ライフサイエンスコーパス: co-substrate

1 elaxation driven by the interaction with the Co substrate.

2 converting NO to nitrate ion with oxygen as co-substrate.

3 degrading enzyme that requires pyruvate as a co-substrate.

4 n(II) as a co-factor and 2-oxoglutarate as a co-substrate.

5 rase that utilizes S-adenosylmethionine as a co-substrate.

6 roM, respectively, in the presence of excess co-substrate.

7 he enzyme requires S-adenosylmethionine as a co-substrate.

8 between the available reducing and oxidizing co-substrates.

9 l-Ara4N, when NAD and glutamate are added as co-substrates.

10 the inclusion of appropriate nucleophiles as co-substrates.

11 lyst, and in a form that contained iron, the co-substrate 2-oxoglutarate, and the reaction product of

12 sable dependence on the concentration of its co-substrate alpha-ketoglutarate.

13 he binary complexes it forms with either the co-substrate (alpha-ketoglutarate) or the substrate (fum

14 as the activating metal, 2-oxoglutarate as a co-substrate, and ascorbic acid as a cofactor.

15 extensin as substrate and 60 microM H2O2 as co-substrate, at 23 degrees pl 4.6 extensin peroxidase g

16 ive yield when CobA is preincubated with the co-substrate ATP.

17 Low concentrations of the co-substrate beta-mercaptoethanol (Kd = approximately 13

18 we have determined the solvent effects of a co-substrate, beta-mercaptoethanol, and of a model nonsu

19 time-resolved measurements of intracellular (co-)substrate binding and release.

20 te kinetics indicate that TH has a different co-substrate binding sequence (pterin + O(2) + L-tyr) th

21 The A154T polymorphism is located within the co-substrate binding site.

22 ed similar binding modes for each in the 2OG co-substrate binding site.

23 , a shift from ordered to random addition in co-substrate binding, and a significantly reduced rate o

24 TlyA interdomain linker as indispensable for co-substrate binding.

25 f serotonin employing varying intracellular (co-)substrate concentrations and interpreted the data us

26 otope effects that increase in proportion to co-substrate concentrations before converging to limitin

27 es of inhibitors based on simple analysis of co-substrate dependency of protein stabilization.

28 s III histone deacylases that use NAD(+)as a co-substrate during amide bond hydrolysis.

29 hydroxylases alike decarboxylate the alphaKG co-substrate, facilitating formation of a high-energy fe

30 and it appeared to increase the strength of CO (substrate for acetyl-CoA synthesis) binding to the r

31 of Mtb TlyA interaction with its obligatory co-substrate for methyltransferase activity, S-adenosyl-

32 ecule in cellular metabolism and an obligate co-substrate for NAD(+)-consuming enzymes, which regulat

33 is not optimized for utilizing H(2)O(2) as a co-substrate for oxidizing L-Trp.

34 -, but not (S)-2-hydroxyglutarate, acts as a co-substrate for the hypoxia-inducible factor prolyl hyd

35 e presence or absence of the enzyme's native co-substrate glutathione (GSH).

36 lytically consumed NO in the presence of the co-substrate hydrogen peroxide (H(2)O(2)).

37 e (alternatively termed 2-oxoglutarate) as a co-substrate in so many oxidation reactions throughout m

38 c5B approximately (125)I-ubiquitin thioester co-substrate in the nanomolar range ([S](1/2) = 140 +/-

39 er is exposed to solvent, the 2-oxoglutarate co-substrate likely adopts an inactive conformation in t

40 ropeptide in the presence and absence of its co-substrates may represent a release mechanism for macr

41 monitored the translocation of substrate and co-substrate Na(+) across the lipid bilayer and the tran

42 ol binding site on SIRT2 contact the sirtuin co-substrate NAD(+) during enzymatic catalysis, and assa

43 eased the nuclear concentration of the SIRT1 co-substrate NAD(+), and decreased chromatin accessibili

44 bition that is dependent on the level of the co-substrate, O(2), and reductant as well as substrate d

45 ich convert Arg into NO and citrulline using co-substrates O2 and NADPH.

46 re makes use of reactive molecular oxygen as co-substrate of oxygenases to hydroxylate and cleave the

47 age in greater numbers than controls lacking co-substrate or when PIMT protein binding was poisoned w

48 easurement of oxygen consumption, peroxidase co-substrate oxidation or prostaglandin (PG) detection.

49 ing in the absence of alpha-ketoglutarate (a co-substrate required by many mononuclear iron enzymes),

50 bolic interdependence of microorganisms, and co-substrate requirements in the catabolism of xenobioti

51 remodelling factors, the Rea1 ATPase and its co-substrate Rsa4, are present on Nug2-associated partic

52 these variants, only D47N and L49A bound the co-substrate S-adenosyl-L-methionine.

53 Inclusion of the PIMT co-substrate, S-adenosylmethionine (AdoMet), during pann

54 ants leading to an uncoupled cleavage of the co-substrate SAM.

55 viding structural evidence for substrate and co-substrate specificity and the inability of PvdA to bi

56 ant amount (170-fold) only when dCTP was the co-substrate suggesting that a hydrogen bond exists only

57 The lipophilic nature of the co-substrate suggests that electron transfer to CoQ occu

58 Using acetyl-CoA as a co-substrate, the high affinity binding of acetyl-CoA is

59 We investigated the potential role of the co-substrate, thiocyanate (SCN-), in modulating the cata

60 es use an Fe(II) cofactor and 2-oxoglutarate co-substrate to oxidize organic substrates.

61 se domain in the presence and absence of the co-substrate UDP-glucose.

62 the traditional UDP-glycosyltransferase UGT co-substrate UDP-glucuronic acid.

63 Nucleophiles used successfully as co-substrates were thiosulphate, 2-mercaptoethanol, merc

64 mentation with 1,4-dihydroxy-2-naphthoate, a co-substrate with C35 -PP for MenA.