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1 ns identified in an individual with inactive dihydrolipoamide dehydrogenase.
2 es in a yeast strain deficient in endogenous dihydrolipoamide dehydrogenase.
3 sposon insertion into the A. phagocytophilum dihydrolipoamide dehydrogenase 1 gene (lpda1 [APH_0065])
4 ons to phenazines through the common subunit dihydrolipoamide dehydrogenase, a flavoprotein encoded b
5 ion while a P453L change resulted in reduced dihydrolipoamide dehydrogenase abundance in the mitochon
6 ls lacking endogenous DLD even when residual dihydrolipoamide dehydrogenase activity was as low as 21
7 these mutations decreased to various degrees dihydrolipoamide dehydrogenase activity, whereas dimer i
8 roteins in subcellular organelles, including dihydrolipoamide dehydrogenase and catalase, and show th
9 ervation through evolution, it is unknown if dihydrolipoamide dehydrogenases are functionally equival
19 acid sequence of TGP2 has high similarity to dihydrolipoamide dehydrogenase (DLDH) from a variety of
20 describes the enzymatic characterization of dihydrolipoamide dehydrogenase (DLDH) from Streptococcus
21 the present study, we have characterized the dihydrolipoamide dehydrogenase (DLDH) of Strepto-coccus
22 coccus pneumoniae strains lacking the enzyme dihydrolipoamide dehydrogenase (DLDH) show markedly redu
24 ehydrogenase (E(1)) and about 6 molecules of dihydrolipoamide dehydrogenase (E(3)) with its binding p
25 ding sites for two other component proteins, dihydrolipoamide dehydrogenase (E3) and pyruvate dehydro
28 dihydrolipoamide acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3) subunits of the pyru
29 ng protein (E3BP), is required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoam
30 -keto acid decarboxylase/dehydrogenase (E1), dihydrolipoamide dehydrogenase (E3), BCKD kinase, and BC
31 1p), dihydrolipoyl transacetylase (E2p), and dihydrolipoamide dehydrogenase (E3), to carry out the ox
32 ranched-chain amino acids was diagnosed with dihydrolipoamide dehydrogenase (E3; dihydrolipoamide: NA
33 E426 is conserved throughout non-halophilic dihydrolipoamide dehydrogenases, E423 is only present in
36 our site-directed mutations of the Haloferax dihydrolipoamide dehydrogenase have been made (E423D, E4
41 arasites possess two distinct genes encoding dihydrolipoamide dehydrogenases (LipDH), which are indis
44 d, the mutation was in the lpd gene encoding dihydrolipoamide dehydrogenase (LPD), a component of PDH
49 tified the lipoamide succinyltransferase and dihydrolipoamide dehydrogenase subunits of the alpha-ket
50 enzymes that include glutathione reductase, dihydrolipoamide dehydrogenase, trypanothione reductase,
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