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1.2.4.1: pyruvate dehydrogenase (acetyl-transferring)

This is an abbreviated version!
For detailed information about pyruvate dehydrogenase (acetyl-transferring), go to the full flat file.

Word Map on EC 1.2.4.1

Reaction

pyruvate
+
[dihydrolipoyllysine-residue acetyltransferase] lipoyllysine
=
[dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine
 +
CO2

Synonyms

aceE, AcoA, CTHT_0006350, CTHT_0069820, dehydrogenase, pyruvate, E1 component of pyruvate dehydrogenase, E1 component of pyruvate dehydrogenase multienzyme complex, E1 component of the pyruvate dehydrogenase multienzyme complex, E1 component subunit alpha, E1 component subunit beta, E1alpha, E1ec, E1p, IAR4, MAB1, MdeB, mitochondrial pyruvate dehydrogenase, More, MtPDC, OsI_14647, OsI_31986, Pda1, PDC, PDH, PDH E1alpha, PDH subunit E1-beta, PDH-A1, PDHa, PdhA1, PDHA1a, PdhB, PDHC, PDHc E1, PDHc-E1, PdhE, PDHE1alpha, PdhH, PH2, pyruvate decarboxylase, pyruvate dehydrogenase, pyruvate dehydrogenase complex, pyruvate dehydrogenase complex E1 component, pyruvate dehydrogenase complex,, pyruvate dehydrogenase E1, pyruvate dehydrogenase E1 alpha subunit, pyruvate dehydrogenase E1 component, pyruvate dehydrogenase E1 component subunit beta, pyruvate dehydrogenase multienzyme complex, pyruvate dehydrogenase multienzyme complex E1, pyruvate dehydrogenase, E1, pyruvate:NAD oxidoreductase, pyruvate:[dihydrolipoyllysine-residue acetyltransferase]-lipoyllysine 2-oxidoreductase (decarboxylating, acceptor-acetylating), pyruvic acid dehydrogenase, pyruvic dehydrogenase, thiamin diphosphate-dependent pyruvate dehydrogenase, thiamin-dependent pyruvate dehydrogenase, thiamine diphosphate-dependent 2-oxo acid decarboxylase, VEG220, Vegetative protein 220

ECTree

     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.4 With a disulfide as acceptor
                1.2.4.1 pyruvate dehydrogenase (acetyl-transferring)

Engineering

Engineering on EC 1.2.4.1 - pyruvate dehydrogenase (acetyl-transferring)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D15A
-
site-directed mutagenesis, 0.19% remaining activity with NAD+ and 16% reduced E1 activity with 2,6-dichlorophenolindophenol as electron acceptor compared to the wild-type E1
D549A
-
in the mutant, binding and reductive acetylation of E2p lipoyl domains are highly impaired
D7A
-
site-directed mutagenesis, 0.14% remaining activity with NAD+ and 63% reduced E1 activity with 2,6-dichlorophenolindophenol as electron acceptor compared to the wild-type E1
D9A
-
site-directed mutagenesis, inactive with NAD+, 80% reduced E1 activity with 2,6-dichlorophenolindophenol as electron acceptor compared to the wild-type E1
E12D
-
site-directed mutagenesis, 2.3% remaining activity with NAD+ and 90% reduced E1 activity with 2,6-dichlorophenolindophenol as electron acceptor compared to the wild-type E1
E12Q
-
site-directed mutagenesis, 3.3% remaining activity with NAD+ and 59% reduced E1 activity with 2,6-dichlorophenolindophenol as electron acceptor compared to the wild-type E1
E401A
9.56% of overall wild type activity and 23.4% of wild type activity with 2,6-dichloroindolphenol
E401K
E410K
-
CC-bond formation is dramatically slowed down (10-fold compared with E1ec) in E401K, the loop dynamics apparently greatly influences covalent addition of substrate to the enzyme-bound thiamine diphosphate
H407A
I11A
-
site-directed mutagenesis, 94% remaining activity with NAD+ and E1 activity with 2,6-dichlorophenolindophenol as electron acceptor is like the wild-type E1 activity
K403A
11.6% of overall wild type activity and 98.0% of wild type activity with 2,6-dichloroindolphenol
K403E
0.56% of overall wild type activity and 5.46% of wild type activity with 2,6-dichloroindolphenol
K410A
23.0% of overall wild type activity and 31.6% of wild type activity with 2,6-dichloroindolphenol
K410E
3.7% of overall wild type activity and 26.1% of wild type activity with 2,6-dichloroindolphenol
K411A
68.2% of overall wild type activity and 77.5% of wild type activity with 2,6-dichloroindolphenol
K411E
38.0% of overall wild type activity and 88.0% of wild type activity with 2,6-dichloroindolphenol
N404A
1.81% of overall wild type activity and 45.1% of wild type activity with 2,6-dichloroindolphenol
P10A
-
site-directed mutagenesis, unaltered activity with NAD+ and 50% reduced E1 activity with 2,6-dichlorophenolindophenol as electron acceptor compared to the wild-type E1
Q408A
31.5% of overall wild type activity and 112.1% of wild type activity with 2,6-dichloroindolphenol
R14A
-
site-directed mutagenesis, 0.25% remaining activity with NAD+ as electron acceptor, E1 activity with 2,6-dichlorophenolindophenol is like the wild-type E1 activity
T13A
-
site-directed mutagenesis, 13% remaining activity with NAD+ and 26% reduced E1 activity with 2,6-dichlorophenolindophenol as electron acceptor compared to the wild-type E1
Y177A
Y177F
-
7% of wild-type activity in enzyme complex
D203A
enzymatic activity similar to wild-type, mutant retains the normal capacity to bind the peripheral subunit-binding domain
D276A
-
site-directed mutagenesis, reduced activity with pyruvate compared to the wild-type enzyme
E251A
enzymatic activity similar to wild-type, mutant retains the normal capacity to bind the peripheral subunit-binding domain
E285A
enzymatic activity similar to wild-type, mutant retains the normal capacity to bind the peripheral subunit-binding domain. Mutant subunit dissociates from the wild-type peripheral subunit-binding domain about 9fold faster than wild-type
F266A
-
site-directed mutagenesis, reduced activity with pyruvate compared to the wild-type enzyme
F324A
enzymatic activity similar to wild-type, mutant retains the normal capacity to bind the peripheral subunit-binding domain. Mutant subunit dissociates from the wild-type peripheral subunit-binding domain about 13fold faster than wild-type
H128A
-
mutation in subunit E1beta, residue His128 provides the proton required to protonate the incoming dithiolane ring in the reductive acetylation of the lipoyl goup
H271A
-
mutation in subunit E1alpha, residue His271 stabilizes the dianion formed during decarboxylation of the 2-oxo acid
K252A
enzymatic activity similar to wild-type, mutant retains the normal capacity to bind the peripheral subunit-binding domain
M322A
enzymatic activity similar to wild-type, mutant retains the normal capacity to bind the peripheral subunit-binding domain
N323A
enzymatic activity similar to wild-type, mutant retains the normal capacity to bind the peripheral subunit-binding domain
R255A
enzymatic activity similar to wild-type, mutant retains the normal capacity to bind the peripheral subunit-binding domain
R267A
-
site-directed mutagenesis, highly reduced activity with pyruvate compared to the wild-type enzyme
R282A
-
site-directed mutagenesis, reduced activity with pyruvate compared to the wild-type enzyme
S283C
-
site-directed mutagenesis, reduced activity with pyruvate compared to the wild-type enzyme
Y281A
-
site-directed mutagenesis, reduced activity with pyruvate compared to the wild-type enzyme
Y281A/R282A
-
site-directed mutagenesis, highly reduced activity with pyruvate compared to the wild-type enzyme
Y281A/R282A/S283A
-
site-directed mutagenesis, highly reduced activity with pyruvate compared to the wild-type enzyme
Y281S/R282S
-
site-directed mutagenesis, highly reduced activity with pyruvate compared to the wild-type enzyme
D289A
-
the beta subunit mutant does not have any detectable activity in assays with NAD+ and shows no change in activity in 2,6-dichlorophenolindophenol assays
D289N
-
the beta subunit mutant shows by 36% reduced activity in assays with NAD+
E229A
-
the beta subunit mutant does not show drastic changes compared to the wild type E1 activities
E229Q
-
the beta subunit mutant does not show drastic changes compared to the wild type E1 activities
E232A
-
the beta subunit mutant does not show drastic changes compared to the wild type E1 activities
E232Q
-
the beta subunit mutant does not show drastic changes compared to the wild type E1 activities
E234A
-
the beta subunit mutant does not show drastic changes compared to the wild type E1 activities
E234Q
-
the beta subunit mutant does not show drastic changes compared to the wild type E1 activities
I329A
-
shows 37-43% reduction in activity compared to the wild type enzyme
R253G
-
the mutation is associated with low PDHc activity and absence of subunit alpha of pyruvate dehydrogenase E1
S264E
pseudophosphorylation mutant, the preceding binding of substrate to the enzyme's active site via the substrate channel and the subsequent reductive acetylation of the E2 component are severely slowed in the mutant enzyme
S264Q
selectively deficient in pyruvate binding and reductive acetylation of component E2
additional information