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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)

Application

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

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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
mutation of promoter binding protein SPL16/GW8 leads to upregulation of pyruvate kinase, pyruvate dehydrogenase E1, dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex, acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial pyruvate carrier, 4-hydroxyphenylpyruvate dioxygenase, and dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex. SPL16 mutations have the potential to boost the grain yield of rice
biotechnology
-
active expression of enzyme from non-halophilic Zymomonas mobilis in the haloarchaeon Haloferax volcanii with no difference in the secondary structure. Post-transcriptional mechanisms in the stationary phase appear to limit the amount of recombinant protein expressed
medicine
synthesis