ライフサイエンスコーパス: ascorbate peroxidase

1 ral description of the binding properties of ascorbate peroxidase.

2 tion 42 can act as the acid-base catalyst in ascorbate peroxidase.

3 redoxins, m-type thioredoxins, and a lumenal ascorbate peroxidase.

4 e role of Arg172 in ascorbate utilization by ascorbate peroxidase.

5 ied as a putative peroxisomal membrane-bound ascorbate peroxidase.

6 ed signal compared with previously described ascorbate peroxidases.

7 and whether they could interact with tomato ascorbate peroxidases.

8 Cytosolic ascorbate peroxidase 1 (Apx1) is a key H(2)O(2) removal

9 Ascorbate peroxidase 1 (APX1) is identified as a BBX18-i

10 Cytosolic ascorbate peroxidase 1 (APX1) protein and mRNA accumulat

11 ion of genes, including heat shock proteins, ascorbate peroxidase 1 and 2, is similar in siz1 and wil

12 Arabidopsis mutants deficient in Ascorbate Peroxidase 1 showed attenuated hydrotropic roo

13 tagenesis, horseradish peroxidase (HRP), and ascorbate peroxidase 2 (APEX-2) proximity labelling, alo

14 Using a modified enhanced ascorbate peroxidase 2 (APEX2) approach with rapamycin-d

15 We recently reported enhanced ascorbate peroxidase 2 (APEX2) as a broadly applicable g

16 ract with P. falciparum KAHRP using enhanced ascorbate peroxidase 2 (APEX2) proximity-dependent bioti

17 We show that HSEs from the promoter of the ASCORBATE PEROXIDASE 2 (APX2) gene were necessary and su

18 ized proximity-dependent biotin labeling via ascorbate peroxidase 2 aired with mass spectrometry to i

19 nother GF14(lambda)-interacting protein, the ascorbate peroxidase 3 that scavenges H2O2 in plant cell

20 talase (35%), guaiacol peroxidase (65%), and ascorbate peroxidase (47%) and lower malondialdehyde (21

21 alpha(1C) or beta(2B) subunits conjugated to ascorbate peroxidase(5) in mouse hearts, and use multipl

22 1%), superoxide dismutase (81.8%, 73.5%) and ascorbate peroxidase (78.5%, 73.7%) thereby reducing Pb

23 However, neither glutathione peroxidase nor ascorbate peroxidase accounted for a significant part of

24 ed higher superoxide dismutase, catalase and ascorbate peroxidase activities as compared to control.

25 hat catalase activity increased in roots and ascorbate peroxidase activity decreased in leaves.

26 en days of Mn-toxicity stress increased leaf ascorbate peroxidase activity of cv ZPV-292 by 78% in lo

27 32 to Ser leads to approximately 70% drop in ascorbate peroxidase activity with no effect on guaiacol

28 ROS-sensitive transcripts and a decrease in ascorbate peroxidase activity.

29 xin, glutathione peroxidase-like enzymes and ascorbate peroxidase, all of which have cell compartment

30 ted antioxidant system that involves both an ascorbate peroxidase and a monodehydroascorbate reductas

31 r system allowed us to demonstrate that both ascorbate peroxidase and ascorbate oxidase affected the

32 similar to the EPR signals of compound I of ascorbate peroxidase and catalase from Micrococcus lysod

33 he location of the ascorbate binding site in ascorbate peroxidase and has identified hydrogen-bonding

34 te-dependent electron transfer system, using ascorbate peroxidase and monodehydroascorbate reductase

35 by higher activity of superoxide dismutase, ascorbate peroxidase and phenylalanine ammonia-lyase.

36 Increases of ascorbate peroxidase and superoxide dismutase activity o

37 the enzymes glutathione reductase, catalase, ascorbate peroxidase and superoxide dismutase together w

38 Incubation in ABA maintains high amounts of ascorbate peroxidase and superoxide dismutase, whereas G

39 ved in heat acclimation, including cytosolic ascorbate peroxidase and the transcription factors HsfA7

40 the location of the aromatic binding site in ascorbate peroxidase and, together with our previous dat

41 omplex formed between a redox metalloenzyme (ascorbate peroxidase) and its reducing substrate (ascorb

42 alanine ammonia-lyase, superoxide dismutase, ascorbate peroxidase, and catalase activity) had 94.64%

43 ntioxidants (superoxide dismutase, catalase, ascorbate peroxidase, and glutathione reductase) in both

44 activity of superoxide dismutase, catalase, ascorbate peroxidase, and glutathione reductase.

45 by reduced abundance of VIR3-target enzymes, ascorbate peroxidase, and glyceraldehyde 3-phophate dehy

46 SRA2 genes (encoding glutathione peroxidase, ascorbate peroxidase, and methionine sulfoxide reductase

47 cavenging enzymes, including catalase (CAT), ascorbate peroxidase, and superoxide dismutase are stron

48 Ascorbate peroxidase (AP) is a key enzyme that scavenges

49 al network by knocking in (KI) an engineered ascorbate peroxidase (APEX) gene to the endogenous locus

50 Proximity labeling with engineered ascorbate peroxidase (APEX) has been widely used to iden

51 Here, we applied engineered ascorbate peroxidase (APEX) to map the proteome at EMCs

52 In this study, we employed an engineered ascorbate peroxidase (APEX)-based proximity biotinylatio

53 By employing ascorbate peroxidase (APEX)-based proximity labeling and

54 Here, we used enhanced ascorbate peroxidase (APEX)-tagged PB2 proteins and elec

55 that features acid-base coil-caged enhanced ascorbate peroxidase (APEX).

56 live Drosophila tissues using an engineered ascorbate peroxidase (APEX).

57 Proximity labeling based on engineered ascorbate peroxidase APEX2 pioneered in situ capture of

58 labeling technique, APEX-seq, which uses the ascorbate peroxidase APEX2 to probe the spatial organiza

59 We applied engineered ascorbate peroxidase APEX2-based subcellular proteomics

60 We used the ascorbate peroxidase (APEX2) proximity labeling system,

61 Notably, the soybean ascorbate peroxidase, APEX2, rapidly biotinylates adjace

62 Measurement of antioxidant enzymes ascorbate peroxidase (APOX), glutathione reductase (GR),

63 ty, associated with lower catalase (CAT) and ascorbate peroxidase (APX) activities, leading to fruits

64 rs of the class I peroxidase family, notably ascorbate peroxidase (APX) and cytochrome c peroxidase (

65 Cytochrome c (CcP) and ascorbate peroxidase (APX) are heme peroxidases which ha

66 CuZn-superoxide dismutase (CuZn-SOD) and ascorbate peroxidase (APX) constitute first line of defe

67 the K+ site found in the proximal pocket of ascorbate peroxidase (APX) could be engineered into cyto

68 +) site found in the proximal heme pocket of ascorbate peroxidase (APX) could be successfully enginee

69 Cytochrome c peroxidase (CCP) and ascorbate peroxidase (APX) have very similar structures,

70 ectroscopic investigations of compound II in ascorbate peroxidase (APX) have yielded conflicting conc

71 Peroxisomal ascorbate peroxidase (APX) is a carboxyl tail-anchored,

72 The peroxisomal isoform of ascorbate peroxidase (APX) is a novel membrane isoform t

73 Ascorbate Peroxidase (APX) was reached at its peak (1.93

74 was isolated that encodes a 32-kD subunit of ascorbate peroxidase (APX) with a single, putative membr

75 The interaction of recombinant ascorbate peroxidase (APX) with its physiological substr

76 Previously we reported that overexpressed ascorbate peroxidase (APX), a peroxisomal membrane prote

77 e (GSH), such as superoxide dismutase (SOD), ascorbate peroxidase (APX), and glutathione reductase (G

78 antioxidant enzymes such as catalase (CAT), ascorbate peroxidase (APX), and guaiacol peroxidase (GPX

79 he activities of the enzymes catalase (CAT), ascorbate peroxidase (APX), and guaiacol peroxidase (GPX

80 ys of several enzymatic antioxidants such as ascorbate peroxidase (APX), catalase (CAT), superoxide d

81 ediates in cytochrome c peroxidase (CcP) and ascorbate peroxidase (APX), collected using the X-ray fr

82 Ascorbate peroxidase (APX), cytochrome c peroxidase (CcP

83 id and glutathione, as well as activities of ascorbate peroxidase (APX), glutathione reductase (GR),

84 ant enzymes viz. superoxide dismutase (SOD), ascorbate peroxidase (APX), guaiacol peroxidase (GPX) an

85 This study aimed to investigate the role of ascorbate peroxidase (APX), guaiacol peroxidase (GPX), p

86 (+)-binding site, analogous to that found in ascorbate peroxidase (APX), was engineered into cytochro

87 hrome c peroxidase (CCP) and plant cytosolic ascorbate peroxidase (APX).

88 used to probe the ascorbate binding site in ascorbate peroxidase (APX).

89 yl histidine (NMH) ligand into an engineered ascorbate peroxidase (APX2) overcomes the reliance on th

90 id expression of a gene encoding a cytosolic ascorbate peroxidase (APX2), whose expression is restric

91 al structures of cytochrome c peroxidase and ascorbate peroxidase are very similar, including the act

92 Ascorbate peroxidases are important defense enzymes that

93 l downstream genes, including those encoding ascorbate peroxidase (AtApx2) and heat shock proteins [A

94 tal histidine (His42) in the W41A variant of ascorbate peroxidase binds to the heme iron in the ferri

95 d approximately 8 A from the proximal Trp in ascorbate peroxidase but absent in cytochrome c peroxida

96 previously shown that the K(+) site found in ascorbate peroxidase can be successfully engineered into

97 Interestingly, cytosolic ascorbate peroxidase (cAPX), a key enzyme controlling H2

98 nd activities of antioxidative enzymes like (ascorbate peroxidase, catalase, and superoxide dismutase

99 sion of antioxidant genes encoding cytosolic ascorbate peroxidase, catalase, and superoxide dismutase

100 yanins, total phenolics, membrane integrity, ascorbate peroxidase, catalase, glutathione reductase an

101 d mutagenesis has been used to introduce the ascorbate peroxidase cation binding site into cytochrome

102 tate of the iron(IV) oxo (or ferryl) form of ascorbate peroxidase compound II (APX-II) is a subject o

103 We identified the plastid ascorbate peroxidase (cpAPX) genes across angiosperms an

104 emonstrate that the T. cruzi heme-containing ascorbate peroxidase cytochrome c peroxidase (APx-CcP),

105 se is a hybrid heme peroxidase, the T. cruzi ascorbate peroxidase-cytochrome c peroxidase enzyme (TcA

106 ol to 78.8 in 750 mg kg(-1) treatment; while ascorbate peroxidase decreased from 21.9 to 14.1 in 500

107 An ascorbate peroxidase derivative (APEX)-transmission elec

108 c peroxidase is thought to be one reason why ascorbate peroxidase does not form a Trp radical.

109 t (chlorophyll and carotenoid), catalase and ascorbate peroxidase enzymes, gene expression, and Cu bi

110 In contrast, early ascorbate peroxidase expression was induced only with Cd

111 compound responses, with a high induction of ascorbate peroxidase expression.

112 using well-annotated datasets, including the ascorbate peroxidase gene family of rice, maize and sorg

113 Two mitochondrial-localized rice ascorbate peroxidase genes fused to DsRed and successful

114 Critically, over-expression of stromal ascorbate peroxidase (H2O2 scavenger) or treatment with

115 APEX, an ascorbate peroxidase, has proven to be one of the most v

116 the H(2)O(2)-scavenging enzymes catalase and ascorbate peroxidase, (ii) a high affinity SA-binding pr

117 uggest that CKC_05770 interacted with tomato ascorbate peroxidases in two in vivo assays but not in v

118 dase, glucose-6-phosphate-dehydrogenase, and ascorbate peroxidase), iron metabolism (iron deficiency-

119 Ascorbate peroxidase is a bifunctional peroxidase that c

120 in a position analogous to the substrate in ascorbate peroxidase is essential for both decarboxylati

121 The Trypanosoma cruzi ascorbate peroxidase is, by sequence analysis, a hybrid

122 xide, malondialdehyde, peroxidase, catalase, ascorbate peroxidase levels, and Na(+) content and a neg

123 alized to mitochondria and chloroplasts) and ascorbate peroxidase (localized to chloroplasts) greatly

124 ts of the ascorbate-glutathione system (e.g. ascorbate peroxidase, manganese superoxide dismutase, an

125 fusing a monomeric heme-binding peroxidase (ascorbate peroxidase, mAPX) to a monomeric form of green

126 eta-1,3-glucanase, a thaumatin-like protein, ascorbate peroxidase, metallothionein, and a putative se

127 ymes-such as superoxide dismutase, catalase, ascorbate peroxidase, monodehydroascorbate reductase, de

128 Analysis of a thylakoidal ascorbate peroxidase mutant (tapx), the (1)O2-retrograde

129 mes like superoxide dismutase, catalase, and ascorbate peroxidase of the fruits over 12 days of stora

130 Cytosolic ascorbate peroxidase over-expression has little effect o

131 howed that WKS1 phosphorylates the thylakoid ascorbate peroxidase protein and reduces its ability to

132 A new study makes use of the ascorbate peroxidase proximity-labeling proteomics appro

133 e sulphide (7), by recombinant pea cytosolic ascorbate peroxidase (rAPX) and a site-directed variant

134 Ascorbate peroxidase represents such an example.

135 vities of catalase, guaiacol peroxidase, and ascorbate peroxidase, resulting in greater leaf cell bio

136 e 2-vinyl group in recombinant pea cytosolic ascorbate peroxidase (rpAPX) by replacement of Ser160 by

137 c mechanism of recombinant soybean cytosolic ascorbate peroxidase (rsAPX) and a derivative of rsAPX i

138 l structure of recombinant soybean cytosolic ascorbate peroxidase (rsAPX) in complex with salicylhydr

139 )O(2)) that includes a stromal and thylakoid ascorbate peroxidase (sAPX and tAPX).

140 (2-Cys) peroxiredoxins (PRXs) and thylakoid ascorbate peroxidase (tAPX), have been proposed to be in

141 However, in ascorbate peroxidase, the porphyrin is oxidized, not the

142 in the catalytic mechanism of pea cytosolic ascorbate peroxidase, two site-directed variants were pr

143 generated a double mutant lacking thylakoid ascorbate peroxidase (tylapx) and cytosolic ascorbate pe

144 ers of proton delivery in a heme peroxidase (ascorbate peroxidase) using computational approaches tha

145 e, we describe kinetic data for a variant of ascorbate peroxidase (W41A) which reacts slowly with ter

146 antioxidant enzymes catalase, peroxidase and ascorbate peroxidase was also increased at harvest by SA

147 ation-modified cysteine residue on cytosolic ascorbate peroxidase was demonstrated using liquid chrom

148 d enhancing the activities of peroxidase and ascorbate peroxidase, which was confirmed by combined co