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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)

Storage Stability

Storage Stability on EC 1.2.4.1 - pyruvate dehydrogenase (acetyl-transferring)

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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, 50 mM potassium phosphate, pH 7.0, 0.5 mM EDTA, several months, no loss of activity
-
-20°C, 2 weeks, 10-20% loss of activity
-
-20°C, 50 mM phosphate buffer, pH 7.0, several months, no loss of activity
-
-20°C, N2-atmosphere, addition of sulfhydryl compounds, several weeks
-
-20°C, stable for several months
-50°C, 50 mM potassium phosphate buffer, pH 7.0, 1 mM MgCl2, 20 mM thiamine diphosphate, 0.1 mM EDTA, 0.4 mM DTT, 0.1 mM NAD+, several months
-
4°C, recombinant enzyme in saturated ammonium sulfate, pH 7.0, stabel for 6 months