ライフサイエンスコーパス: coenzyme

1 rotein domain, resulting in the amide-linked coenzyme.

2 tial nicotinamide adenine dinucleotide (NAD) coenzyme.

3 es, these biomimetics outperform the natural coenzymes.

4 human Naa60 (hNaa60) in complex with Acetyl-Coenzyme A (Ac-CoA) or Coenzyme A (CoA).

5 with inositol hexaphosphate (InsP6), acetyl-coenzyme A (AcCoA) and/or substrate Resistance to Ralsto

6 at catalyzes pyruvate's conversion to acetyl coenzyme A (AcCoA), thereby connecting these two pathway

7 ased levels of acetyl phosphate, acetoacetyl coenzyme A (acetoacetyl-CoA), butyryl CoA, acetoacetate,

8 Acetyl coenzyme A (acetyl-CoA) generated from glucose and aceta

9 Metabolic production of acetyl coenzyme A (acetyl-CoA) is linked to histone acetylation

10 riglycerides, suggesting an increased acetyl coenzyme A (acetyl-CoA) load.

11 rnative carbon source utilization for acetyl coenzyme A (acetyl-CoA) production and gluconeogenesis.

12 esis by suppressing the expression of acetyl coenzyme A (acetyl-CoA) synthetase (Acss), leading to de

13 d is sensitive to the availability of acetyl coenzyme A (acetyl-CoA), we investigated a role for meta

14 demonstrate that A-485 competes with acetyl coenzyme A (acetyl-CoA).

15 e, enabling biosynthesis of cytosolic acetyl coenzyme A (acetyl-CoA, the two-carbon isoprenoid precur

16 The AMP-forming acyl coenzyme A (acyl-CoA) synthetases are a large class of e

17 ched-chain amino acid metabolism, isovaleryl-Coenzyme A (CoA) and isobutyryl-CoA, with three molecule

18 N-acyltransferase reaction using fatty acyl-coenzyme A (CoA) and long-chain base (LCB) substrates to

19 Cofactors such as NAD, AMP, and Coenzyme A (CoA) are essential for a diverse set of reac

20 (PanK) is a regulatory enzyme that controls coenzyme A (CoA) biosynthesis.

21 olution crystal structure of AF-Est2 reveals Coenzyme A (CoA) bound in the vicinity of the active sit

22 roduce mm flux through the key fluoromalonyl coenzyme A (CoA) building block, thereby offering the po

23 Pharmaceutical inhibition of acetyl-coenzyme A (CoA) carboxylase (ACC), a key fatty acid bio

24 (OG) is a small molecule inhibitor of acetyl coenzyme A (CoA) carboxylase (ACC), the enzyme that cont

25 kinase (AMPK) levels, and diminished acetyl coenzyme A (CoA) carboxylase phosphorylation than in the

26 Two genes, Psyr_2474, encoding an acyl-coenzyme A (CoA) dehydrogenase, and Psyr_4843, encoding

27 catalyzes the reduction of hydroxycinnamoyl-coenzyme A (CoA) esters using NADPH to produce hydroxyci

28 metabolic machinery for the biosynthesis of Coenzyme A (CoA) from exogenous pantothenic acid (Vitami

29 While homologous to mammalian enoyl-coenzyme A (CoA) hydratases, EchA6 is non-catalytic yet

30 brida) flowers have the precursor 4-coumaryl coenzyme A (CoA) in common.

31 o enzymes, Ptr4CL3 and Ptr4CL5, catalyze the coenzyme A (CoA) ligation of 4-coumaric acid to 4-coumar

32 ation of the meta-hydroxyl group of caffeoyl-coenzyme A (CoA) on the pathway to monolignols, with the

33 cate that YacG is frequently associated with coenzyme A (CoA) production enzymes, linking the protein

34 levels of intermediate and anaplerotic acyl-coenzyme A (CoA) species incorporated into the Krebs cyc

35 tauri extraplastidial lipids, while the 16:4-coenzyme A (CoA) species was not detected.

36 carbon-carbon bond forming step between acyl coenzyme A (CoA) substrates offer a versatile route for

37 tochondrion-associated long-chain fatty acyl coenzyme A (CoA) thioesterase that is highly expressed i

38 lysophosphatidylethanolamine (LPE) with acyl-coenzyme A (CoA), designated LYSOPHOSPHATIDYLETHANOLAMIN

39 ing the final and committed step in the acyl-coenzyme A (CoA)-dependent biosynthesis of triacylglycer

40 n complex with Acetyl-Coenzyme A (Ac-CoA) or Coenzyme A (CoA).

41 ynthesis of the universal essential cofactor Coenzyme A (CoA).

42 s FALDH) prior to activation via coupling to coenzyme A (CoA).

43 anine, spermine, dihydrouracil, and acryloyl-coenzyme A (CoA).

44 ocess that requires the generation of acetyl-coenzyme A (CoA).

45 es high carbon flux through the ethylmalonyl coenzyme A (ethylmalonyl-CoA) pathway (EMC pathway).

46 tein E (ApoE) and 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR)) has been linked t

47 Until recently, 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase inhibitors (statins) have

48 Hydroxy-methyl-glutaryl-coenzyme A (HMG-CoA) reductase inhibitors or statins are

49 Statins, or 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase inhibitors, have anti-inf

50 ition particle or 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase.

51 We show that succinyl-coenzyme A (succinyl-CoA) binds to KAT2A.

52 Caffeoyl-coenzyme A 3-O-methyltransferase (CCoAOMT) is an S-adeno

53 PqsBC catalyzes the condensation of octanoyl-coenzyme A and 2-aminobenzoylacetate (2-ABA) to form the

54 best inhibitors are competitive with acetyl coenzyme A and an X-ray cocrystal structure reveals that

55 amide synthase that uses C16 fatty acid acyl-coenzyme A and dihydroxy LCB substrates but increased ac

56 e enzyme phosphotransacylase (PTAC) recycles Coenzyme A and generates an acyl phosphate that can serv

57 ation of N-acetylglutamate (NAG) from acetyl coenzyme A and glutamate.

58 irement for growth and specifically inhibits coenzyme A and isoleucine biosynthesis.

59 ze the hydrolysis of thioester bonds between coenzyme A and phenylacetyl-CoA.

60 Upon incubation of the enzyme with acyl-coenzyme A and reduced nicotinamide adenine dinucleotide

61 to depletion of the energy substrate acetyl coenzyme A and the antioxidant glutathione.

62 ynthases that use very-long-chain fatty acyl-coenzyme A and trihydroxy LCB substrates.

63 s the polymerization of 3-(R)-hydroxybutyryl-coenzyme A as a means of carbon storage in many bacteria

64 cyltransferase that uses preferentially 16:0-coenzyme A as an acyl donor.

65 eracting partner, Golgi adaptor protein acyl-coenzyme A binding domain containing protein 3 (ACBD3).

66 uncover that the Golgi resident protein acyl-coenzyme A binding domain-containing 3 (ACBD3) serves as

67 emperature as the different variants of acyl-coenzyme A binding protein have similar m-values when th

68 This is the second inborn error of coenzyme A biosynthesis to be implicated in NBIA.

69 mulates the conversion of pyruvate to acetyl-coenzyme A by the pyruvate dehydrogenase complex.

70 ar gene (ACC2) that targets homomeric acetyl-coenzyme A carboxylase (ACCase) to plastids.

71 T cell-specific deletion of acetyl coenzyme A carboxylase 1 (ACC1), an enzyme that catalyze

72 tural environments, where heteromeric acetyl-coenzyme A carboxylase encoded in part by the chloroplas

73 d nuclear gene that targets homomeric acetyl-coenzyme A carboxylase to plastids, where the multidomai

74 in ACC2, encoding a plastid-targeted acetyl-coenzyme A carboxylase, cause hypersensitivity to specti

75 DI-010976, an allosteric inhibitor of acetyl-coenzyme A carboxylases (ACC) ACC1 and ACC2, reduces hep

76 the post-translational biotinylation of acyl coenzyme A carboxylases.

77 3) Direct acetyl transfer between LD and coenzyme A catalyzed by E2pCD was observed with a rate c

78 ecreased the expression of medium-chain acyl coenzyme A dehydrogenase (MCAD) and short-chain acyl coe

79 A dehydrogenase (MCAD) and short-chain acyl coenzyme A dehydrogenase (SCAD), involved in the regulat

80 unable to convert free fatty acids to their coenzyme A derivatives, accumulates free fatty acids dur

81 Changes in stearoyl-coenzyme A desaturase (SCD) expression and activity were

82 0 (P = 1.6 x 10(-8)) as a marker of stearoyl coenzyme A desaturase 1 activity, and the ratio of 20:3n

83 level on the non-heme diiron enzyme benzoyl coenzyme A epoxidase, BoxB.

84 The biosynthesis of the major acyl carrier Coenzyme A from pantothenic acid (PA) is critical for su

85 degradation through hydration of the dienoyl-coenzyme A intermediate as observed in Geobacter metalli

86 Coenzyme A is an essential metabolite known for its cent

87 In cells, Coenzyme A is synthesized de novo in five enzymatic step

88 Downregulation of 4-coumaric acid:coenzyme A ligase (4CL) can reduce lignin content in a n

89 nolignols under the catalysis of p-coumaroyl-coenzyme A monolignol transferase (PMT).

90 The rice (Oryza sativa) p-COUMAROYL-Coenzyme A MONOLIGNOL TRANSFERASE gene was introduced in

91 Plants expressing the p-COUMAROYL-Coenzyme A MONOLIGNOL TRANSFERASE transgene can therefor

92 tion, we cloned and characterized a caffeoyl-coenzyme A O-methyltransferase (PhCCoAOMT1) from the pet

93 s and in vivo rescue potential of the acetyl-Coenzyme A precursor S-acetyl-4'-phosphopantetheine as a

94 One therapeutic strategy is to generate Coenzyme A precursors downstream of the defective step i

95 Cinnamoyl-coenzyme A reductase (CCR) catalyzes the reduction of hy

96 olesterol, in the 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCR) activity, and in the in vit

97 3-hydroxy-3-methylglutaryl-Coenzyme A reductase (HMGCR) encodes the rate-limiting e

98 ombination with a 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMGCR) inhibitor (statin), will re

99 ubiquitination of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCR), which catalyzes a rate-lim

100 particle (SRP) or 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMGCR).

101 ncoding PCSK9 and 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMGCR; the target of statins) as i

102 interfering with 3-hydroxy-3-methyl glutaryl coenzyme A reductase (HMGR) activity, a key player in is

103 The enzyme 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGR) has a key regulatory role in

104 Inhibitors of 3-hydroxy-3-methylglutaryl-Coenzyme A reductase and isoprenylation attenuated, wher

105 Hydroxymethyl glutaryl-coenzyme A reductase degradation protein 1 (Hrd1) is an

106 es of the influence of hydroxymethylglutaryl-coenzyme A reductase inhibitors (also known as statins)

107 Purpose The 3-hydroxy-3-methylglutaryl-coenzyme A reductase inhibitors (statins) have activity

108 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors (statins) have been vari

109 Statins, 3-hydroxy-3-methyl-glutaryl-coenzyme A reductase inhibitors have been shown to impro

110 Statins (3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors) are an important group

111 Statins (3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors), commonly prescribed in

112 ted with elevated 3-hydroxy-3-methylglutaryl-coenzyme A reductase mRNA levels and anti-Src-Tyr416 imm

113 osynthetic enzyme 3-hydroxy-3-methylglutaryl-coenzyme A reductase results from its sterol-induced bin

114 roxylase) and ccr1g (deficient for cinnamoyl-coenzyme A reductase) lines, albeit to a lower extent.

115 protein 2, human 3-hydroxy-3-methylglutaryl-coenzyme A reductase, and human low-density lipoprotein

116 e-limiting enzyme 3-hydroxy-3-methylglutaryl-coenzyme A reductase, and increased plasma membrane chol

117 ically inhibiting 3-hydroxy-3-methylglutaryl coenzyme A reductase, which is a rate-limiting enzyme fo

118 Here, we reintroduced CINNAMOYL-COENZYME A REDUCTASE1 (CCR1) expression specifically in

119 he genes encoding 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A REDUCTASE1 (HMGR1) and MAKIBISHI1, the rate-l

120 The acetyl coenzyme A synthase (ACS) enzyme plays a central role in

121 onfirmed the role of a hydroxymethylglutaryl-coenzyme A synthase cassette, three flavin-dependent tai

122 ein-based model for the NiP center of acetyl coenzyme A synthase using a nickel-substituted azurin pr

123 nic genes such as 3-hydroxy-3-methylglutaryl-coenzyme A synthase, fatty acid synthase, and stearoyl-C

124 this study is to explore parasite fatty acyl-coenzyme A synthetase (ACS) as a novel drug target.

125 Succinyl Coenzyme A synthetase (SCS) is a key mitochondrial enzym

126 Although many Archaea have AMP-Acs (acetyl-coenzyme A synthetase) and ADP-Acs, the extant methanoge

127 ctroscopy, the cutin mutants long-chain acyl-coenzyme A synthetase2 (lacs2), permeable cuticle1 (pec1

128 enin polyketide biosynthetic metabolon (ACYL COENZYME A SYNTHETASE5, POLYKETIDE SYNTHASE A [PKSA], PK

129 is activation is mediated by long-chain acyl-coenzyme A synthetases (LACSs), which are encoded by a f

130 cycle for the generation of cytosolic acetyl-coenzyme A that can be used for fatty acid and cholester

131 need to be converted to their corresponding coenzyme A thioesters to become metabolically available.

132 It catalyzes acyl-coenzyme A thioesters to synthesize naringenin chalcone

133 talyze the sequential esterification of acyl-coenzyme A thioesters to the R4, R3, R3', and R2 positio

134 aine via the activated benzoyl- or cinnamoyl-Coenzyme A thioesters, respectively.

135 Of the two major 3-ketoacyl coenzyme A thiolases, KAT2 plays the primary role in BA

136 LDHA maintains high concentrations of acetyl-coenzyme A to enhance histone acetylation and transcript

137 n enzyme that catalyzes conversion of acetyl coenzyme A to malonyl coenzyme A, a carbon donor for lon

138 the transfer of an acetyl group from acetyl coenzyme A to polyamines such as spermidine and spermine

139 rix where glycine is condensed with succinyl coenzyme A to yield delta-aminolevulinic acid.

140 the synthesis of nicotinate, NAD+, NADP+ and coenzyme A were detected among the essential vitamins an

141 he transfer of an acetyl group from P-HPD to coenzyme A yielding dihydroxyacetone phosphate and acety

142 tins, or HMG CoA (3-hydroxy-3-methylglutaryl-coenzyme A) reductase inhibitors, are drugs with multipl

143 s conversion of acetyl coenzyme A to malonyl coenzyme A, a carbon donor for long-chain FA synthesis,

144 in vitro assay requiring only isolated LDs, Coenzyme A, and ATP to drive lipid synthesis.

145 imidine, isoprenoid, methionine, riboflavin, coenzyme A, and folate, as well as other biosynthetic pa

146 ate (P-HPD, an isomer of AI-2-phosphate) and coenzyme A, determine the crystal structure of an LsrF c

147 ex (PDHc), which converts pyruvate to acetyl coenzyme A, enables E. coli to resist these antimicrobia

148 ctly dependent on metabolites such as acetyl-coenzyme A, S-adenosylmethionine, and NAD+, among others

149 for their mission: E1 and E2 generate acetyl-coenzyme A, whereas the FAD/NAD(+)-dependent E3 performs

150 onverted to the central intermediate benzoyl-coenzyme A, which is enzymatically reduced to cyclohexa-

151 re, we identify the PO membrane protein acyl-coenzyme A-binding domain protein 5 (ACBD5) as a binding

152 Low-molecular mass (10 kD) cytosolic acyl-coenzyme A-binding protein (ACBP) has a substantial infl

153 Here we show that acyl-coenzyme A-binding protein (ACBP) potently facilitates v

154 SAR-related proteins THIOREDOXIN h3, ACYL-COENZYME A-BINDING PROTEIN6, and PATHOGENESIS-RELATED1 w

155 rrier protein) synthase (ACPS) catalyzes the coenzyme A-dependent activation of apo-ACPP to generate

156 ECR encoding the mitochondrial trans-2-enoyl-coenzyme A-reductase involved in human mtFAS.

157 physical interaction of the major SOAT, acyl-coenzyme A:cholesterol acyltransferase (ACAT)-related en

158 ress the cholesterol-esterifying enzyme acyl-coenzyme A:cholesterol acyltransferase (ACAT1), but not

159 of increased or decreased expression of ACYL-COENZYME A:DIACYLGLYCEROL ACYLTRANSFERASE1 (DGAT1) or PH

160 ne expressing castor FA hydroxylase and acyl-Coenzyme A:RcDGAT2 in its seeds.

161 olignol biosynthetic enzyme hydroxycinnamoyl coenzyme A:shikimate hydroxycinnamoyl transferase (HCT)

162 rget of pitavastatin, hydroxymethylglutarate coenzyme-A reductase (HMGCR), was found to be over-expre

163 We describe, for example, a putative coenzyme-A-induced-fit substrate binding mechanism media

164 The trapped ternary complex with coenzyme and product reveals five conserved basic residu

165 mprises two Rossmann fold domains which bind coenzyme and substrate respectively.

166 irst study to report identification of major coenzymes and antioxidants and quantify them, simultaneo

167 The identities of coenzymes and antioxidants in blood NMR spectra were est

168 )H NMR experiment can simultaneously measure coenzymes and antioxidants in extracts of whole human bl

169 Considering that the levels of coenzymes and antioxidants represent a sensitive measure

170 e and evaluate important metabolites such as coenzymes and antioxidants that are present at high conc

171 attachment of NAD(+)-glycerol dehydrogenase coenzyme-apoenzyme complex onto supporting gold electrod

172 phate (PMP), the two active forms of the AGT coenzyme, are found.

173 duction of methyl-coenzyme M (CH3-S-CoM) and coenzyme B (HS-CoB) to methane and heterodisulfide CoM-S

174 s essential for B12 biochemistry and renders coenzyme B12 (AdoCbl) so intriguingly suitable for enzym

175 l for human metabolism, the organocobalamins coenzyme B12 and methylcobalamin, are highly photolabile

176 m Aquincola tertiaricarbonis in complex with coenzyme B12 and the substrates (S)-3-hydroxybutyryl- an

177 e of converting vitamin B12 derivatives into coenzyme B12 by catalyzing the thermodynamically challen

178 dent of the radical chemistry common to both coenzyme B12 enzymology and its known photochemistry.

179 The catalytic power of enzymes containing coenzyme B12 has been, in some respects, the "last basti

180 On binding of coenzyme B12 the monomeric apoprotein forms tetramers in

181 which Perry Frey described as a "poor man's coenzyme B12," were believed to be relatively rare chemi

182 Bacterial coenzyme B12-dependent 2-hydroxyisobutyryl-CoA mutase (H

183 The coenzyme B12-dependent photoreceptor protein, CarH, is a

184 ermined that an ordered bi-bi mechanism with coenzyme binding first followed by the binding of substr

185 mation of an inactive dimer, alter substrate/coenzyme binding, or impair structural stability of HSD1

186 enzymatic hydride transfer with nicotinamide coenzyme biomimetics (NCBs) is critical to enhancing the

187 orters, a number of new proteins involved in coenzyme biosynthesis and iron metabolism, the pyruvate

188 group of such pathways is those involved in coenzyme biosynthesis.

189 thioether functional groups in amino acids, coenzymes, cofactors, and various products of secondary

190 The enzyme loading, working pH, and coenzyme concentration were optimized.

191 th concomitant loss of two fluoride ions and coenzyme conversion to pyridoxamine 5'-phosphate (PMP).

192 to enhancing the performance of nicotinamide coenzyme-dependent biocatalysts.

193 d 6PGDH enzymes and computer-aided substrate-coenzyme docking, the key amino acid residues responsibl

194 This study demonstrates coenzyme engineering of a hyperthermophilic 6PGDH and it

195 Coenzyme engineering that changes NAD(P) selectivity of

196 PH-binding site and was dependent on reduced coenzyme F420 (F420H2), a stronger reductant with a mid-

197 Coenzyme F420 is a redox cofactor found in methanogens a

198 t amino acids as well as rare cofactors like coenzyme F420 The latter likely accounts for the strong

199 esis of thiamin, menaquinone, molybdopterin, coenzyme F420, and heme.

200 We used comparative genomics to identify the coenzyme F430 biosynthesis (cfb) genes and characterized

201 These data show that coenzyme F430 can be synthesized from sirohydrochlorin u

202 e proteins that catalyse the biosynthesis of coenzyme F430 from sirohydrochlorin, termed CfbA-CfbE, a

203 However, it is unclear how coenzyme F430 is synthesized from the common primogenito

204 tase (MCR) is a nickel tetrahydrocorphinoid (coenzyme F430) containing enzyme involved in the biologi

205 The enzyme uses an ancillary factor called coenzyme F430, a nickel-containing modified tetrapyrrole

206 ique nickel-containing tetrapyrrole known as coenzyme F430.

207 It serves both as a critical coenzyme for enzymes that fuel reduction-oxidation react

208 Flavin mononucleotide (FMN) is a coenzyme for numerous proteins involved in key cellular

209 f PL 5'-phosphate (PLP), which is the active coenzyme form of vitamin B-6, are reduced during inflamm

210 r pyridoxal 5'-phosphate (PLP), which is the coenzyme form of vitamin B-6, may impair many metabolic

211 ispensible for all organisms, notably as the coenzyme form pyridoxal 5'-phosphate.

212 otinamide adenine dinucleotide (NAD(+)) is a coenzyme found in all living cells.

213 The ability to visualize the ubiquitous coenzymes fundamental to cellular functions, simultaneou

214 und data, reliable peak identities for these coenzymes have been established.

215 As the major coenzyme in fuel oxidation and oxidative phosphorylation

216 Adenine Dinucleotide (NADH) is an important coenzyme in the human body that participates in many met

217 he initial identification of PLP's role as a coenzyme in this extensive class of enzymes.

218 in adenine dinucleotide, which are essential coenzymes in all free-living organisms.

219 ow immobilization of anionic nucleotides and coenzymes, in addition to charge- and size-selective cap

220 of Phe 34 can influence the position of the coenzyme, indicating a new regulatory mechanism involvin

221 The lipoate coenzyme is essential for function of the pyruvate (PDH)

222 notated characteristic fingerprints for each coenzyme is provided for easy identification and absolut

223 Stoichiometric use of natural coenzymes is not viable economically, and the instabilit

224 n-imine nitrogen, which covalently binds the coenzyme, is protonated.

225 catalyzes the reversible reduction of methyl-coenzyme M (CH3-S-CoM) and coenzyme B (HS-CoB) to methan

226 Methyl-coenzyme M reductase (MCR) catalyzes the reversible redu

227 lism, including those that encode the methyl-coenzyme M reductase (MCR) complex.

228 using methane monooxygenase (MMO) and methyl coenzyme M reductase (MCR) enzymes.

229 Methyl-coenzyme M reductase (MCR) is a nickel tetrahydrocorphin

230 Methyl-coenzyme M reductase (MCR) is the key enzyme of methanog

231 Methyl-coenzyme M reductase (MCR), found in strictly anaerobic

232 ments that 3-NOP specifically targets methyl-coenzyme M reductase (MCR).

233 engineered archaeal strain to produce methyl-coenzyme M reductase from unculturable anaerobic methano

234 genesis in methanogens is mediated by methyl-coenzyme M reductase, an enzyme that is also responsible

235 Methyl-coenzyme M reductase, the rate-limiting enzyme in methan

236 substrates with extended carbon chains and a coenzyme moiety-unusual for a thiolase-are unknown.

237 adenine-dinucleotide (GlDH-NAD(+)) apoenzyme-coenzyme molecular wiring system on the base gold electr

238 synthesizes polymers of ADP-ribose from the coenzyme NAD(+) and plays multifaceted roles in cellular

239 The extent of conversion of coenzyme NAD(+) to NADH in cells is dependent on formate

240 a profound vulnerability to depletion of the coenzyme NAD+.

241 an-made synthetic biomimetics of the natural coenzymes NAD(P)H in redox biocatalysis.

242 We show that the binding of the coenzyme NADH alone or in concert with GTP results in a

243 cterium Thermotoga maritima from its natural coenzyme NADP(+) to NAD(+).

244 the enzyme azoreductase, in the presence of coenzyme NADPH, the azobenzene linkages undergo a bond s

245 Coenzymes of cellular redox reactions and cellular energ

246 dinucleotide phosphate (NADP(+) and NADPH); coenzymes of energy including adenosine triphosphate (AT

247 Coenzymes of redox reactions: oxidized/reduced nicotinam

248 slational modification or the recruitment of coenzymes or metal ions to achieve catalytic function.

249 on, and aromatization, all in the absence of coenzymes or recruitment of specialized domains.

250 d its human homolog ALDH3A1 to mitochondrial coenzyme Q (CoQ) biosynthesis, an essential pathway disr

251 mitochondrial matrix octapeptidase Oct1p and coenzyme Q (CoQ) biosynthesis-a pathway essential for mi

252 Coenzyme Q (CoQ) is an essential lipid of cells present

253 Coenzyme Q (CoQ) is an isoprenylated quinone that is ess

254 ring flavoprotein that shuttles electrons to coenzyme Q (CoQ).

255 Coenzyme Q (Q or ubiquinone) is a redox active lipid com

256 n which the intra-mitochondrial synthesis of coenzyme Q (ubiquinone, Q) and Q levels are profoundly d

257 and enables autophosphorylation but inhibits coenzyme Q biosynthesis in vivo, demonstrating functiona

258 athway, which is necessary for mitochondrial coenzyme Q biosynthesis.

259 yme Q by the other proteins constituting the coenzyme Q biosynthetic pathway.

260 amination and ultimately its conversion into coenzyme Q by the other proteins constituting the coenzy

261 The biosynthesis of coenzyme Q from pABA requires a deamination reaction at

262 inates from a depletion of the mitochondrial coenzyme Q pool.

263 S to a persulfide and transfers electrons to coenzyme Q via a flavin cofactor.

264 role in bacterial ubiquinone (also known as coenzyme Q) biosynthesis or microbial biodegradation of

265 Ubiquinone (also known as coenzyme Q) is a ubiquitous lipid-soluble redox cofactor

266 n to 4-hydroxybenzoic acid as a precursor of coenzyme Q, a redox lipid essential to the function of t

267 Ubiquinone (UQ), also referred to as coenzyme Q, is a widespread lipophilic molecule in both

268 and transferring the energy to mitochondrial coenzyme Q.

269 hyl-6-(3-methyl-2-butenyl)-1,4-benzoquinone (coenzyme Q1) as a surrogate for coenzyme Q10, the cofact

270 econd step of the final reaction sequence of Coenzyme Q10 (CoQ) biosynthesis.

271 We focused on the coenzyme Q10 (CoQ10) biosynthesis gene Coq2, the silenci

272 Primary coenzyme Q10 (CoQ10) deficiencies are rare, clinically h

273 Coenzyme Q10 (CoQ10) may represent a safe therapeutic op

274 stnatal supplementation with the antioxidant coenzyme Q10 (CoQ10) would prevent this programmed pheno

275 olet, has been used for the determination of coenzyme Q10 (CoQ10).

276 fied starch (OSA-ST) was used to encapsulate coenzyme Q10 (CoQ10).

277 Hereditary defects of coenzyme Q10 biosynthesis cause steroid-resistant nephro

278 mutations in genes that function within the coenzyme Q10 biosynthesis pathway, suggesting that SRNS

279 lls lacking MFN2 can be partially rescued by coenzyme Q10 supplementation, which suggests a possible

280 decanoic acid) and lipophilic nutraceutical (Coenzyme Q10) was investigated using a rat feeding study

281 eatine, 66 received minocycline, 71 received coenzyme Q10, 71 received GPI-1485, and 138 received pla

282 enzoquinone (coenzyme Q1) as a surrogate for coenzyme Q10, the cofactor of this enzyme.

283 is of glutathione, phospholipids, NADPH, and coenzyme Q10.

284 ial phosphatase regulator of biosynthesis of coenzyme Q6 (ubiquinone or CoQ6) and a mitochondrial red

285 ules hinders catalytic processes that employ coenzyme recycling.

286 energy exploitation including photocatalytic coenzyme regeneration, templating, and carbon nitride ba

287 Methanopterin (MPT) and its analogs are coenzymes required for methanogenesis and methylotrophy

288 etics are excellent analogues of the natural coenzymes, revealed also in crystal structures of the en

289 -to-glycine mutation of this loop flips this coenzyme selectivity and enables autophosphorylation but

290 R31I/T32I exhibited a 4,278-fold reversal of coenzyme selectivity from NADP(+) to NAD(+).

291 xhibited a ~6.4 x 10(4)-fold reversal of the coenzyme selectivity from NADP(+) to NAD(+).

292 cterium Moorella thermoacetica with reversed coenzyme selectivity from NADP(+) to NAD(+).

293 lop a rational design strategy to change the coenzyme specificity of 6-phosphogluconate dehydrogenase

294 Engineering the coenzyme specificity of redox enzymes plays an important

295 ve a dose-dependent response to nicotinamide coenzymes, such as the reduced form of nicotinamide aden

296 Pyridine nucleotides are redox coenzymes that are critical in bioenergetics, metabolism

297 The B vitamins give rise to vital coenzymes that are indispensable for growth and developm

298 rely on unstable and expensive nicotinamide coenzymes that have prevented their widespread exploitat

299 oic acid from the environment and attach the coenzyme to its cognate proteins, which are generally th

300 ter-soluble molecules act as, or as part of, coenzymes within the cell.