Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

1.4.3.2: L-amino-acid oxidase

This is an abbreviated version!
For detailed information about L-amino-acid oxidase, go to the full flat file.

Word Map on EC 1.4.3.2

Reaction

an L-amino acid
+
H2O
+
O2
=
a 2-oxo carboxylate
+
NH3
+
H2O2

Synonyms

AAD, ACTX-6, ACTX-8, Akbu-LAAO, APIT, apotxin, aromatic L-amino acid oxidase, Balt-LAAO-I, bordonein-L, Bpir-LAOO-1, CC-LPOX, DAA, Dolabellanin, escapin, head kidney and gill, IL4I1, Il4i1 protein, ink toxin 1, Interleukin Four Induced Gene 1 protein, L-AAO, L-AAO/MOG, L-AAO1, L-amino acid oxidase, L-amino acid: O2 oxidoreductase, L-amino acid:O2 oxidoreductase, L-amino acid:O2 oxidoreductase (deaminating), L-aminooxidase, L-Aox, L-phenylalanine oxidase, LAAO, LAAO-1, LAAO-I, LAAO-II, LAAO1, LAAO4, LAAOI, LAAOII, LAO, LAO1, M-LAO, ophio-amino-acid oxidase, Pm1, RoLAAO, sarA, Sebastes schlegeli antibacterial protein, Sebastes schlegelii antibacterial protein, SSAP, TJ-LAO, toxophallin, TSV-LAO

ECTree

     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.3 With oxygen as acceptor
                1.4.3.2 L-amino-acid oxidase

Engineering

Engineering on EC 1.4.3.2 - L-amino-acid oxidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N54A/N164A/N193A/N331A
mutation of the potential glycosylatoon sites, mutant enzyme has the same mobility as the lower band of 9His-LAAO4 treated with PNGaseF
H209A
non-metal coordinating mutant, the levels of iron, zinc, and magnesium are similar to those of wild-type
H348A
D165K
-
slight increase in kcat/KM value for phenylpyruvate
D165K/F263M
-
slight increase in kcat/KM value for phenylpyruvate
D165K/F263M/L336
-
2fold increase in kcat/KM value for phenylpyruvate
D165K/L336M
-
slight increase in kcat/KM value for phenylpyruvate
D165K/S179L/F263V/L336V
-
slight increase in kcat/KM value for phenylpyruvate
F263M
-
slight increase in kcat/KM value for phenylpyruvate
F263M/L336M
-
2fold increase in kcat/KM value for phenylpyruvate
L336M
-
slight increase in kcat/KM value for phenylpyruvate
D165K
-
slight increase in kcat/KM value for phenylpyruvate
-
D165K/F263M
-
slight increase in kcat/KM value for phenylpyruvate
-
D165K/S179L/F263V/L336V
-
slight increase in kcat/KM value for phenylpyruvate
-
F263M
-
slight increase in kcat/KM value for phenylpyruvate
-
L336M
-
slight increase in kcat/KM value for phenylpyruvate
-
D238A
the interaction of Asp238 with the terminal, positively charged group of the substratesis critical for substrate binding but not for catalytic control between the oxidase/monooxygenase activities
D238E
mutant displays increased catalytic activities
D238F
mutant exhibits altered substrate specificity to long hydrophobic substrates
C254I
the mutant enzyme shows 5times higher specific activity of oxidase activity than that of the wild type enzyme
additional information