4.1.99.5 A118F site-directed mutagenesis, the mutant shows increased activity with n-butanal compared to the wild-type enzyme. A118F does not show any obvious activity against C14,16,18 aldehydes, and only exhibits slight activity towards n-dodecanal and n-decanal for long-chain substrates 747351 4.1.99.5 A121F site-directed mutagenesis, the mutant shows increased activity with C4,6,7 aldehydes compared to the wild-type enzyme 747351 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 -, 727312 4.1.99.5 A134F site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type -, 748564 4.1.99.5 C107A site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme -, 749051 4.1.99.5 C107A/C117A site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme -, 749051 4.1.99.5 C117A site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme -, 749051 4.1.99.5 C70F site-directed mutagenesis, the mutant shows increased activity with n-hexanal compared to the wild-type enzyme 747351 4.1.99.5 C71A site-directed mutagenesis, the mutant shows reduced hydrocarbon producing activity and facilitated formation of a dimer compared to wild-type enzyme -, 749051 4.1.99.5 C71A/C107A site-directed mutagenesis, the mutant has reduced activity compared to wild-type, and an activity comparable to or even lower than the activity of the C71A variant 749051 4.1.99.5 C71A/C107A/C117A site-directed mutagenesis, the mutant has reduced activity compared to wild-type, and an activity comparable to or even lower than the activity of the C71A variant 749051 4.1.99.5 C71A/C117A site-directed mutagenesis, the mutant has reduced activity compared to wild-type, and an activity comparable to or even lower than the activity of the C71A variant 749051 4.1.99.5 C71S site-directed mutagenesis, the mutant shows reduced hydrocarbon producing activity and facilitated formation of a dimer compared to wild-type enzyme -, 749051 4.1.99.5 D143A site-directed mutagenesis, altered activity compared to wild-type -, 747409 4.1.99.5 D49H site-directed mutagenesis, altered activity compared to wild-type 747409 4.1.99.5 D49H/N123H site-directed mutagenesis, altered activity compared to wild-type 747409 4.1.99.5 F150Y site-directed mutagenesis, altered activity compared to wild-type 747409 4.1.99.5 F86Y/F87Y site-directed mutagenesis, structure comparison with the wild-type enzyme -, 749212 4.1.99.5 F87Y site-directed mutagenesis, the mutant shows increased activity with n-decanal compared to the wild-type enzyme -, 747351 4.1.99.5 G31F site-directed mutagenesis 747351 4.1.99.5 I127G site-directed mutagenesis, increased activity compared to wild-type -, 747353 4.1.99.5 I127G/A48G site-directed mutagenesis, increased activity compared to wild-type -, 747353 4.1.99.5 I24Y site-directed mutagenesis, the mutant shows increased activity with n-heptanal compared to the wild-type enzyme -, 747351 4.1.99.5 I27F site-directed mutagenesis, the mutant shows increased activity with n-decanal and n-dodecanal compared to the wild-type enzyme 747351 4.1.99.5 L146T site-directed mutagenesis, altered activity compared to wild-type 747409 4.1.99.5 L148R site-directed mutagenesis, altered activity compared to wild-type 747409 4.1.99.5 L194A site-directed mutagenesis, the mutant has kinetic properties very similar to the wild-type enzyme -, 746597 4.1.99.5 L198F site-directed mutagenesis, the mutant shows increased activity with C7-10 aldehydescompared to the wild-type enzyme -, 747351 4.1.99.5 M193Y site-directed mutagenesis, the mutant shows increased activity with C6-10 aldehydes compared to the wild-type enzyme 747351 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 -, 727312 4.1.99.5 additional information cADO is engineered to improve specificity for short- to medium-chain aldehydes, site-directed mutagenesis of some residues in analogy to the more active enzyme from Prochlorococcus marinus strain MIT9313 -, 747409 4.1.99.5 additional information enzyme structure analysis, comparisons of wild-type and mutant structures, overview -, 749212 4.1.99.5 additional information installation of a recombinant hydrocarbon production system in Escherichia coli strain BL21(DE3)DELTAyqhDDELTAahr for production of n-alkanes by a combinant ion of four enzymes, i.e. aldehyde deformylating oxygenase (from Nostoc punctiforme ), ferredoxin (from Synechocystis), phosphopantetheinyl transferase (from Bacillus subtilis) and carboxylic acid reductase (from Mycobacterium marinum), method optimization and evaluation, overview. GC-MS analysis of the volatile alkanes produced. Comparison of ADO orthologues from different origins in hydrocarbon biosynthesis in vivo -, 748564 4.1.99.5 additional information installation of a recombinant hydrocarbon production system in Escherichia coli strain BL21(DE3)DELTAyqhDDELTAahr for production of n-alkanes by a combinant ion of four enzymes, i.e. aldehyde deformylating oxygenase (from Prochlorococcus marinus, wild-type and mutant A134F), ferredoxin (from Synechocystis), phosphopantetheinyl transferase (from Bacillus subtilis) and carboxylic acid reductase (from Mycobacterium marinum), method optimization and evaluation, overview. GC-MS analysis of the volatile alkanes produced. Comparison of ADO orthologues from different origins in hydrocarbon biosynthesis in vivo -, 748564 4.1.99.5 additional information installation of a recombinant hydrocarbon production system in Escherichia coli strain BL21(DE3)DELTAyqhDDELTAahr for production of n-alkanes by a combinant ion of four enzymes, i.e. aldehyde deformylating oxygenase (from Synechococcus sp. RS9917), ferredoxin (from Synechocystis), phosphopantetheinyl transferase (from Bacillus subtilis) and carboxylic acid reductase (from Mycobacterium marinum), method optimization and evaluation, overview. GC-MS analysis of the volatile alkanes produced. Comparison of ADO orthologues from different origins in hydrocarbon biosynthesis in vivo 748564 4.1.99.5 additional information installation of a recombinant hydrocarbon production system in Escherichia coli strain BL21(DE3)DELTAyqhDDELTAahr for production of n-alkanes by a combinant ion of four enzymes, i.e. aldehyde deformylating oxygenase (from Synechocystis sp. PCC 6803), ferredoxin (from Synechocystis), phosphopantetheinyl transferase (from Bacillus subtilis) and carboxylic acid reductase (from Mycobacterium marinum), method optimization and evaluation, overview. GC-MS analysis of the volatile alkanes produced. Comparison of ADO orthologues from different origins in hydrocarbon biosynthesis in vivo 748564 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 -, 747353 4.1.99.5 additional information structure-guided protein engineering to alter substrate specificity of aldehyde-deformylating oxygenase towards aldehydes carbon chain length. The impact of the engineered cADO mutants on the change of the hydrocarbon profile is demonstrated by co-expressing acyl-ACP thioesterase BTE, fadD and V184F in Escherichia coli, showing that n-undecane is the main fatty alkane -, 747351 4.1.99.5 N123H site-directed mutagenesis, altered activity compared to wild-type 747409 4.1.99.5 N149A site-directed mutagenesis, altered activity compared to wild-type 747409 4.1.99.5 Q110L site-directed mutagenesis, altered activity compared to wild-type 747409 4.1.99.5 Q49H/F150Y site-directed mutagenesis, altered activity compared to wild-type 747409 4.1.99.5 Q49H/N123H/F150Y site-directed mutagenesis, altered activity compared to wild-type 747409 4.1.99.5 R62A site-directed mutagenesis, altered activity compared to wild-type -, 747409 4.1.99.5 T146L site-directed mutagenesis, altered activity compared to wild-type 747409 4.1.99.5 V184F site-directed mutagenesis, the mutant shows increased activity with n-dodecanal and n-decanal compared to the wild-type enzyme 747351 4.1.99.5 V28F site-directed mutagenesis, the mutant shows increased activity with n-dodecanal compared to the wild-type enzyme 747351 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 -, 727312 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 -, 727312 4.1.99.5 W178R site-directed mutagenesis, altered activity compared to wild-type 747409 4.1.99.5 Y122F site-directed mutagenesis, altered activity compared to wild-type -, 747409 4.1.99.5 Y122F site-directed mutagenesis, structure comparison with the wild-type enzyme -, 749212 4.1.99.5 Y150F site-directed mutagenesis, altered activity compared to wild-type 747409 4.1.99.5 Y21R site-directed mutagenesis -, 747351 4.1.99.5 Y39F site-directed mutagenesis, altered activity compared to wild-type -, 747409