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1.13.11.63: beta-carotene 15,15'-dioxygenase

This is an abbreviated version!
For detailed information about beta-carotene 15,15'-dioxygenase, go to the full flat file.

Word Map on EC 1.13.11.63

Reaction

beta-carotene
+
O2
= 2 all-trans retinal

Synonyms

BC-15,15'-oxygenase, BCM, BCMO, Bcmo1, Bcmo2, BCO, BCO1, BCO2, Bcox, beta,beta-carotene 15,15'-mono-oxygenase 1, beta,beta-carotene 15,15'-monooxygenase, beta,beta-carotene 15,15'-monooxygenase 1, beta,beta-carotene 15,15'-monooxygenase-1, beta,beta-carotene 15,15-monooxygenase 1, beta,beta-carotene-15,15'-monooxygenase, beta,beta-carotene-15,15'-oxygenase, beta-carotene 15,15' oxygenase, beta-carotene 15,15'-dioxygenase, beta-carotene 15,15'-monooxygenase, beta-carotene 15,15'-monooxygenase 1, beta-carotene 15,15'-oxygenase, beta-carotene 15,15-monooxygenase, beta-carotene dioxygenase 1, beta-carotene oxygenase 2, beta-carotene-15,15'-dioxygenase, beta-carotene-15,15'-monooxygenase, beta-carotene-15,15'-oxygenase, beta-carotene-15,15'-oxygenase-1, beta-carotene-15,15'-oxygenase-2, beta-CD, betaCDIOX, betaCO, BLH, brp/blh-family beta-carotene monooxygenase, brpA, carotenoid oxygenase, Ci-BCO, CMO1, EC 1.13.11.21, EC 1.14.99.36, NinaB

ECTree

     1 Oxidoreductases
         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
             1.13.11 With incorporation of two atoms of oxygen
                1.13.11.63 beta-carotene 15,15'-dioxygenase

Engineering

Engineering on EC 1.13.11.63 - beta-carotene 15,15'-dioxygenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A379V
-
naturally occuring polymorphism, the mutation causes 33% reduced BCMO1 activity compared to wild-type in vitro and 32% reduced conversion of beta-carotene after a pharmacological dose in female volunteers
K108F
site-directed mutagenesis, the mutant shows highly decreased affinity for substrates with ionone rings at both ends, such as alpha-carotene, beta-carotene, and beta-cryptoxanthin, and a 7.2fold increased Km for beta-carotene compared to the wild-type enzyme. But the mutation has little effect on the affinity of the enzyme for substrates with one ionone ring and one open-chain end, such as beta-apo-4'-carotenal and beta-apo-8'-carotenal
K108L
site-directed mutagenesis, the mutant shows highly decreased affinity for substrates with ionone rings at both ends, such as alpha-carotene, beta-carotene, and beta-cryptoxanthin, and a 2.9fold increased Km for beta-carotene compared to the wild-type enzyme. But the mutation has little effect on the affinity of the enzyme for substrates with one ionone ring and one open-chain end, such as beta-apo-4'-carotenal and beta-apo-8'-carotenal
N329T
-
naturally occuring polymorphism
R228C
-
naturally occuring polymorphism
R267S
-
naturally occuring polymorphism, the mutation does not show any effect on BCMO1 activity in vitro and in vivo
R267S/A379V
-
naturally occuring polymorphism, the mutation causes 57% reduced BCMO1 activity compared to wild-type in vitro and 69% reduced conversion of beta-carotene after a pharmacological dose in female volunteers
R537K
-
naturally occuring polymorphism
T170M
-
naturally occuring polymorphism, the mutant shows 90% reduced BCMO1 activity compared to wild-type in vitro causing hypercarotenemia and hypovitaminose A
T381L
T382P
-
naturally occuring polymorphism
Y236S
-
naturally occuring polymorphism
D52A
more than 50% loss of activity
D52A/E140A
no enzymatic activity
E140A
more than 50% loss of activity
E314A
little reduction in enzymatic activity
E405A
no enzymatic activity
E450A
little reduction in enzymatic activity
E457A
about 80% loss of activity
E469A
about 50% decrease in activity, cells are bleached when left growing overnight
H172A
no enzymatic activity
H174A
little reduction in enzymatic activity
H237A
no enzymatic activity
H308A
no enzymatic activity
H309A
little reduction in enzymatic activity
H49A
little reduction in enzymatic activity
H514A
no enzymatic activity
H58A
little reduction in enzymatic activity
additional information