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Literature summary for 1.1.3.7 extracted from

  • Hernandez-Ortega, A.; Lucas, F.; Ferreira, P.; Medina, M.; Guallar, V.; Martinez, A.T.
    Role of active site histidines in the two half-reactions of the aryl-alcohol oxidase catalytic cycle (2012), Biochemistry, 51, 6595-6608.
    View publication on PubMed
Search for more literature for 1.1.3.7

Cloned(Commentary)

Cloned (Comment) Organism
gene aao, expression of wild-type and mutant emzymes in Escherichia coli Pleurotus eryngii

Protein Variants

Protein Variants Comment Organism
H502A site-directed mutagenesis, the mutant shows over 1800fold decreased both catalytic and transient-state reduction constants for 4-methoxybenzyl alcohol, as well as a strong decrease in the alcohol affinity, compared to the wild-type enzyme Pleurotus eryngii
H502S site-directed mutagenesis, the mutant shows over 1200fold decreased both catalytic and transient-state reduction constants for 4-methoxybenzyl alcohol, as well as a strong decrease in the alcohol affinity compared to the wild-type enzyme Pleurotus eryngii
H546A site-directed mutagenesis, the mutant shows over 35fold decreased both catalytic and transient-state reduction constants for 4-methoxybenzyl alcohol, as well as a strong decrease in the alcohol affinity compared to the wild-type enzyme Pleurotus eryngii
H546S site-directed mutagenesis, the mutant shows decreased both catalytic and transient-state reduction constants for 4-methoxybenzyl alcohol, as well as a strong decrease in the alcohol affinity compared to the wild-type enzyme Pleurotus eryngii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten steady-state and transient-state kinetics of overall and half-reactions of wild-type and mutant enzymes by (anaerobic) stopped-flow spectrophotometry, changes in the flavin redox state, detailed overview Pleurotus eryngii
0.049
-
 4-methoxybenzyl alcohol pH 6.0, 25°C, wild-type enzyme Pleurotus eryngii
0.31
-
 4-methoxybenzyl alcohol pH 6.0, 25°C, mutant H546A Pleurotus eryngii
1.16
-
 4-methoxybenzyl alcohol pH 6.0, 25°C, mutant H546S Pleurotus eryngii
1.289
-
 4-methoxybenzyl alcohol pH 6.0, 25°C, mutant H502S Pleurotus eryngii
3.82
-
 4-methoxybenzyl alcohol pH 6.0, 25°C, mutant H502A Pleurotus eryngii

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Pleurotus eryngii
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-methoxybenzyl alcohol + O2 Pleurotus eryngii i.e. 4-anisyl alcohol 4-methoxybenzaldehyde + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Pleurotus eryngii O94219
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant emzymes from Escherichia coli to homogeneity Pleurotus eryngii

Reaction

Reaction Comment Organism Reaction ID
an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2 two conserved histidine residues, His502 and His546, are involved in catalysis and play roles in the two half-reactions, with a stronger histidine involvement in the reductive than in the oxidative half-reaction. His502 is the catalytic base in the AAO reductive half-reaction. The His502 proton transfer does not limit the oxidative half-reaction, stereoselective hydride transfer. Quantum mechanical/molecular mechanical study, mutational analysis, and computational simulations, detailed overview Pleurotus eryngii
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-methoxybenzyl alcohol + O2 i.e. 4-anisyl alcohol Pleurotus eryngii 4-methoxybenzaldehyde + H2O2
-
 ?

Synonyms

Synonyms Comment Organism
AAO
-
 Pleurotus eryngii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Pleurotus eryngii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.069
-
 4-methoxybenzyl alcohol pH 6.0, 25°C, mutant H502S Pleurotus eryngii
0.072
-
 4-methoxybenzyl alcohol pH 6.0, 25°C, mutant H502A Pleurotus eryngii
3.5
-
 4-methoxybenzyl alcohol pH 6.0, 25°C, mutant H546A Pleurotus eryngii
17
-
 4-methoxybenzyl alcohol pH 6.0, 25°C, mutant H546S Pleurotus eryngii
197
-
 4-methoxybenzyl alcohol pH 6.0, 25°C, wild-type enzyme Pleurotus eryngii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 assay at Pleurotus eryngii

pH Range

pH Minimum pH Maximum Comment Organism
3 9 pH-dependencies of wild-type and mutant enzymes, overview Pleurotus eryngii

Cofactor

Cofactor Comment Organism Structure
FAD changes in the flavin redox state during catalysis, overview Pleurotus eryngii

General Information

General Information Comment Organism
evolution the enzyme belongs to the glucose–methanol–choline oxidase superfamily Pleurotus eryngii
physiological function the flavoenzyme aryl-alcohol oxidase is involved in lignin degradation Pleurotus eryngii

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.019
-
 4-methoxybenzyl alcohol pH 6.0, 25°C, mutant H502S Pleurotus eryngii
0.054
-
 4-methoxybenzyl alcohol pH 6.0, 25°C, mutant H502A Pleurotus eryngii
3
-
 4-methoxybenzyl alcohol pH 6.0, 25°C, mutant H546S Pleurotus eryngii
53
-
 4-methoxybenzyl alcohol pH 6.0, 25°C, mutant H546A Pleurotus eryngii
3980
-
 4-methoxybenzyl alcohol pH 6.0, 25°C, wild-type enzyme Pleurotus eryngii