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1.14.13.239: carnitine monooxygenase

This is an abbreviated version!
For detailed information about carnitine monooxygenase, go to the full flat file.

Word Map on EC 1.14.13.239

Reaction

L-carnitine
+
NAD(P)H
 +
H+
 +
O2
=
(3R)-3-hydroxy-4-oxobutanoate
 +
trimethylamine
 +
NAD(P)+
 +
H2O

Synonyms

carnitine TMA lyase, CntA, cntAB, CntB, yeaWX

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.13.239 carnitine monooxygenase

Engineering

Engineering on EC 1.14.13.239 - carnitine monooxygenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D75K
mutation in putative FMN-binding residue of subunit CntB, mutant reveals a characteristic decrease of the absorption at 340 and 463 nm and the parallel reduction of the fluorescence signal at 526 nm plus a significant decrease of the cofactor content. 70% residual activity
E205D
E205Q
mutation of the bridging Glu205 residue of subunit CntA, mutant shows no detectable enzymatic activity and a moderately reduced Fe and sulfur content
S82A
mutation in putative FMN-binding residue of subunit CntB, mutant reveals a characteristic decrease of the absorption at 340 and 463 nm and the parallel reduction of the fluorescence signal at 526 nm plus a significant decrease of the cofactor content. 35% residual activity
Y203F
mutant is active
D75K
-
mutation in putative FMN-binding residue of subunit CntB, mutant reveals a characteristic decrease of the absorption at 340 and 463 nm and the parallel reduction of the fluorescence signal at 526 nm plus a significant decrease of the cofactor content. 70% residual activity
-
E205D
-
mutation of the bridging Glu205 residue of subunit CntA, mutant shows no detectable enzymatic activity and a moderately reduced Fe and sulfur content
-
E205Q
-
mutation of the bridging Glu205 residue of subunit CntA, mutant shows no detectable enzymatic activity and a moderately reduced Fe and sulfur content
-
S82A
-
mutation in putative FMN-binding residue of subunit CntB, mutant reveals a characteristic decrease of the absorption at 340 and 463 nm and the parallel reduction of the fluorescence signal at 526 nm plus a significant decrease of the cofactor content. 35% residual activity
-