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

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

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

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

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

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

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

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

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

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

24 p-Hydroxybenzoate hydroxylase (PHBH) hydroxylates activa

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

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

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

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

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

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

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

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

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

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

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

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

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

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

39 A novel p-hydroxybenzoate hydroxylase enzyme detected by proteom

40 Proline 293 of p-hydroxybenzoate hydroxylase from Pseudomonas aeruginos

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

42 p-Hydroxybenzoate hydroxylase is a flavoprotein monooxyg

43 p-Hydroxybenzoate hydroxylase is extensively studied as

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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