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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)

Molecular Weight

Molecular Weight on EC 1.2.4.1 - pyruvate dehydrogenase (acetyl-transferring)

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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
2 * 100000, SDS-PAGE
136000
-
gel filtration
150000
-
calculation from sedimentation and diffusion data, low speed sedimentation equilibrium centrifugation, meniscus depletion method
154000
-
-
160000
-
recombinant alpha2,beta2 tetramer
169000
-
whole pyruvate dehydrogenase enzyme complex, gel filtration
182000 - 183000
-
calculation from sedimentation and diffusion data
185000
gel filtration
200000
-
SDS-PAGE
240000
-
gel filtration, recombinant protein from Escherichia coli and from Haloferax volcanii
36000
40315
-
x * 40315, pyruvate dehydrogenase multienzyme complex component E1alpha, sequence calculation
41000
-
alpha2,beta2, 2 * 41000 + 2 * 36000
42000
-
alpha2,beta2, 2 * 42000 + 2 * 36000, SDS-PAGE, calculated from gene sequence
43000
-
SDS-PAGE
60000
-
4 * 60000, SDS-PAGE
93000
2 * 93000, SDS-PAGE, 2 * 98082, calculated
98082
2 * 93000, SDS-PAGE, 2 * 98082, calculated
99470
pyruvate dehydrogenase multienzyme complex component E1
99474
additional information
-
MW of native complex isolated from kidney and heart: 7000000 Da and 8500000 Da respectively