ライフサイエンスコーパス: peroxidatic

1 ion of an intersubunit disulfide bond in the peroxidatic active site of the system's other component,

2 ons serve to stabilize a loop that forms the peroxidatic active site.

3 rvival and raise questions about whether the peroxidatic activity as well as the protective catalatic

4 the cytosol in stationary phase or that the peroxidatic activity of KatA is critical for stationary-

5 Catalatic-peroxidatic activity with different peroxidatic cosubstr

6 nia, contains two enzymes with catalatic and peroxidatic activity, KatA and KatB.

7 e AhpC, while C46S and C46,165S displayed no peroxidatic activity.

8 ich form intersubunit disulfide bonds in the peroxidatic AhpC protein of the alkyl hydroperoxide redu

9 ith GSH yields glutathionylation at both the peroxidatic (C(P)) and resolving cysteines (C(R)), the f

10 They are canonically characterized by a peroxidatic (called L, for "low reduction potential") ac

11 Our results clearly identify Cys46 as the peroxidatic center of AhpC and Cys165 as an important re

12 S, confirming the identity of Cys(61) as the peroxidatic center.

13 Under standard peroxidatic conditions (HRP, H(2)O(2), air), HRP oxidize

14 Under standard peroxidatic conditions (HRP/H(2)O(2)/air), the major pro

15 Finally, under peroxidatic conditions, 1a (R = cyclopropyl) inactivates

16 atalatic-peroxidatic activity with different peroxidatic cosubstrates is comparable for KatA and KatB

17 nd III to form compound II will maintain the peroxidatic cycle of the enzyme.

18 izes the sulfenic acid derivative of the Prx peroxidatic Cys (C(P)SOH) to the sulfinate (C(P)SO(2) (-

19 catalytically active cysteine residues, the peroxidatic Cys (CP) and, if present, the resolving Cys

20 In the active site the peroxidatic Cys is over-oxidized to cysteine sulfonic ac

21 is located five residues downstream from the peroxidatic Cys, and these residues form a disulfide dur

22 Mutational studies revealed that the peroxidatic (Cys60) and resolving (Cys93) cysteine resid

23 , the catalytic cysteine, referred to as the peroxidatic cysteine (C(P)), acts as a nucleophile in at

24 We determined a pK(a) of ~5.8 for the peroxidatic cysteine (Cys45) using both spectroscopic an

25 likely responsible for the protection of the peroxidatic cysteine against oxidative inactivation.

26 This molecular switch contains the peroxidatic cysteine and acts to buttress the oligomeriz

27 talysis requires two conserved residues, the peroxidatic cysteine and the resolving cysteine, which a

28 rx-S-SG reductase activity relies not on the peroxidatic cysteine but rather on the resolving cystein

29 5, but dissociated from MKP-1 when the Prdx1 peroxidatic cysteine Cys52 was over-oxidized to sulfonic

30 t manner through the oxidation status of its peroxidatic cysteine Cys52.

31 Mrx1 and the sulfenic acid derivative of the peroxidatic cysteine of MtAhpE.

32 and extended the alpha-helix with the former peroxidatic cysteine residue C61 by six residues.

33 ily of enzymes that reduce peroxides using a peroxidatic cysteine residue; among these, members of th

34 ive-site microenvironment activates both the peroxidatic cysteine side chain and the peroxide substra

35 One of these, overoxidation of the peroxidatic cysteine to the sulfinic derivative, inactiv

36 ciates with the enzyme; then it oxidizes the peroxidatic cysteine, and finally, the rate-limiting dis

37 ide in bacteria and acts through a reactive, peroxidatic cysteine, Cys46, and a second cysteine, Cys1

38 d consequent inactivation of the active-site peroxidatic cysteine.

39 idative inactivation by overoxidation of the peroxidatic cysteine.

40 hat exhibits no preferential reactivity with peroxidatic cysteines, but MtAhpE-SSH was less reactive

41 versible manner through sulfenylation of the peroxidatic cysteines, C201 and C208.

42 activities should be mutually antagonistic, peroxidatic electron donors (PxEDs) enhance KatG catalas

43 alternative cyt c conformers, known to gain peroxidatic function, may represent redox messengers at

44 ional changes allowing for the low-potential peroxidatic heme (Fe(L)) to adopt a high-spin, five-coor

45 n unusually stable Fe(IV)=O porphyrin at the peroxidatic heme.

46 d of a methionine residue and to enhance the peroxidatic properties of the protein considered importa

47 vement of free Cl2 in the chloride-dependent peroxidatic reactions catalyzed by chloroperoxidase (CPO

48 id (ba) are compared with previously studied peroxidatic substrates catechol (cat) and 2, 4,6-trimeth

49 We propose that the peroxidatic substrates interact predominantly outside th