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4.1.1.76: arylmalonate decarboxylase

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

Word Map on EC 4.1.1.76

Reaction

2-aryl-2-methylmalonate
=
2-arylpropanoate
 +
CO2

Synonyms

AMDase, aryl/alkenyl malonate decarboxylase, Arylmalonate decarboxylase, Arylmalonate decarboxylase (Alcaligenes bronchisepticus strain KU 1201), Decarboxylase, arylmalonate, Decarboxylase, arylmalonate (Bordetella bronchiseptica clone pAMD100 reduced), Decarboxylase, arylmalonate (Bordetella bronchiseptica strain KU1201 reduced)

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.76 arylmalonate decarboxylase

Engineering

Engineering on EC 4.1.1.76 - arylmalonate decarboxylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A68C/C188S
-
no specific activity using phenylmalonate as a substrate
C101S
-
mutant enzymes Cys101Ser, Cys148Ser, Cys171Ser and Cys188Ser. CD spectra indicate that the conformational differences of Cys101Ser and Cys188Ser compared to that of the native enzyme are not significant. Only Cys188Ser shows a drastic decrease in enzyme activity, indicating that Cys188 is located at the active centre
C148S
-
mutant enzymes Cys101Ser, Cys148Ser, Cys171Ser and Cys188Ser. CD spectra indicate that the conformational differences of Cys101Ser and Cys188Ser compared to that of the native enzyme are not significant. Only Cys188Ser shows a drastic decrease in enzyme activity, indicating that Cys188 is located at the active centre
C171S
-
mutant enzymes Cys101Ser, Cys148Ser, Cys171Ser and Cys188Ser. CD spectra indicate that the conformational differences of Cys101Ser and Cys188Ser compared to that of the native enzyme are not significant. Only Cys188Ser shows a drastic decrease in enzyme activity, indicating that Cys188 is located at the active centre
C188S
G190A
the mutant shows 4.6% relative activity compared to the wild type enzyme
G190S/P14V/P15G
the mutant shows 1.9% relative activity compared to the wild type enzyme
G74C/C188G
the mutant has a 5.6fold increase in activity compared with the G74C/C188S mutant
G74C/C188S
G74C/M159L
the mutant shows 14% decarboxylation activity and 165% racemisation activity compared to mutant G74C
G74C/M159L/C188G
the mutant shows a 210fold increase in activity compared with the G74C/C188S mutant
G74C/M159L/C188G/P14V/P15G
inactive
G74C/M159L/C188G/V43I/A125P/V156l
G74C/S36N/G74C/C188S
-
enhanced activity compared to G74C/C188S
G74C/V13D/G190H
inactive
G74C/V43A
the mutant with shows a 20fold shift towards promiscuous racemisation based on a reduced activity in the decarboxylation reaction and a 2fold increase in the racemisation activity. The mutant shows an extended substrate range, with a 30fold increase in the reaction rate towards ketoprofen
L72C/C188S
-
no specific activity using phenylmalonate as a substrate
L77C/C188S
-
no specific activity using phenylmalonate as a substrate
M159C
the mutant shows 1.4% relative activity compared to the wild type enzyme using phenylmalonate or methyl(phenyl)propanedioic acid as substrate, the mutant shows 1.7% relative activity compared to the wild type enzyme using 2-hydroxy-2-phenylmalonic acid as substrate
M159G
the mutant shows 19% relative activity compared to the wild type enzyme
M159S
the mutant shows 2.6% relative activity compared to the wild type enzyme
M159V
M73C/C188S
-
no specific activity using phenylmalonate as a substrate
P14V/P15G
S36N
-
activity is about 1/10 compared to that of the wild-type enzyme
S36N/G74C/C188S
S71C/C188S
-
mutant exhibits decarboxylation activity and gives the opposite enantiomer to that formed by the wild type enzyme
S76C/C188S
-
no specific activity using phenylmalonate as a substrate
T75C/C188S
-
no specific activity using phenylmalonate as a substrate
V69C/C188S
-
no specific activity using phenylmalonate as a substrate
V70C/C188S
-
no specific activity using phenylmalonate as a substrate
Y48F/G74C/C188G
the mutant shows a 23fold increase in activity compared with the G74C/C188S mutant
Y48F/G74C/M159L/C188G
the mutant shows a 920fold activity increase relative to the G74C/C188S mutant
C188S
-
in contrast to the bellshaped pH profile of the wild-type enzyme, the activity of the mutant enzyme C188S retains its full activity from pH 6.0 to pH 11.0
-
A68C/C188S
-
no specific activity using phenylmalonate as a substrate
-
C188S
-
mutant exhibits decarboxylation activity and gives the opposite enantiomer to that formed by the wild type enzyme
-
G74C
-
exhibits racemisation activity towards arylpropionates, in addition to its original decarboxylase activity
-
G74C/C188S
S71C/C188S
-
mutant exhibits decarboxylation activity and gives the opposite enantiomer to that formed by the wild type enzyme
-
V69C/C188S
-
no specific activity using phenylmalonate as a substrate
-