Cloned (Comment) | Organism |
---|---|
gene hapE, expression of wild-type and mutant enzymes in Escherichia coli | Pseudomonas fluorescens |
Protein Variants | Comment | Organism |
---|---|---|
H61T | the H61T mutant is purified as apo-enzyme and mainly exists as a dimeric species, the binding of FAD to the enzyme restores the octameric conformation | Pseudomonas fluorescens |
R339A | site-directed mutagenesiss, the mutant shows decreased activity and affinity to NADPH compared to the wild-type enzyme, the mutant only weakly interacts with 3-aminopyridine adenine dinucleotide phosphate | Pseudomonas fluorescens |
R440A | site-directed mutagenesiss, inactive mutant, the mutant shows highly increased affinity to NADPH compared to the wild-type enzyme | Pseudomonas fluorescens |
General Stability | Organism |
---|---|
the association with the coenzyme NADPH is crucial for enzyme stability, 3-aminopyridine adenine dinucleotide phosphate highly stabilizes the inactive dimeric state of the enzyme | Pseudomonas fluorescens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
3-Aminopyridine adenine dinucleotide phosphate | cofactor analogue, tight binding to the wild-type enzyme and mutant R440A | Pseudomonas fluorescens |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
145100 | - |
mutant R339A, dimeric structure, mass spectrometry | Pseudomonas fluorescens |
145100 | - |
mutant R440A, dimeric structure, mass spectrometry | Pseudomonas fluorescens |
145200 | - |
wild-type enzyme, dimeric structure, mass spectrometry | Pseudomonas fluorescens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(4-hydroxyphenyl)ethan-1-one + NADPH + O2 | Pseudomonas fluorescens | - |
4-hydroxyphenyl acetate + NADP+ + H2O | - |
? | |
(4-hydroxyphenyl)ethan-1-one + NADPH + O2 | Pseudomonas fluorescens ACB | - |
4-hydroxyphenyl acetate + NADP+ + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas fluorescens | - |
gene hapE | - |
Pseudomonas fluorescens ACB | - |
gene hapE | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
(4-hydroxyphenyl)ethan-1-one + NADPH + H+ + O2 = 4-hydroxyphenyl acetate + NADP+ + H2O | reaction mechanism | Pseudomonas fluorescens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(4-hydroxyphenyl)ethan-1-one + NADPH + O2 | - |
Pseudomonas fluorescens | 4-hydroxyphenyl acetate + NADP+ + H2O | - |
? | |
(4-hydroxyphenyl)ethan-1-one + NADPH + O2 | - |
Pseudomonas fluorescens ACB | 4-hydroxyphenyl acetate + NADP+ + H2O | - |
? | |
additional information | the enzyme catalyzes Baeyer-Villiger oxidations of a wide range of ketones, thereby generating esters or lactones, overview | Pseudomonas fluorescens | ? | - |
? | |
additional information | the enzyme catalyzes Baeyer-Villiger oxidations of a wide range of ketones, thereby generating esters or lactones, overview | Pseudomonas fluorescens ACB | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | - |
Pseudomonas fluorescens |
More | quaternary structure of wild-type and mutant enzymes, overview | Pseudomonas fluorescens |
octamer | - |
Pseudomonas fluorescens |
Synonyms | Comment | Organism |
---|---|---|
HAPMO | - |
Pseudomonas fluorescens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | required for activity, each subunit contains a non-covalently, tightly bound FAD cofactor, binding of FAD is important for the octameric conformation | Pseudomonas fluorescens | |
additional information | complex formation between the cofactors NADPH or 3-aminopyridine adenine dinucleotide phosphate | Pseudomonas fluorescens | |
NADPH | - |
Pseudomonas fluorescens |