prochlorococcus marinus
-
 an alkane + formate + H2O + 2 NADP+
-
 ?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+ Prochlorococcus marinus MIT 9313
-
 an alkane + formate + H2O + 2 NADP+
-
 ?

Organism

Organism UniProt Comment Textmining
Prochlorococcus marinus Q7V6D4
-
-
Prochlorococcus marinus MIT 9313 Q7V6D4
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
 Prochlorococcus marinus an alkane + formate + H2O + 2 NADP+
-
 ?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
 Prochlorococcus marinus MIT 9313 an alkane + formate + H2O + 2 NADP+
-
 ?
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+
-
 ?
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

Synonyms Comment Organism
ADO
-
 Prochlorococcus marinus
aldehyde-deformylating oxygenase
-
 Prochlorococcus marinus
PMT1231
-
 Prochlorococcus marinus

Temperature Optimum [°C]

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

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Prochlorococcus marinus

General Information

General Information Comment Organism
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