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Literature summary for 1.14.13.84 extracted from

  • van den Heuvel, R.H.; Tahallah, N.; Kamerbeek, N.M.; Fraaije, M.W.; van Berkel, W.J.; Janssen, D.B.; Heck, A.J.
    Coenzyme binding during catalysis is beneficial for the stability of 4-hydroxyacetophenone monooxygenase (2005), J. Biol. Chem., 280, 32115-32121.
    View publication on PubMed
Search for more literature for 1.14.13.84

Cloned(Commentary)

Cloned (Comment) Organism
gene hapE, expression of wild-type and mutant enzymes in Escherichia coli Pseudomonas fluorescens

Protein Variants

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

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

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 [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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Pseudomonas fluorescens
-
 gene hapE
-
Pseudomonas fluorescens ACB
-
 gene hapE
-

Reaction

Reaction Comment Organism Reaction ID
(4-hydroxyphenyl)ethan-1-one + NADPH + H+ + O2 = 4-hydroxyphenyl acetate + NADP+ + H2O reaction mechanism Pseudomonas fluorescens
a

Substrates and Products (Substrate)

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

Subunits Comment Organism
dimer
-
 Pseudomonas fluorescens
More quaternary structure of wild-type and mutant enzymes, overview Pseudomonas fluorescens
octamer
-
 Pseudomonas fluorescens

Synonyms

Synonyms Comment Organism
HAPMO
-
 Pseudomonas fluorescens

Cofactor

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