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1 using 2-propanol (30%, v/v) as cosolvent and 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 cleaver identified, is used as the reducing cosubstrate.
6 or Ca(2+) in its second role as a nucleotide cosubstrate.
7 that LPMOs can use H2O2, instead of O2, as a cosubstrate.
8 DP donor to the beta-OHTyr-6 of the aglycone cosubstrate.
9 ar substrates with TcdB yet uses a different cosubstrate.
10 ge that reduces ALKBH7's ability to bind its cosubstrate.
11 te substitute poorly for 2-oxoglutarate as a cosubstrate.
12 rved rate-limiting step involving release of cosubstrate.
13 y a Pictet-Spengler reaction with a carbonyl cosubstrate.
14 accommodates the adenosyl moiety of the NAD+ cosubstrate.
15 vated by a human enzyme in the presence of a cosubstrate.
16 dependent on the concentration of the oxygen cosubstrate.
17 ltetrahydropterin, respectively, was used as cosubstrate.
18 corresponding sulfinic acids using O(2) as a cosubstrate.
19 mption of the metabolically valuable alphaKG cosubstrate.
20 O chitin-binding protein CBP21 using H2O2 as cosubstrate.
21 PylB catalysis rather than canonically as a cosubstrate.
22 lize either oxygen or hydrogen peroxide as a cosubstrate.
23 lize either oxygen or hydrogen peroxide as a cosubstrate.
24 xidase utilizing NO as an electron donor and cosubstrate.
25 erized to date require molecular oxygen as a cosubstrate.
26 oxidoreductase (EmoB) to provide FMNH2 as a cosubstrate.
27 duces dehydroalanine to D-Ala using NAPDH as cosubstrate.
28 erminal alkenes using hydrogen peroxide as a cosubstrate.
29 otinamide adenine dinucleotide (NAD(+)) as a cosubstrate.
30 ced holomycin to holomycin utilizing O(2) as cosubstrate.
31 o depend upon the concentration of the other cosubstrate.
32 ncentrations of S-alkylglutathiones serve as cosubstrates.
33 between the reductant and oxygen-containing cosubstrates.
34 ate, and cytidine triphosphate were suitable cosubstrates.
35 ch as l-cysteine and beta-mercaptoethanol as cosubstrates.
36 ormula: see text] and [Formula: see text] as cosubstrates.
37 g) and then at P(gamma) (ADP-forming) of ATP cosubstrates.
38 avin reductase), chloride ion, and oxygen as cosubstrates.
39 n utilizing oxygen or hydrogen peroxide as a cosubstrate?
40 ared to Km(1a) 3.4 +/- 0.4 mM when 2a is the cosubstrate].
42 rand jellyroll core with both Fe(II) and the cosubstrate 2-oxoglutarate bound in the active site.
45 rather than utilizing the typical keto-acid cosubstrates, 2-oxoglutarate, pyruvate, and oxaloacetate
46 efficient versus the original dipolarophile cosubstrate (2m and 2a, respectively), reveals that whil
47 ture of Teg12, Teg12 bound to the desulfated cosubstrate 3'-phosphoadenosine 5'-phosphate, and Teg12
48 18-kDa PCP fragment and by radioassay using cosubstrate [3H] pantetheinyl-coenzyme A for all PCP-con
49 ((carboxylmethyl)amino)butanoic acid (CABA), cosubstrate a-ketoglutarate, and an Fe(IV)=O mimic oxova
52 Excitingly, the ternary complex of HygX with cosubstrate alpha-ketoglutarate and putative product hyg
53 e results, in Fe(II)-reconstituted TfdA, the cosubstrate alpha-KG chelates to the metal via a C-1 car
55 e conducted on TauD samples treated with NO, cosubstrate alphaKG, and either protonated or specifical
58 complex with the 10-formyl-5,8-dideazafolate cosubstrate and a glycinamide ribonucleotide analogue, h
59 also known as 2-oxoglutarate) as an obligate cosubstrate and are inhibited by succinate, fumarate, an
60 also known as 2-oxoglutarate) as an obligate cosubstrate and are inhibited by succinate, fumarate, an
62 An absolute requirement for dioxygen as a cosubstrate and iron as cofactor suggests that HIF-PH fu
64 irrespective of which aminoglycoside is the cosubstrate and occurs without a significant change in t
66 ration of the Fe(II) in the presence of both cosubstrate and substrate appears to be critical for the
67 The enzyme requires molecular oxygen as a cosubstrate and utilizes a noncovalently bound flavin co
68 Kinetic parameters of peptide and NAD(+) cosubstrates and IC(50) values of standard reference inh
72 ant forms the five-coordinate site when both cosubstrates are bound, the Fe(II) site of the Glu280Lys
73 lii lethal toxin (TcsL), which uses the same cosubstrate as TcdB but shares Rac only as a common subs
76 ous enzyme that couples the oxidation of the cosubstrate ascorbate to the oxidation of substrate ACC
77 12) by transferring the adenosyl group from cosubstrate ATP to a transient Co (1+)corrinoid species
83 tural differences that reflect substrate and cosubstrate binding effects and implies roles for the in
85 antly decreases V(max) with little effect on cosubstrate binding in G117C, G117S, and G117N mutants.
86 mutant exhibited little difference in either cosubstrate binding or stimulation of melibiose transpor
87 elical 'lid' region that gates access to the cosubstrate binding pocket and an active center that con
88 sferase displays a relatively well-conserved cosubstrate binding pocket but is unique in its active s
96 3-MeBFPP, is a substrate with three peptide cosubstrates, but is not an effective substrate with a f
98 TS that does not require CH(2)H(4)folate as cosubstrate, by mutant TSs was analyzed and showed that
100 ored by 1.7-10.0-fold in the presence of the cosubstrate CoASH, while the entropy becomes 2.0-22.5-fo
103 trates under conditions with a subsaturating cosubstrate concentration and uncompetitive against preQ
104 LacY cause effects on sugar recognition and cosubstrate coupling that are stereotypical of neutral s
105 ffects on melibiose transport and binding of cosubstrates depended on the physical-chemical propertie
106 RoxA incorporates both oxygen atoms of its cosubstrate dioxygen into the rubber cleavage product OD
107 d holo forms of AKR11A demonstrates that the cosubstrate does not play the dramatic role in active si
110 e reactivities of nonnative organic peroxide cosubstrates effectively exclude the possibility of a pi
111 his corrects a longstanding misperception of cosubstrate effects, provides more realistic kinetic con
119 S-adenosyl-l-methionine (SAM) is a necessary cosubstrate for numerous essential enzymatic reactions i
120 trons from one reaction to another, and as a cosubstrate for other enzymes such as the sirtuins and p
121 sphate-modified ATP analog, ATP-biotin, as a cosubstrate for phosphorylbiotinylation of NME1 and NME2
123 ld be expected if Ca(2+) were only used as a cosubstrate for the nucleotide substrate, but rather fol
128 g enzyme (k(cat) = 250 s(-)1) that binds the cosubstrate fructose 6-phosphate (Fru-6-P) with relative
131 m transfer and halogenation reactions (using cosubstrates guaiacol, thioanisole, and monochlorodimedo
132 the normal order of addition of the oxidant cosubstrate (H(2)O(2)) before organic substrate [2,4,6-t
133 peroxidase order of addition of the oxidant cosubstrate (H(2)O(2)) followed by organic substrate (TC
136 , 13-diacetylbaccatin III and benzoyl-CoA as cosubstrates in the corresponding cell-free extract.
137 evel activity is observed with H(2)O(2) as a cosubstrate indicating an important role in ET for O(2)
140 pport the view that translocation of the UGT cosubstrate is a rate-limiting step of the glucuronidati
144 d in conditions under which the substrate or cosubstrate is consumed in a multielectron redox process
145 with NADPH, in which the redox state of the cosubstrate is directly validated by single-crystal spec
147 oxidatic activity with different peroxidatic cosubstrates is comparable for KatA and KatB, but KatA i
151 ctor, are used to deliver electrons from the cosubstrate NADPH to molecular oxygen, analogous to othe
153 method, the kinetics of the reaction of the cosubstrate nicotinamide adenine dinucleotide and the co
155 roxide (H2O2) and bromide (Br-), a preferred cosubstrate of EPO, to generate the cytotoxic oxidant hy
157 duction of alpha-ketoglutarate (alpha-KG), a cosubstrate of TATase required to regenerate the pyridox
160 Because key metabolites are cofactors or cosubstrates of chromatin-modifying enzymes, changes in
162 e effect of the concentration of the various cosubstrates on the POD reaction rate demonstrated that
163 llographic analyses reveal inhibition by 2OG cosubstrate or primary substrate competitors as well as
164 zyme to the mixed-valent form, and O(2), the cosubstrate, oxidizes the fully reduced form to the mixe
166 pted re-examination of the effect of several cosubstrates (phenol, acetaminophen, N,N,N',N'-tetrameth
167 tion consists of the formation of a cofactor(cosubstrate)-PKMT-substrate complex, lysine deprotonatio
170 e measurements with a chromogenic peroxidase cosubstrate previously were used to evaluate the kinetic
172 We recently demonstrated the substrate and cosubstrate promiscuity of the wild-type human ChAT (hCh
174 (NO) interactions as they may relate to the cosubstrate, pseudo halide thiocyanate (SCN(-)), and sub
175 nding mode spanning the binding sites of the cosubstrate pterin and the substrate tryptophan and by c
176 ant for catalysis, specifically those of the cosubstrate pterin, the substrate tryptophan as well as
177 e presence of O2, chloride ion, and L-Trp as cosubstrates, purified RebH displays robust regiospecifi
178 conventional conformation of the bound NADP+ cosubstrate, raising the possibility that it donates the
179 on than the WT enzyme in the presence of the cosubstrate/reductant ascorbate and that this process is
180 flavoprotein monooxygenases and their common cosubstrate requirements, the reaction of FADH(2) and O(
181 mall molecule PRMT5 inhibitors engage either cosubstrate S-adenosyl methionine (SAM) or peptide-subst
184 productive CO(2) loss in the presence of the cosubstrate S-adenosylmethionine (SAM), with S-adenosylh
186 controls reactivity by interactions with the cosubstrate, SAM, which is bound to the catalytic iron-s
187 (-) or Cl(-) is oxidized in the absence of a cosubstrate, show that only modest tuning is required to
188 l Cbl analogues using glutathione or NADH as cosubstrates, similarly to previously characterized CblC
189 domain; however, glycerol is not acting as a cosubstrate since no glycerophosphate product was detect
190 , with a completely unoccupied substrate and cosubstrate site, while the ternary complex is the first
191 by simultaneously blocking the substrate and cosubstrate sites, as revealed by structural analyses.
193 n between MTS derivatives and A395C, and the cosubstrate, sodium, slows reaction of MTSEA with Y405C
198 ently distinct molecular mechanisms coupling cosubstrate/ substrate binding to catalytic activity.
199 nt on the concentrations of their respective cosubstrates, suggesting that both ligands bind randomly
200 and dioxygen for catalysis with the alpha-KG cosubstrate supplying the additional reducing equivalent
201 might regenerate 2-oxoglutarate, which is a cosubstrate that facilitates the breakdown of alanine by
202 NAD(+)) is an endogenous enzyme cofactor and cosubstrate that has effects on diverse cellular and phy
204 te conformational equilibrium in the alphaKG cosubstrate that modulates the O(2) accessibility of the
207 yrrolyl-2-carboxyl-thioester of CouN1 is the cosubstrate, the in vitro product differs from clorobioc
208 ibition using dihydrofolate and NADPH as the cosubstrates, the previously unreported compounds 2 and
210 fectively uses plasma levels of bromide as a cosubstrate to brominate bases in nucleotides and double
211 nergy from the downhill translocation of one cosubstrate to catalyze the accumulation of the other.
212 r non-heme-iron(II) cofactor and dioxygen as cosubstrate to cleave these C-H bonds and direct the rin
214 ses iron as its cofactor and dioxygen as its cosubstrate to effect the unique, ring-cleaving, four-el
217 r hydrogen peroxide or molecular oxygen as a cosubstrate to generate a reactive halogen atom for cata
218 e, and the ferrocenium methanol acted as the cosubstrate to GOx to catalyze the oxidation of glucose
219 tion catalyst, using coenzyme A (CoASH) as a cosubstrate to phosphopantetheinylate Ser880 of the 155-
220 have generally employed dithiothreitol as a cosubstrate to reductively cleave the persulfide interme
221 four electrons per turnover to reduce the O2 cosubstrate to the oxidation state of water and incorpor
222 ation number change with the binding of both cosubstrates to the enzyme, and determines this to be du
223 eficient in binding a particular cofactor or cosubstrate, to complement each other by generating NO u
226 enzymes is their utilization of NAD(+) as a cosubstrate, which has led to the suggestion that Sir2 a
228 rationale, catalysis by CD-0387 with 2-ME as cosubstrate, while less efficient, is not subject to pot
229 (CT)) have been successfully employed as the cosubstrate with S. lentus in the biodegradation of an a
230 12 accepts a bulky hydrophobic dipolarophile cosubstrate, with rates of product formation up to 70-fo
231 three enzymes efficiently used H(2)O(2) as a cosubstrate, yielding product profiles identical to thos