EC Number   |
Protein Variants |
Reference |
|---|
   4.1.99.5 | more |
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 | more |
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 | more |
enzyme structure analysis, comparisons of wild-type and mutant structures, overview |
-, 749212 |
| 4.1.99.5 | more |
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 | more |
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 | more |
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 | more |
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 | more |
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 | G31F |
site-directed mutagenesis |
747351 |
| 4.1.99.5 | Y21R |
site-directed mutagenesis |
-, 747351 |
