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1.2.1.104: pyruvate dehydrogenase system

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

Reaction

pyruvate
+
CoA
+
NAD+
=
acetyl-CoA
+
CO2
+
NADH

Synonyms

aceE, AceF, At1g54220, At3g13930, At3g52200, CTHT_0006350, CTHT_0069820, dihydrolipoamide acetyltransferase, dihydrolipoyllysine-residue acetyltransferase component, DLAT, DLD, DLST, E1 component of pyruvate dehydrogenase complex, E1 component subunit alpha, E1 component subunit beta, IAR4, LpdA, Lta3, MAB1, More, Mrp-3, Pda1, Pda1p, PDC, PDCp, PDH, PDH complex, PDH-E1 catalytic subunit, PDHa, PdhA1, PDHalpha, PdhB1, PDHC, PdhE, PDHE1alpha1, PdhH, PdhX, PH2, plastidial pyruvate dehydrogenase complex, pyruvate decarboxylase, pyruvate dehydrogenase, pyruvate dehydrogenase alpha subunit, pyruvate dehydrogenase complex, pyruvate dehydrogenase E1

ECTree

     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.1 With NAD+ or NADP+ as acceptor
                1.2.1.104 pyruvate dehydrogenase system

General Stability

General Stability on EC 1.2.1.104 - pyruvate dehydrogenase system

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is stable in high ionic strength buffers
enzyme is unstable in low ionic strength buffers and in the presence of organic solvents
PDC displays size versatility in an ionic strength-dependent manner. PDC (yPDC) is a salt-labile complex that dissociates into sub-megadalton individual components even under physiological ionic strength. Each oligomeric component of PDC displays a larger size than expected. The activity of PDC is reduced in higher ionic strength
very sensitive to freezing and thawing
very sensitive to proteolysis, especially during purification
-