ライフサイエンスコーパス: p-hydroxybenzoate

1 form a hydroperoxide, which then oxygenates p-hydroxybenzoate.

2 form a hydroperoxide, which then oxygenates p-hydroxybenzoate.

3 form a hydroperoxide, which then oxygenates p-hydroxybenzoate.

4 diate form in the presence of high levels of p-hydroxybenzoate.

5 he negative charge of the phenolic oxygen of p-hydroxybenzoate.

6 effective catalyst for the hydroxylation of p-hydroxybenzoate.

7 nse of the naturally incorporated monolignol p-hydroxybenzoates.

8 PobR responds to the inducer-metabolite p-hydroxybenzoate and activates transcription of pobA, t

9 a transcriptional activator that responds to p-hydroxybenzoate and activates transcription of pobA.

10 ed that catabolism of the phenolic compounds p-hydroxybenzoate and protocatechuate via the beta-ketoa

11 nK and PcaK have overlapping specificity for p-hydroxybenzoate and, most clearly, for protocatechuate

12 rs the pK(a) of the phenolic oxygen of bound p-hydroxybenzoate, and eliminates the pH dependence of t

13 Details of the substrate, p-hydroxybenzoate, and substrate analog, p-aminobenzoate

14 paraben, BPF, PFOSAA, benzophenone-3, benzyl p-hydroxybenzoate, and triphenyl phosphate-by running a

15 d was reduced at a rate similar to that with p-hydroxybenzoate bound at high pH.

16 rmal conformation of the reduced enzyme with p-hydroxybenzoate bound.

17 also forms an open conformation for binding p-hydroxybenzoate, but only transiently.

18 First, the rate of hydroxylation of p-hydroxybenzoate by the transiently formed flavin hydro

19 techol branch, was consumed in preference to p-hydroxybenzoate, degraded via the protocatechuate bran

20 The mutant PobR depended on p-hydroxybenzoate for its activity, but this dependence

21 Until recently, it has not been clear how p-hydroxybenzoate gains access to the buried active site

22 -acylated; poplar lignins, for example, have p-hydroxybenzoate groups on 1-15% of their syringyl subu

23 transgenic wood released fewer ester-linked p-hydroxybenzoate groups than control trees, and reveale

24 -hydroxy-decanoic acid (10-HDAA), and methyl p-hydroxybenzoate (HOB) found at similar levels.

25 The flavin of p-hydroxybenzoate hydroxylase (PHBH) adopts two conforma

26 of several complexes involving FAD bound to p-hydroxybenzoate hydroxylase (PHBH) have revealed that

27 p-Hydroxybenzoate hydroxylase (PHBH) hydroxylates activa

28 p-Hydroxybenzoate hydroxylase (PHBH) is a homodimeric en

29 p-Hydroxybenzoate hydroxylase (PHBH) is a homodimeric fl

30 p-Hydroxybenzoate hydroxylase (PHBH) is an FAD-dependent

31 The FAD of p-hydroxybenzoate hydroxylase (PHBH) is known to exist i

32 ructure can be assigned to the well-studied, p-hydroxybenzoate hydroxylase (PHBH) SCOP superfamily of

33 rall architecture is most similar to that of p-hydroxybenzoate hydroxylase (PHBH), although there are

34 es have revealed two flavin conformations in p-hydroxybenzoate hydroxylase (PHBH), the in-position an

35 bles that of the NADPH-dependent flavoenzyme p-hydroxybenzoate hydroxylase (PHBH).

36 to clarify the mechanism of hydroxylation by p-hydroxybenzoate hydroxylase (PHBH).

37 ve demonstrated two flavin conformations for p-hydroxybenzoate hydroxylase (PHBH).

38 essential steps in the reaction catalyzed by p-hydroxybenzoate hydroxylase (PHBH).

39 y step in the paradigm aromatic hydroxylase, p-hydroxybenzoate hydroxylase (PHBH): the oxidation of p

40 Biochemical comparison of PvdA to p-hydroxybenzoate hydroxylase (PHBH, from Pseudomonas fl

41 overall fold of 3HB6H is similar to that of p-hydroxybenzoate hydroxylase and other flavoprotein aro

42 A novel p-hydroxybenzoate hydroxylase enzyme detected by proteom

43 Proline 293 of p-hydroxybenzoate hydroxylase from Pseudomonas aeruginos

44 ubstrate analog, p-aminobenzoate, binding to p-hydroxybenzoate hydroxylase have been elicited by Rama

45 p-Hydroxybenzoate hydroxylase is a flavoprotein monooxyg

46 p-Hydroxybenzoate hydroxylase is extensively studied as

47 g that the control of the flavin position in p-hydroxybenzoate hydroxylase represents a compromise be

48 Apo-p-hydroxybenzoate hydroxylase was reconstituted using 2'

49 some flavin-dependent hydroxylases (notably, p-hydroxybenzoate hydroxylase), binding of the hydroxyla

50 le of catalysis in RebC may resemble that of p-hydroxybenzoate hydroxylase, with substrate binding pr

51 ly of aromatic hydroxylases characterized by p-hydroxybenzoate hydroxylase.

52 s,cis-muconate, inhibited the utilization of p-hydroxybenzoate in the presence of benzoate.

53 d network abstracts the phenolic proton from p-hydroxybenzoate in the transition state of oxygen tran

54 me because (unlike wild-type) the binding of p-hydroxybenzoate is a rate-limiting process.

55 nt indicates that the deprotonation of bound p-hydroxybenzoate is also required for flavin movement,

56 ogenolysis, it is generally assumed that the p-hydroxybenzoate is cleaved before the deacylated ligni

57 f ML conjugates: ML-acetate, ML-benzoate, ML-p-hydroxybenzoate, ML-vanillate, ML-p-coumarate, and ML-

58 The p-hydroxybenzoate moiety itself also undergoes carboxyla

59 This compound, differing from p-hydroxybenzoate only in that it contains an additional

60 ses of wild-type and mutant PHBH, with bound p-hydroxybenzoate or p-aminobenzoate, reveal a chain of

61 ory genes blocking degradation of vanillate, p-hydroxybenzoate, or protocatechuate were selected.

62 enzoate hydroxylase (PHBH): the oxidation of p-hydroxybenzoate (p-OHB).

63 tral changes caused by the binding of either p-hydroxybenzoate (pOHB) or 2,4-dihydroxybenzoate (2,4-d

64 xygenase that catalyzes the hydroxylation of p-hydroxybenzoate (pOHB) to 3,4-dihydroxybenzoate in an

65 t be in the in-position for hydroxylation of p-hydroxybenzoate (pOHB), whereas the out-position is es

66 protonation state of the aromatic substrate p-hydroxybenzoate (pOHB), which when ionized to the phen

67 COQ2 (p-hydroxybenzoate polyprenyl transferase) encodes the en

68 bound to wt PHBH and wt PHBH plus substrate, p-hydroxybenzoate, provided examples of the "in" conform

69 ing sets of enzymes that convert quinate and p-hydroxybenzoate, respectively, to protocatechuate.

70 palladium-assisted reactions on the cinnamyl p-hydroxybenzoates resulting in initial beta-ether cleav

71 to measure the pKa of the -OH group in bound p-hydroxybenzoate, the substrate was labeled with 18O in

72 However, in the presence of the substrate p-hydroxybenzoate there is clear evidence from the Raman

73 hat are triggered by deprotonation of buried p-hydroxybenzoate through a H-bond network that leads to

74 xygenase that catalyzes the hydroxylation of p-hydroxybenzoate to form 3,4-dihydroxybenzoate.

75 form a hydroperoxide, which then reacts with p-hydroxybenzoate to form an oxygenated product.

76 nformation is the mechanism for sequestering p-hydroxybenzoate to initiate catalysis.

77 structural gene for the enzyme that converts p-hydroxybenzoate to protocatechuate.

78 he enzyme by NADPH in response to binding of p-hydroxybenzoate to the enzyme and (2) oxidation of red

79 ide phosphate (NADPH) in response to binding p-hydroxybenzoate to the enzyme and oxidation of reduced

80 cofactor FAD by NADPH in response to binding p-hydroxybenzoate to the enzyme and reaction of reduced

81 factor, FAD, by NADPH in response to binding p-hydroxybenzoate to the enzyme, and oxidation of reduce

82 Deprotonation of p-hydroxybenzoate to the phenolate and reprotonation of

83 For p-hydroxybenzoate, upon complexation, the -COO- symmetri

84 g close to the pca-qui-pob gene cluster (for p-hydroxybenzoate utilization) and distant from the func

85 These mutant enzymes bind p-hydroxybenzoate very fast, but with very low affinity,