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

BRENDA support

4.1.1.1: pyruvate decarboxylase

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

Word Map on EC 4.1.1.1

Reaction

a 2-oxo carboxylate
=
an aldehyde
 +
CO2

Synonyms

2-oxo acid carboxylyase, 8-10 nm cytoplasmic filament-associated protein, acetohydroxyacid synthase, AHAS, alpha-Carboxylase, alpha-Keto acid carboxylase, ANC27, bifunctional pyruvate decarboxylase/pyruvate ferredoxin oxidoreductase, Decarboxylase, pyruvate, GPDC1, IFPL730, KivD, KlPDC, KviD, NcPDC, P59NC, PDC, PDC I, PDC II, PDC1, Pdc1p, PDC2, PDC3, PDC4, Pdc5, Pdc5p, Pdc6, PDCS.c., PDCZ.m., PDHC, POR, pyruvamide-activated yeast pyruvate decarboxylase, pyruvate decarboxylase, pyruvate decarboxylase 1, pyruvate decarboxylase 2, pyruvate decarboxylase complex, Pyruvic decarboxylase, R-selective pyruvate decarboxylase, SCPDC, scpdc1, ScPDC5, TTHA1213, yeast pyruvate decarboxylase, YPDC, ZbPDC, ZmPDC

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.1 pyruvate decarboxylase

Engineering

Engineering on EC 4.1.1.1 - pyruvate decarboxylase

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
D28A
-
the mutant is almost catalytically inactive
E477Q
-
the mutant is almost catalytically inactive
F381W
-
site-directed mutagenesis, mutation of KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, alters the substrate specificity to a pyruvate decarboxylase showing high kcat and activity with pyruvate compared to the wild-type enzyme
M538W
-
site-directed mutagenesis, mutation of KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, alters the substrate specificity to a pyruvate decarboxylase showing higher kcat and activity with pyruvate compared to the wild-type enzyme
S286Y
-
site-directed mutagenesis, mutation of KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, alters the substrate specificity to a pyruvate decarboxylase showing high kcat and activity with pyruvate compared to the wild-type enzyme
V461I
-
site-directed mutagenesis, mutation of KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, alters the substrate specificity to a pyruvate decarboxylase showing higher kcat and activity with pyruvate compared to the wild-type enzyme
A143T/T156A/Q367H/N396I/K478R
A287G
-
the mutant shows reduced activity compared to the wild type enzyme
C221A
C221A/C222A
C221D
-
mutant with nearly wild-type activity, hyperbolic kinetics
C221D/C222A
-
double mutant with 70% of wild-type activity, but reduced Hill coefficient of 1, no substrate activation, effect on transition states, kinetics
C221E
-
mutant with nearly wild-type activity, hyperbolic kinetics
C221E/C222A
C221S
C222A
-
still possesses 20-30% specific activity compared to the wild type enzyme and can still be inhibited by the (E)-4-(4-chlorophenyl)-2-oxo-3-butenoic acid class of inhibitors/substrate analogues as well as cinnamaldehydes
D291A
-
site-directed mutagenesis, the mutant shows altered kinetics with highly reduced kcat compared to the wild-type enzyme
D291N
-
site-directed mutagenesis, the mutant shows altered kinetics with highly reduced activity compared to the wild-type enzyme
E477Q
E477Q/E91D
-
retains catalytic activity
E51A
-
site-directed mutagenesis of the active site residue, the mutant shows reduced activity compared to the wild-type enzyme,and the mutant is no longer capable of forming a hydrogen bond with cofactor thiamine diphosphate
E51D/E91D
-
no residual catalytic activity
E51N
-
site-directed mutagenesis of the active site residue, the mutant is still capable of forming a hydrogen bond with cofactor thiamine diphosphate, albeit weaker, and shows reduced activity compared to the wild-type enzyme
E51Q
-
site-directed mutagenesis of the active site residue, the mutant is still capable of forming a hydrogen bond with cofactor thiamine diphosphate, albeit weaker, and shows reduced activity compared to the wild-type enzyme
E91A
-
mutant with 30fold reduced specific activity, reduced turnover number and catalytic efficiency, abolished cooperativity, reduced thermal stability, impaired ability to bind the cofactors
E91Q
-
mutant with 4fold reduced specific activity, reduced turnover number and catalytic efficiency, abolished cooperativity, reduced thermal stability, impaired ability to bind the cofactors
H114F
H115F
H225F
-
the mutant shows reduced activity compared to the wild type enzyme
H310F
-
the mutant shows reduced activity compared to the wild type enzyme
H92F
-
the mutant shows wild type activity
L111A
-
site-directed mutagenesis, the mutant shows 47% of the wild-type kcat
L111Q
-
site-directed mutagenesis, the mutant shows 73% of the wild-type kcat
L111V
-
site-directed mutagenesis, the mutant shows 21% of the wild-type kcat
N293A
-
site-directed mutagenesis, the mutant shows altered kinetics with highly reduced kcat compared to the wild-type enzyme
S298A
-
site-directed mutagenesis, the mutant shows altered kinetics with highly reduced kcat compared to the wild-type enzyme
S300A
-
site-directed mutagenesis, the mutant shows altered kinetics with slightly reduced kcat compared to the wild-type enzyme
S311A
-
the mutant shows reduced activity compared to the wild type enzyme
T294A
-
site-directed mutagenesis, the mutant shows altered kinetics with highly reduced kcat compared to the wild-type enzyme
W412A
-
mutant with 10fold reduced specific activity, reduced turnover number and catalytic efficiency, very much reduced substrate activation, reduced affinity for thiamine diphosphate, reduced stability
W412F
-
mutant with 4fold reduced specific activity, reduced turnover number and catalytic efficiency
H747R
mutation leads to 3fold increased acetaldehyde formation, with 30% decrease in acetolactate formation
Y35N/K139R/V172A/H474R
shows 3.1fold higher acetaldehyde-forming activity than the wild-type
H747R
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
mutation leads to 3fold increased acetaldehyde formation, with 30% decrease in acetolactate formation
-
Y35N/K139R/V172A/H474R
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
shows 3.1fold higher acetaldehyde-forming activity than the wild-type
-
D27E
-
0.072% of wild-type specific activity, small decrease in affinity for cofactors thiamine diphosphate and Mg2+, kinetic properties, mutation slows the decarboxylation step
D27N
-
0.049% of wild-type specific activity, small decrease in affinity for cofactors thiamine diphosphate and Mg2+, kinetic properties, mutation slows the decarboxylation step
D440E
-
active, but unlike the wild type enzyme, exhibits a lag phase in product formation which can be reduced by preincubation with 5 mM thiamine diphosphate. Mutant N467D shows decreased affinity for thiamine diphosphate
E473D
E473N
-
inactive
E473Q
E50D
-
2.9% of wild-type activity
E50Q
-
0.46% of wild-type activity
I472A
-
mutation influences the decarboxylation and carboligation reactions. The enlarged substrate-binding site allows the decarboxylation of longer aliphatic 2-keto acids (C4-C6) as well as aromatic 2-keto acids besides pyruvate, yielding hydroxypropiophenone, benzoin and phenylacetylcarbinol. Mutation impairs enantioselectivity
I472A/I476F
increase in substrate binding affinity and specificity, highest enantioselectivity for (S)-acetoin, very low yield of product
I476A
-
mutation influences the decarboxylation and carboligation reactions and impairs enantioselectivity
I476E
-
mutation influences the decarboxylation and carboligation reactions and impairs enantioselectivity
I476F
rapid loss of cofactor thiamine diphosphate. Improvement of enantioselectivity for (S)-acetoin
I476L
-
mutation influences the decarboxylation and carboligation reactions and impairs enantioselectivity
I476V
-
mutation influences the decarboxylation and carboligation reactions and impairs enantioselectivity
mutant I472A
2fold decrease in pyruvate decarboxylase activity, switch in substrate specificity to catalyse decarboxylation of benzoylformate, chimera between pyruvate decarboxylase and benzoylformate decarboxylase. Preferred substrates are 2-ketopentanoic acid and 2-ketohexanoic acid. Improvement of enantioselectivity for (S)-acetoin
N482D
-
mutation has a significant influence on the carboligation reaction, the binding of the cofactors and the thermostability are not affected
W329M
-
the carboligase activity of the mutant is 2.8% as high as the decarboxylase activity which is about 10fold higher than the wild type enzyme
W392M
-
higher carboligase/(R)-phenylacetylcarbinol-producing activity, more stable and higher resistance towards acetaldehyde than wild-type PDC
additional information