ライフサイエンスコーパス: peroxidatic

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

27 5, but dissociated from MKP-1 when the Prdx1 peroxidatic cysteine Cys52 was over-oxidized to sulfonic

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

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

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

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

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

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

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

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

36 idative inactivation by overoxidation of the peroxidatic cysteine.

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

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

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

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

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

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

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

44 We propose that the peroxidatic substrates interact predominantly outside th

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