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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.
5                                   Since free lipoamide and lipoic acid levels were shown to be undete
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
9 a lower K(I) for NADH, and a higher K(I) for lipoamide compared with the other two enzymes.
10 ihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) components of alpha-ketoglu
11 rotein microscopy as a simultaneous assay of lipoamide dehydrogenase (LipDH) autofluorescence.
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'
14                                              Lipoamide dehydrogenase also catalyzes NADH oxidation by
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
17             The mechanisms and structures of lipoamide dehydrogenase and glutathione reductase are al
18 o other well-studied members of this family, lipoamide dehydrogenase and glutathione reductase, cycle
19       For each of two target enzymes tested, lipoamide dehydrogenase and mycobacterial proteasome ATP
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
23                                              Lipoamide dehydrogenase can also catalyze the NADH-depen
24                                              Lipoamide dehydrogenase catalyses the NAD(+)-dependent o
25                                              Lipoamide dehydrogenase catalyzes the reversible NAD(+)-
26    We report the 2.4 A crystal structure for lipoamide dehydrogenase encoded by lpdC from Mycobacteri
27             Although annotated as a probable lipoamide dehydrogenase in M. tuberculosis, LpdA cannot
28 to peas (Pisum sativum), where mitochondrial lipoamide dehydrogenase is encoded by a single gene and
29 wed by reduction of the flavin, just as with lipoamide dehydrogenase or glutathione reductase.
30 te similar to that observed in titrations of lipoamide dehydrogenase or glutathione reductase.
31                                          The lipoamide dehydrogenase reaction catalyzed by the purifi
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
35                                              Lipoamide dehydrogenase, a component of the alpha-ketogl
36                       Thioredoxin reductase, lipoamide dehydrogenase, and glutathione reductase are m
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
40  never been observed before in any wild-type lipoamide dehydrogenase.
41 efficiently reduced by NADH-dependent bovine lipoamide dehydrogenase.
42 d, including xanthine oxidase (XO)/xanthine, lipoamide dehydrogenase/ NADH, isolated mitochondria, mi
43 has two genes encoding for two mitochondrial lipoamide dehydrogenases.
44 f NADH and thio-NAD(+) in the absence of D,L-lipoamide, demonstrated that the enzyme uses a ping-pong
45  aureus cells experiencing a high demand for lipoamide-dependent enzymes.
46                                Likewise, the lipoamide derivative was efficiently reduced by NADH-dep
47 ass spectral analysis of the lipoic acid and lipoamide derivatives confirmed both the expected molecu
48 ions of enzyme redox states as a function of lipoamide/dihydrolipoamide, NAD(+)/NADH, and pH.
49  revealed that Zn(2+) competes with oxidized lipoamide for the two-electron-reduced enzyme.
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
52 ative half-reactions, respectively, when D,L-lipoamide is the oxidant.
53 ew vinylchlorine-containing metabolites, the lipoamides janthielamide A and kimbeamides A-C and the k
54 d by the recombinant enzyme as assessed by a lipoamide-lipoamide dehydrogenase-coupled assay.
55 hanges in reduction and acetylation state of lipoamide moieties set by the NAD(+)/NADH ratio.
56  the lipoylated peptide, suggesting that the lipoamide moiety plays a marginal role within the autore
57 a proton donor in the reductive acylation of lipoamide on the lipoyl-bearing domain.
58 alyzed by lipoamide dehydrogenase and either lipoamide or DlaT (SucB).
59 lting proteins for their ability to catalyze lipoamide reduction/oxidation alone and in complex with
60                                        These lipoamides represent the newest additions to a relativel
61 ed LA production and decreased activities of lipoamide-requiring enzymes.
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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