ライフサイエンスコーパス: cosubstrate

1 that LPMOs can use H2O2, instead of O2, as a cosubstrate.

2 Both enzymes require dioxygen as a cosubstrate.

3 me by addition of the substrate prior to the cosubstrate.

4 resence of recombinant G9a enzyme and AdoMet cosubstrate.

5 erized to date require molecular oxygen as a cosubstrate.

6 cleaver identified, is used as the reducing cosubstrate.

7 or Ca(2+) in its second role as a nucleotide cosubstrate.

8 DP donor to the beta-OHTyr-6 of the aglycone cosubstrate.

9 ar substrates with TcdB yet uses a different cosubstrate.

10 oxidoreductase (EmoB) to provide FMNH2 as a cosubstrate.

11 te substitute poorly for 2-oxoglutarate as a cosubstrate.

12 rved rate-limiting step involving release of cosubstrate.

13 accommodates the adenosyl moiety of the NAD+ cosubstrate.

14 vated by a human enzyme in the presence of a cosubstrate.

15 dependent on the concentration of the oxygen cosubstrate.

16 ltetrahydropterin, respectively, was used as cosubstrate.

17 ge that reduces ALKBH7's ability to bind its cosubstrate.

18 duces dehydroalanine to D-Ala using NAPDH as cosubstrate.

19 erminal alkenes using hydrogen peroxide as a cosubstrate.

20 y a Pictet-Spengler reaction with a carbonyl cosubstrate.

21 otinamide adenine dinucleotide (NAD(+)) as a cosubstrate.

22 ced holomycin to holomycin utilizing O(2) as cosubstrate.

23 O chitin-binding protein CBP21 using H2O2 as cosubstrate.

24 o depend upon the concentration of the other cosubstrate.

25 using 2-propanol (30%, v/v) as cosolvent and cosubstrate.

26 ncentrations of S-alkylglutathiones serve as cosubstrates.

27 ch as l-cysteine and beta-mercaptoethanol as cosubstrates.

28 g) and then at P(gamma) (ADP-forming) of ATP cosubstrates.

29 avin reductase), chloride ion, and oxygen as cosubstrates.

30 ared to Km(1a) 3.4 +/- 0.4 mM when 2a is the cosubstrate].

31 finity for the substrate GSH but not for the cosubstrate 1-chloro-2,4-dinitrobenzene (CDNB).

32 rand jellyroll core with both Fe(II) and the cosubstrate 2-oxoglutarate bound in the active site.

33 t requires the dioxygenase cofactor iron and cosubstrate 2-oxoglutarate.

34 rather than utilizing the typical keto-acid cosubstrates, 2-oxoglutarate, pyruvate, and oxaloacetate

35 efficient versus the original dipolarophile cosubstrate (2m and 2a, respectively), reveals that whil

36 ture of Teg12, Teg12 bound to the desulfated cosubstrate 3'-phosphoadenosine 5'-phosphate, and Teg12

37 18-kDa PCP fragment and by radioassay using cosubstrate [3H] pantetheinyl-coenzyme A for all PCP-con

38 In addition to substrate and cosubstrate, ACCO requires the activator CO(2) for conti

39 tyltransferase catalytic domain bound to its cosubstrate acetyl-CoA at 1.05 A resolution.

40 Excitingly, the ternary complex of HygX with cosubstrate alpha-ketoglutarate and putative product hyg

41 e results, in Fe(II)-reconstituted TfdA, the cosubstrate alpha-KG chelates to the metal via a C-1 car

42 coupled to the oxidative decarboxylation of cosubstrate, alpha-ketoglutarate (alpha-KG).

43 e conducted on TauD samples treated with NO, cosubstrate alphaKG, and either protonated or specifical

44 heir substrates and decarboxylation of their cosubstrate, alphaKG, to CO(2) and succinate.

45 11.6 muM for dimethylallyl diphosphate as a cosubstrate and 24.3 muM for GDP.

46 complex with the 10-formyl-5,8-dideazafolate cosubstrate and a glycinamide ribonucleotide analogue, h

47 The role of natural DOM as potential cosubstrate and detoxification reactant may improve futu

48 An absolute requirement for dioxygen as a cosubstrate and iron as cofactor suggests that HIF-PH fu

49 otinic acid adenine dinucleotide (NAAD) as a cosubstrate and is inhibited by nicotinic acid.

50 irrespective of which aminoglycoside is the cosubstrate and occurs without a significant change in t

51 s as well as compounds that bind across both cosubstrate and primary substrate binding sites.

52 ration of the Fe(II) in the presence of both cosubstrate and substrate appears to be critical for the

53 The enzyme requires molecular oxygen as a cosubstrate and utilizes a noncovalently bound flavin co

54 Kinetic parameters of peptide and NAD(+) cosubstrates and IC(50) values of standard reference inh

55 vity in the presence of a small DNA oligomer cosubstrate, and chi-cutting activity.

56 P4H uses alpha-ketoglutarate and O2 as cosubstrates, and forms succinate and CO2 as well as Hyp

57 They use only NADPH and oxygen as cosubstrates, and produce only NADP(+) and water as bypr

58 ant forms the five-coordinate site when both cosubstrates are bound, the Fe(II) site of the Glu280Lys

59 lii lethal toxin (TcsL), which uses the same cosubstrate as TcdB but shares Rac only as a common subs

60 PvdA uses the same cosubstrates as several flavin-dependent hydroxylases th

61 te site only when both the substrate ACC and cosubstrate ascorbate are bound to the enzyme.

62 ous enzyme that couples the oxidation of the cosubstrate ascorbate to the oxidation of substrate ACC

63 12) by transferring the adenosyl group from cosubstrate ATP to a transient Co (1+)corrinoid species

64 In the presence of cosubstrate ATP, ACATs raise the Co(II)/Co(I) reduction

65 presence of cobalt and vice versa, with the cosubstrates being transported in a 1:1 ratio.

66 tural differences that reflect substrate and cosubstrate binding effects and implies roles for the in

67 ancer-associated mutation affects productive cosubstrate binding in ALKBH7.

68 antly decreases V(max) with little effect on cosubstrate binding in G117C, G117S, and G117N mutants.

69 mutant exhibited little difference in either cosubstrate binding or stimulation of melibiose transpor

70 elical 'lid' region that gates access to the cosubstrate binding pocket and an active center that con

71 sferase displays a relatively well-conserved cosubstrate binding pocket but is unique in its active s

72 red in the apo form but becomes ordered upon cosubstrate binding.

73 ly conserved Thr-467, which is implicated in cosubstrate binding.

74 e, resulting in the reorientation of several cosubstrate-binding residues.

75 Both cosubstrate-binding sites are mainly contributed by the

76 Thus it seems that oxygen (the cosubstrate) binds in a different site to that observed

77 Thus NADPH is not only crucial as a cosubstrate, but can also act as a molecular chaperone t

78 3-MeBFPP, is a substrate with three peptide cosubstrates, but is not an effective substrate with a f

79 as substrates for the alkylation of peptide cosubstrates by yeast protein farnesyl transferase.

80 TS that does not require CH(2)H(4)folate as cosubstrate, by mutant TSs was analyzed and showed that

81 gards to kcat and Km values for dUMP and the cosubstrate CH2H4-folate.

82 ored by 1.7-10.0-fold in the presence of the cosubstrate CoASH, while the entropy becomes 2.0-22.5-fo

83 Cosubstrate coenzyme A (CoA), the phosphopantetheinyl gr

84 This emergent behavior, which we named cosubstrate compensation (CSC), enables the ETC to maint

85 trates under conditions with a subsaturating cosubstrate concentration and uncompetitive against preQ

86 LacY cause effects on sugar recognition and cosubstrate coupling that are stereotypical of neutral s

87 ffects on melibiose transport and binding of cosubstrates depended on the physical-chemical propertie

88 RoxA incorporates both oxygen atoms of its cosubstrate dioxygen into the rubber cleavage product OD

89 d holo forms of AKR11A demonstrates that the cosubstrate does not play the dramatic role in active si

90 The addition of reducing cosubstrate during reaction of PGHS-1 with peroxide prot

91 his corrects a longstanding misperception of cosubstrate effects, provides more realistic kinetic con

92 In the absence of cosubstrate, enzyme catalyzed the enolization/proton exc

93 reducing equivalents for its healthy growth; cosubstrate experiments support this finding.

94 Its cosubstrate, FADH(2), is supplied by HpaC, an NAD(P)H-fl

95 Microsomal uptake of the cosubstrate for all glucuronidation reactions, UDP-glucu

96 mes responsible for producing the obligatory cosubstrate for all sulfotransferases.

97 NADPH is an obligatory cosubstrate for iNOS synthesis of NO.

98 ,200-Da homodimer, and FMNH2 is an essential cosubstrate for its activity.

99 trons from one reaction to another, and as a cosubstrate for other enzymes such as the sirtuins and p

100 ld be expected if Ca(2+) were only used as a cosubstrate for the nucleotide substrate, but rather fol

101 3'-phosphoadenosine-5 '-phosphosulfate, the cosubstrate for the sulfonation reaction.

102 Many cosubstrates for the peroxidase activity of prostaglandi

103 g enzyme (k(cat) = 250 s(-)1) that binds the cosubstrate fructose 6-phosphate (Fru-6-P) with relative

104 es not alter the apparent affinities for the cosubstrates glutamate or sodium.

105 affinity (KD =130 nm) in the presence of the cosubstrate glutathione (GSH).

106 m transfer and halogenation reactions (using cosubstrates guaiacol, thioanisole, and monochlorodimedo

107 the normal order of addition of the oxidant cosubstrate (H(2)O(2)) before organic substrate [2,4,6-t

108 peroxidase order of addition of the oxidant cosubstrate (H(2)O(2)) followed by organic substrate (TC

109 nucleotide (NAD(+)) is an enzyme cofactor or cosubstrate in many essential biological pathways.

110 chain that blocks the site for a nucleophile cosubstrate in PRTases.

111 , 13-diacetylbaccatin III and benzoyl-CoA as cosubstrates in the corresponding cell-free extract.

112 ormation about the substrate specificity and cosubstrate inhibition of the enzyme.

113 We present evidence that an organic cosubstrate inhibits NDFO, likely by keeping periplasmic

114 pport the view that translocation of the UGT cosubstrate is a rate-limiting step of the glucuronidati

115 We show here that the preferred cosubstrate is actually H2O2 and that HppE therefore alm

116 d in conditions under which the substrate or cosubstrate is consumed in a multielectron redox process

117 The loop that folds over the NAD(P)H cosubstrate is disordered in the apo form but becomes or

118 oxidatic activity with different peroxidatic cosubstrates is comparable for KatA and KatB, but KatA i

119 In previous studies, using ATP as the cosubstrate, it was reported that the APH(2'')-Ia domain

120 tude of that observed with its natural thiol cosubstrate, L-homocysteine.

121 PEP appears to depend on the presence of the cosubstrate MgATP.

122 ctor, are used to deliver electrons from the cosubstrate NADPH to molecular oxygen, analogous to othe

123 l reductase domain binds FAD and FMN and the cosubstrate NADPH.

124 method, the kinetics of the reaction of the cosubstrate nicotinamide adenine dinucleotide and the co

125 H(2)O(2) inhibition by converting it to the cosubstrate O(2).

126 roxide (H2O2) and bromide (Br-), a preferred cosubstrate of EPO, to generate the cytotoxic oxidant hy

127 t conjugates to a bovine serum albumin (BSA) cosubstrate of larger hydrodynamic mass.

128 duction of alpha-ketoglutarate (alpha-KG), a cosubstrate of TATase required to regenerate the pyridox

129 of GOx was not oxidized by O(2), the natural cosubstrate of the enzyme.

130 ated that GTP, and not ATP, is the preferred cosubstrate of this enzyme.

131 ty can seriously overestimate the effects of cosubstrate on cyclooxygenase velocity.

132 e effect of the concentration of the various cosubstrates on the POD reaction rate demonstrated that

133 llographic analyses reveal inhibition by 2OG cosubstrate or primary substrate competitors as well as

134 zyme to the mixed-valent form, and O(2), the cosubstrate, oxidizes the fully reduced form to the mixe

135 the addition of substrate, TBP, prior to the cosubstrate, peroxide.

136 pted re-examination of the effect of several cosubstrates (phenol, acetaminophen, N,N,N',N'-tetrameth

137 tion consists of the formation of a cofactor(cosubstrate)-PKMT-substrate complex, lysine deprotonatio

138 Addition of SAM tightened up the cosubstrate pocket in both proteins and prevented the al

139 e measurements with a chromogenic peroxidase cosubstrate previously were used to evaluate the kinetic

140 The cosubstrates produced only a slight (10-60%) stimulation

141 We recently demonstrated the substrate and cosubstrate promiscuity of the wild-type human ChAT (hCh

142 (NO) interactions as they may relate to the cosubstrate, pseudo halide thiocyanate (SCN(-)), and sub

143 e presence of O2, chloride ion, and L-Trp as cosubstrates, purified RebH displays robust regiospecifi

144 conventional conformation of the bound NADP+ cosubstrate, raising the possibility that it donates the

145 on than the WT enzyme in the presence of the cosubstrate/reductant ascorbate and that this process is

146 flavoprotein monooxygenases and their common cosubstrate requirements, the reaction of FADH(2) and O(

147 s as a binary complex with its desmethylated cosubstrate S-adenosyl-l-homocysteine.

148 The cosubstrate S-adenosylmethionine (SAM) stabilizes the ac

149 productive CO(2) loss in the presence of the cosubstrate S-adenosylmethionine (SAM), with S-adenosylh

150 Addition of the cosubstrate, S-adenosylmethionine (SAM), prevents degrad

151 controls reactivity by interactions with the cosubstrate, SAM, which is bound to the catalytic iron-s

152 (-) or Cl(-) is oxidized in the absence of a cosubstrate, show that only modest tuning is required to

153 domain; however, glycerol is not acting as a cosubstrate since no glycerophosphate product was detect

154 , with a completely unoccupied substrate and cosubstrate site, while the ternary complex is the first

155 by simultaneously blocking the substrate and cosubstrate sites, as revealed by structural analyses.

156 main that is bound at both the substrate and cosubstrate sites.

157 n between MTS derivatives and A395C, and the cosubstrate, sodium, slows reaction of MTSEA with Y405C

158 Using lipid II precursor as cosubstrate, sortase A catalyzes the amide linkage betwe

159 ere previously shown to dictate the acyl-CoA cosubstrate specificity in the carnitine series.

160 Similar alterations in nucleophile cosubstrate specificity were also observed.

161 ently distinct molecular mechanisms coupling cosubstrate/ substrate binding to catalytic activity.

162 nt on the concentrations of their respective cosubstrates, suggesting that both ligands bind randomly

163 and dioxygen for catalysis with the alpha-KG cosubstrate supplying the additional reducing equivalent

164 might regenerate 2-oxoglutarate, which is a cosubstrate that facilitates the breakdown of alanine by

165 NAD(+)) is an endogenous enzyme cofactor and cosubstrate that has effects on diverse cellular and phy

166 PAPS is the obligate cosubstrate that is synthesized in tissues to make avail

167 Furthermore, when 2m is the cosubstrate, the affinity of 29G12 for its dipole 1a is

168 yrrolyl-2-carboxyl-thioester of CouN1 is the cosubstrate, the in vitro product differs from clorobioc

169 ibition using dihydrofolate and NADPH as the cosubstrates, the previously unreported compounds 2 and

170 Peroxidase cosubstrates thus have a much smaller stimulatory effect

171 fectively uses plasma levels of bromide as a cosubstrate to brominate bases in nucleotides and double

172 nergy from the downhill translocation of one cosubstrate to catalyze the accumulation of the other.

173 r non-heme-iron(II) cofactor and dioxygen as cosubstrate to cleave these C-H bonds and direct the rin

174 , the AcuC protein did not require NAD(+) as cosubstrate to deacetylate AcsA(Ac).

175 ses iron as its cofactor and dioxygen as its cosubstrate to effect the unique, ring-cleaving, four-el

176 H2O2 by utilizing plasma levels of Br- as a cosubstrate to form potent brominating agents.

177 strates while decomposing the 2-oxoglutarate cosubstrate to form succinate and CO(2).

178 r hydrogen peroxide or molecular oxygen as a cosubstrate to generate a reactive halogen atom for cata

179 e, and the ferrocenium methanol acted as the cosubstrate to GOx to catalyze the oxidation of glucose

180 tion catalyst, using coenzyme A (CoASH) as a cosubstrate to phosphopantetheinylate Ser880 of the 155-

181 have generally employed dithiothreitol as a cosubstrate to reductively cleave the persulfide interme

182 four electrons per turnover to reduce the O2 cosubstrate to the oxidation state of water and incorpor

183 ation number change with the binding of both cosubstrates to the enzyme, and determines this to be du

184 eficient in binding a particular cofactor or cosubstrate, to complement each other by generating NO u

185 In complex with the cosubstrate UDP-N-acetylglucosamine (UDP-GlcNAc),O-linke

186 The IPP analogue (3-ClIPP) was a cosubstrate when incubated with dimethylallyl diphosphat

187 enzymes is their utilization of NAD(+) as a cosubstrate, which has led to the suggestion that Sir2 a

188 In the absence of added reducing cosubstrates, which maximizes the levels of oxidized enz

189 rationale, catalysis by CD-0387 with 2-ME as cosubstrate, while less efficient, is not subject to pot

190 (CT)) have been successfully employed as the cosubstrate with S. lentus in the biodegradation of an a

191 12 accepts a bulky hydrophobic dipolarophile cosubstrate, with rates of product formation up to 70-fo