1.13.12.9: phenylalanine 2-monooxygenase
This is an abbreviated version!
For detailed information about phenylalanine 2-monooxygenase, go to the full flat file.
Word Map on EC 1.13.12.9
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1.13.12.9
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fad
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l-methionine
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proenzyme
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l-tyrosine
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purple
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ammonia
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flavin
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l-amino
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noncatalytic
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l-met
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prosequence
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charge-transfer
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analysis
- 1.13.12.9
- fad
- l-methionine
- proenzyme
- l-tyrosine
-
purple
- ammonia
- flavin
-
l-amino
-
noncatalytic
- l-met
-
prosequence
-
charge-transfer
- analysis
Reaction
Synonyms
L-Phe oxidase, L-phenylalanine oxidase, L-phenylalanine oxidase (deaminating and decarboxylating), oxidase, phenylalanine (deaminating, decarboxylating), PAOpt, proPAO
ECTree
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Engineering
Engineering on EC 1.13.12.9 - phenylalanine 2-monooxygenase
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M142A
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kcat is 1/10 of the wild-type enzyme, Km is elevated, affinity for oxygen seems decreased
R143A
R143K
Y536A
Y536F
M142A
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kcat is 1/10 of the wild-type enzyme, Km is elevated, affinity for oxygen seems decreased
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R143A
R143K
Y536F
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mutant enzyme shows 17fold lower activity compared to wild-type. Wild-type PAOpt produces higher amounts of phenylacetamide (PAM) than phenylpyruvate (PPV) as expected, but PAM is not produced by the R143K and Y536F mutants
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mutant enzyme shows 400fold lower activity compared to wild-type. Wild-type PAOpt produces higher amounts of phenylacetamide (PAM) than phenylpyruvate (PPV) as expected, but PAM is not produced by the R143K and Y536F mutants
R143K
the mutant has about 400fold lower activity than the wild type enzyme
mutant enzyme shows 17fold lower activity compared to wild-type. Wild-type PAOpt produces higher amounts of phenylacetamide (PAM) than phenylpyruvate (PPV) as expected, but PAM is not produced by the R143K and Y536F mutants
Y536F
the mutant has about 17fold lower activity than the wild type enzyme
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mutant enzyme shows 400fold lower activity compared to wild-type. Wild-type PAOpt produces higher amounts of phenylacetamide (PAM) than phenylpyruvate (PPV) as expected, but PAM is not produced by the R143K and Y536F mutants
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R143K
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the mutant has about 400fold lower activity than the wild type enzyme
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