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1 are activated by strain such as lipoic acid/lipoamide.
2 doxin-like active site that is responsive to lipoamide.
3 enotrisulfide derivatives of lipoic acid and lipoamide.
4 were noncompetitive versus NADH, NAD(+), and lipoamide and >100-fold selective compared to human Lpd.
6 rare family of marine cyanobacterial-derived lipoamides and a new structural class of compounds exhib
7 intermediates on the E1p component, and the lipoamide-bound covalent intermediate on the E2p compone
8 mine that SIRT4 enzymatically hydrolyzes the lipoamide cofactors from the E2 component dihydrolipoyll
10 ihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) components of alpha-ketoglu
12 (P)H, flavin adenine dinucleotide (FAD), and lipoamide dehydrogenase (LipDH) over the wavelength rang
13 ssibility of species-selective inhibition of lipoamide dehydrogenase (Lpd), an enzyme central to Mtb'
15 zed Ohr by NADH was shown to be catalyzed by lipoamide dehydrogenase and either lipoamide or DlaT (Su
16 oredoxin reductase is like the mechanisms of lipoamide dehydrogenase and glutathione reductase and di
18 o other well-studied members of this family, lipoamide dehydrogenase and glutathione reductase, cycle
20 nd EH(4) forms of Mycobacterium tuberculosis lipoamide dehydrogenase and rapidly mixed these enzyme f
21 mide dehydrogenase that is distinct from the lipoamide dehydrogenase associated with the pyruvate deh
22 reduction of the Mycobacterium tuberculosis lipoamide dehydrogenase by NADH and [4S-(2)H]-NADH was s
26 We report the 2.4 A crystal structure for lipoamide dehydrogenase encoded by lpdC from Mycobacteri
28 to peas (Pisum sativum), where mitochondrial lipoamide dehydrogenase is encoded by a single gene and
32 pdA gene, which encodes the oxidative enzyme lipoamide dehydrogenase required for tricarboxylic acid
33 oded by bkdD indicate that E. faecalis has a lipoamide dehydrogenase that is distinct from the lipoam
34 targets major enzymes of energy production (lipoamide dehydrogenase) and antioxidant defense (thiore
37 e, in contrast to the closely related enzyme lipoamide dehydrogenase, for which only EH2 is active.
38 l members of the enzyme family that includes lipoamide dehydrogenase, glutathione reductase and mercu
39 c uptake regulatory repressor, and possibly, lipoamide dehydrogenase, the L protein component of the
42 d, including xanthine oxidase (XO)/xanthine, lipoamide dehydrogenase/ NADH, isolated mitochondria, mi
44 f NADH and thio-NAD(+) in the absence of D,L-lipoamide, demonstrated that the enzyme uses a ping-pong
47 ass spectral analysis of the lipoic acid and lipoamide derivatives confirmed both the expected molecu
50 ion and acetylation of the L1 domain or free lipoamide increased kinase activity, those modifications
51 /- 0.15, (D)V(app) = 1.05 +/- 0.07] when D,L-lipoamide is the oxidant but large and equivalent [(D)(V
53 ew vinylchlorine-containing metabolites, the lipoamides janthielamide A and kimbeamides A-C and the k
56 the lipoylated peptide, suggesting that the lipoamide moiety plays a marginal role within the autore
59 lting proteins for their ability to catalyze lipoamide reduction/oxidation alone and in complex with
62 alloxan, dehydroascorbate, DTNB, lipoic acid/lipoamide, S-nitrosoglutathione, selenodiglutathione, se
63 uorothioamidyl lysine adducts identified the lipoamide succinyltransferase and dihydrolipoamide dehyd
64 . aureus when growth is heavily reliant upon lipoamide-utilizing enzymes, but dispensable when this r
65 s and the R,S-(+/-) racemic mixture of LA or lipoamide, we identified the biologically active form of
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