ライフサイエンスコーパス: multienzyme

1 constructing useful synthetic assembly-line multienzymes.

2 New multienzyme amperometric biosensors are presented here w

3 n nature, we developed an efficient two-step multienzyme approach for the synthesis of a series of GD

4 We have used a novel multienzyme approach to generate a set of highly represe

5 nslocated to the appropriate site on the PKS multienzyme are located at the N-terminal region of the

6 These large multienzymes are organized into a series of functional u

7 The applicability of the new multienzyme assay to wine samples is illustrated.

8 synthases (PKSs) are a family of homologous multienzyme assemblies that catalyze the biosynthesis of

9 Editosomes are megadalton multienzyme assemblies that provide a catalytic surface

10 respiratory chain complexes can arrange into multienzyme assemblies, so-called supercomplexes.

11 types of active sites within this family of multienzyme assemblies.

12 The Escherichia coli RNA degradosome is a multienzyme assembly that functions in transcript turnov

13 assembly of conotoxins is a highly regulated multienzyme-assisted process.

14 This multienzyme bidirectional helicase-primase complex can p

15 ucts produced on modular polyketide synthase multienzymes by an assembly-line process in which each m

16 xidase, and highlights the potential of this multienzyme cascade for the efficient synthesis of chira

17 Herein we report the application of a multienzyme cascade, generated in a single bacterial who

18 ds that organize the spatial arrangements of multienzyme cascades with control over their relative di

19 ssembly of a cyclase complex or even a large multienzyme catalytic center.

20 The multienzyme catalytic phosphorylation of phosphatidylino

21 hydrolase into the bacterial cellulosome, a multienzyme cellulolytic complex, via its interaction wi

22 Clostridium cellulovorans produces a multienzyme cellulose-degrading complex called the cellu

23 cus flavefaciens produces a highly organized multienzyme cellulosome complex that plays a key role in

24 idly solubilizes cellulose with the aid of a multienzyme cellulosome complex.

25 dules play a crucial role in the assembly of multienzyme cellulosome complexes.

26 fungal and bacterial cellulase systems, the multienzyme cellulosome system of the anaerobic, cellulo

27 sible chaperone in the assembly of CynD or a multienzyme CNO complex.

28 scherichia coli 1-lip pyruvate dehydrogenase multienzyme complex (1-lip PDHc) with the C259N and C259

29 branched chain alpha-ketoacid dehydrogenase multienzyme complex (approximately 4-5 x 10(3) kDa) is a

30 The pyruvate dehydrogenase multienzyme complex (Mr of 5-10 million) is assembled ar

31 es of the human 2-oxoglutarate dehydrogenase multienzyme complex (OGDHc), a rate-limiting enzyme in t

32 2) phosphorylates the pyruvate dehydrogenase multienzyme complex (PDC) and thereby controls the rate

33 The pyruvate dehydrogenase multienzyme complex (PDC) is a key regulatory point in c

34 s the activity of the pyruvate dehydrogenase multienzyme complex (PDC).

35 (E3) subunits of the pyruvate dehydrogenase multienzyme complex (PDH).

36 the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDHc) and its E1 (ThDP-dependent) c

37 the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDHc) by its coenzyme thiamin dipho

38 the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDHc) has been determined at a reso

39 the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDHc) has been determined with phos

40 the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDHc), as a representative of the P

41 the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDHc), binds to the enzyme with gre

42 The Escherichia coli pyruvate dehydrogenase multienzyme complex (PDHc), consisting of multiple copie

43 herichia coli's 2-oxoglutarate dehydrogenase multienzyme complex (termed BBL) with a combination of s

44 lation of biotin and is one component of the multienzyme complex acetyl-CoA carboxylase that catalyze

45 lation of biotin and is one component of the multienzyme complex acetyl-CoA carboxylase that catalyze

46 lation of biotin and is one component of the multienzyme complex acetyl-CoA carboxylase, which cataly

47 th variants displayed pyruvate dehydrogenase multienzyme complex activity at levels of 11% (Y177A E1)

48 us stearothermophilus pyruvate dehydrogenase multienzyme complex adopts a unique, compact structure.

49 ated the composition and organization of the multienzyme complex alpha-ketoglutarate dehydrogenase (a

50 ering the understanding of its function in a multienzyme complex and in the membrane-bound P64K prote

51 performs two functions: It is a respiratory multienzyme complex and it recognizes a mitochondrial ta

52 dmark structure was the first structure of a multienzyme complex and the first structure revealing an

53 t of Escherichia coli pyruvate dehydrogenase multienzyme complex are essential for several catalytic

54 ch probably have consequences in the overall multienzyme complex assembly.

55 utida and P. aeruginosa encode the inducible multienzyme complex branched-chain keto acid dehydrogena

56 for its growth and produces an extracellular multienzyme complex called the cellulosome, which is inv

57 he entire assembly and characterization of a multienzyme complex can be completed within 1-2 weeks.

58 The multienzyme complex catalyzes the reversible oxidation o

59 nformation regarding recognition within this multienzyme complex class with an alpha(2) E1 assembly.

60 the entire family of homodimeric (alpha2) E1 multienzyme complex components, and should serve as a mo

61 lar eukaryotes, one of these assemblies is a multienzyme complex composed of eight proteins that have

62 integral component of T4 dNTP synthetase, a multienzyme complex containing phage-coded enzymes, whic

63 The Escherichia coli pyruvate dehydrogenase multienzyme complex contains multiple copies of three en

64 s by E3 or E1, respectively, showed that the multienzyme complex does not behave as a simple competit

65 domains of E1p relative to heterotetrameric multienzyme complex E1 components operating on branched

66 gnment of the E. coli pyruvate dehydrogenase multienzyme complex E1 subunit and yeast transketolase c

67 two enzymes are found in dNTP synthetase, a multienzyme complex for deoxyribonucleotide biosynthesis

68 virus (mORV) core particle is an icosahedral multienzyme complex for viral mRNA synthesis and provide

69 cetyl-CoA decarbonylase/synthase (ACDS) is a multienzyme complex found in methanogens and certain oth

70 (E2) component of the pyruvate dehydrogenase multienzyme complex from Bacillus stearothermophilus is

71 The pyruvate dehydrogenase multienzyme complex from Bacillus stearothermophilus was

72 ranscarboxylase is a 1.2 million Dalton (Da) multienzyme complex from Propionibacterium shermanii tha

73 ins both en route to the lysosome and in the multienzyme complex has remained elusive.

74 the acetyl-CoA decarbonylase/synthase (ACDS) multienzyme complex in Archaea.

75 It is the first structure of any multienzyme complex in pyrimidine biosynthesis and is a

76 restingly, GSK3beta can be released from the multienzyme complex in response to PKA phosphorylation o

77 viding biophysical evidence for a diffusible multienzyme complex in the mitochondrial matrix.

78 quivalent domain in a pyruvate dehydrogenase multienzyme complex in which the domain remains of const

79 anched-chain keto acid dehydrogenase (BCKAD) multienzyme complex involved in branched-chain fatty aci

80 the Escherichia coli pyruvate dehydrogenase multienzyme complex is an outcome of redistribution of a

81 omponent of the 2-oxoglutarate dehydrogenase multienzyme complex is composed of 24 subunits arranged

82 This multienzyme complex is itself regulated through reversib

83 ne-depleted conditions, these enzymes form a multienzyme complex known as the purinosome.

84 l and functional organization of the largest multienzyme complex known.

85 polypeptide from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus assem

86 omponent of the pyruvate dehydrogenase (PDH) multienzyme complex of Bacillus stearothermophilus has i

87 In the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus, the

88 tyltransferase in the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus.

89 n interactions in the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus.

90 rase component of the pyruvate dehydrogenase multienzyme complex of Escherichia coli is catalysed spe

91 de chain of the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli was over-express

92 Glu139 of the large alpha-subunit of the multienzyme complex of fatty acid oxidation from Escheri

93 His450 of the large alpha-subunit of the multienzyme complex of fatty acid oxidation from Escheri

94 f the branched-chain keto acid dehydrogenase multienzyme complex of Pseudomonas putida.

95 th subunits of the fatty acid beta-oxidation multienzyme complex that are normally present in the mat

96 rom Propionibacterium shermanii is a 1.2 MDa multienzyme complex that couples two carboxylation react

97 oduces the prototypical cellulosome, a large multienzyme complex that efficiently hydrolyzes plant ce

98 Tryptophan synthase is an alpha2beta2 multienzyme complex that exhibits coupling of the alpha-

99 al gene copies of the pyruvate dehydrogenase multienzyme complex that have evolved into a pyruvate de

100 Component A3a is a multienzyme complex that includes the mcrC gene product,

101 troviral protease is a key enzyme in a viral multienzyme complex that initiates an ordered sequence o

102 dy, we demonstrate that this pathway forms a multienzyme complex that is associated with the nuclear

103 etases examined can be isolated as part of a multienzyme complex that is more stable, and consequentl

104 SAHH associates with DAO as part of a larger multienzyme complex that may function in planta as a nic

105 cetyl-CoA decarbonylase/synthase (ACDS) is a multienzyme complex that plays a central role in energy

106 s still carried out, but in the context of a multienzyme complex that remains structurally intact dur

107 onucleoside triphosphate biosynthesis form a multienzyme complex that we call T4 deoxyribonucleoside

108 novo purine biosynthetic pathway may form a multienzyme complex to facilitate substrate flux through

109 esized and posttranslationally modified by a multienzyme complex to their biologically active forms.

110 A (PPCA), a serine carboxypeptidase, forms a multienzyme complex with beta-galactosidase and neuramin

111 Lysosomal neuraminidase-1 (NEU1) forms a multienzyme complex with beta-galactosidase and protecti

112 The Escherichia coli degradosome is a multienzyme complex with four major protein components:

113 The study revealed that the multienzyme complex with the active sites directed towar

114 n-regulated chloroplast protein CP12 forms a multienzyme complex with the Calvin-Benson cycle enzymes

115 he nucleus during S-phase, where they form a multienzyme complex with thymidylate synthase (TYMS) and

116 the Escherichia coli pyruvate dehydrogenase multienzyme complex with Y177A and Y177F substitutions w

117 is an independent folding domain of a large multienzyme complex, 2-oxoglutarate dehydrogenase.

118 sembles its catalytic apparatus into a large multienzyme complex, the cellulosome.

119 The reaction is catalyzed by a 0.8 MDa multienzyme complex, the editosome.

120 Evidence has been presented for a metabolic multienzyme complex, the purinosome, that participates i

121 By linking the MAP3K, MAP2K and MAPK into a multienzyme complex, these MAPK-specific scaffold protei

122 mponents of the 2-oxoglutarate dehydrogenase multienzyme complex.

123 onents of the E. coli pyruvate dehydrogenase multienzyme complex.

124 omponent of the human pyruvate dehydrogenase multienzyme complex.

125 pyruvate by the pyruvate dehydrogenase (PDH) multienzyme complex.

126 ications are believed to be carried out by a multienzyme complex.

127 Glu462 increases the thermostability of the multienzyme complex.

128 , which confer quaternary flexibility to the multienzyme complex.

129 mbly of the cellulosomal components into the multienzyme complex.

130 iffer considerably from those of the larger, multienzyme complexes (cellulosomes).

131 encoding three alpha-ketoacid dehydrogenase multienzyme complexes (KADHs) that have central metaboli

132 s about the functional significance of these multienzyme complexes and whether they might play a more

133 The pyruvate dehydrogenase multienzyme complexes are among the largest multifunctio

134 he pyruvate and 2-oxoglutarate dehydrogenase multienzyme complexes are specifically recognised by the

135 type activity levels for E3 and all affected multienzyme complexes but are phenotypically normal.

136 nd E2 enzymes of the 2-oxoacid dehydrogenase multienzyme complexes by a previous model.

137 ipoyl cofactor, which is employed by several multienzyme complexes for the oxidative decarboxylation

138 from the family of 2-oxo acid dehydrogenase multienzyme complexes form large protein scaffolds, to w

139 In nature, the catalytic efficiency of multienzyme complexes highly depends on their spatial or

140 hesis seems to be spatially regulated by the multienzyme complexes in a cluster-size-dependent manner

141 bition method may be a powerful way to study multienzyme complexes in their physiological context.

142 ofactor required for the function of several multienzyme complexes involved in the oxidative decarbox

143 tion are still unknown, but the formation of multienzyme complexes is considered a feasible Golgi pro

144 rogenase complex (PDC) is one of the largest multienzyme complexes known and consists of a dodecahedr

145 Multienzyme complexes of fatty acid oxidation from Esche

146 shown that glycolytic enzymes (GEs) exist as multienzyme complexes on the inner surface of human eryt

147 ic enzymes (GEs) have been shown to exist in multienzyme complexes on the inner surface of the human

148 essential cofactor for several mitochondrial multienzyme complexes required for oxidative metabolism.

149 Cellulosomes are multienzyme complexes responsible for efficient degradat

150 acteria, where they are assembled into large multienzyme complexes termed cellulosomes.

151 component of the three functional classes of multienzyme complexes that catalyze the oxidative decarb

152 drogenase is a common component of mammalian multienzyme complexes that decarboxylate alpha-ketoacids

153 tabolism have long been hypothesized to form multienzyme complexes that regulate glucose flux in livi

154 tly involved in the hydratase catalysis, the multienzyme complexes with either an alpha/Asp69 --> Asn

155 oprotein in at least two major mitochondrial multienzyme complexes would be consistent with a role in

156 Through anchoring and formation of multienzyme complexes, specific, localized signal transd

157 quired for the function of several essential multienzyme complexes, such as pyruvate dehydrogenase (P

158 H are structurally and catalytically similar multienzyme complexes, suggesting a common mode of inhib

159 e assembly of one of Nature's most elaborate multienzyme complexes, the cellulosome, results from the

160 e assembly of one of nature's most elaborate multienzyme complexes, the cellulosome.

161 mes, but via one or more membrane-associated multienzyme complexes.

162 cal role in stabilizing and regulating these multienzyme complexes.

163 ns catalysed by the 2-oxo acid dehydrogenase multienzyme complexes.

164 utarate dehydrogenase, and glycine reductase multienzyme complexes.

165 utarate dehydrogenase, and glycine reductase multienzyme complexes.

166 tute for mtLPD2 and associate with all these multienzyme complexes.

167 (E3) components, of 2-oxo acid dehydrogenase multienzyme complexes.

168 rix, are interchangeable among the different multienzyme complexes.

169 integral component of the function of these multienzyme complexes.

170 that react with components of mitochondrial multienzyme complexes.

171 e additional flexibility in highly populated multienzyme complexes.

172 gluconeogenesis, supporting the formation of multienzyme complexes.

173 the quaternary structure of highly populated multienzyme complexes.

174 ote cell proliferation often proceed through multienzyme complexes.

175 dihydrolipoyl moieties of four mitochondrial multienzyme complexes: pyruvate dehydrogenase, alpha-ket

176 ence that cell wall synthesis is mediated by multienzyme complexes; however, our results suggest that

177 icrobes, cellulases are assembled into large multienzymes complexes, termed "cellulosomes," which all

178 lyketide synthase was grafted onto the first multienzyme component (DEBS1) of the erythromycin-produc

179 acilitated dynamics of communication between multienzyme components.

180 The design of multienzyme composition (MEC) was applied to yield a hyd

181 ing leftovers (broiler necks), by means of a multienzyme composition, containing four commercially av

182 is work, we re-evaluate FASP and the related multienzyme digestion (MED) FASP method.

183 dy, we used glycoproteomic analysis based on multienzyme digestion followed by LC tandem MS analysis

184 The sample was then analyzed via our multienzyme digestion procedure followed by nano liquid

185 By extending multienzyme digestion strategies that use sample filtrat

186 ed dissociation (CID), in combination with a multienzyme digestion strategy (Lys-C, trypsin, and Glu-

187 T4 genes that encode other components of the multienzyme DNA replicase.

188 Here, we describe a multienzyme effector complex (termed SHREC) that mediate

189 pathway, these factors can greatly simplify multienzyme engineering.

190 organization of the bacterial and eukaryotic multienzyme fatty acid synthase systems offer the prospe

191 open reading frames are expressed, identify multienzyme function and point to 'orphan' function.

192 chaeal PCNA 'tool-belt' recruitment model of multienzyme function that can facilitate both high fidel

193 Here we report a multienzyme-functionalized magnetic microcarriers-assist

194 lar to many non-ribosomal peptide synthetase multienzymes, has a central role.

195 rane environments and in the assembly of the multienzyme hyperstructures of bacterial cell wall biosy

196 flecting how difficult it is to purify these multienzymes in amounts adequate for kinetic and structu

197 Two levels of multienzyme labeling were used to measure a broad concen

198 fication strategy of graphene sheets and the multienzyme labeling, the developed immunosensor showed

199 A multienzyme layer containing choline oxidase (ChOx) and

200 oteins with ubiquitin is mediated by dynamic multienzyme machinery (E1, E2, and E3).

201 our results reveal a functionally relevant, multienzyme metabolic complex for glucose metabolism in

202 aching and FRET corroborate the formation of multienzyme metabolic complexes in living cells, which a

203 Previously, the studies on multienzyme nanocomplexes assembled on DNA scaffolds dem

204 Human XPA is an essential component in the multienzyme nucleotide excision repair (NER) pathway.

205 readily obtained by highly efficient one-pot multienzyme (OPME) reactions.

206 e conversion of DBT to HBP is catalyzed by a multienzyme pathway consisting of two monooxygenases and

207 The multienzyme pathway for heme formation culminates with t

208 ed by directed evolution and introduced into multienzyme pathways may lead to improved whole-cell cat

209 Several multienzyme pathways, including the excision repair of d

210 ture that is shared with other key branched, multienzyme pathways, such as glycolysis, where pathway

211 used to control PG hydrolases present within multienzyme PG-remodelling machines.

212 Cellulosomes are large, multienzyme, plant cell wall-degrading protein complexes

213 Sumoylation occurs by a multienzyme process similar to ubiquitination and, in Sa

214 so initiate blood digestion as components of multienzyme proteolytic complexes in malaria, platyhelmi

215 olled alignment of active sites promotes the multienzyme reaction efficiency.

216 ontrolled at nanoscale can have an effect on multienzyme reaction.

217 kinetic characteristics for this sequential multienzyme reaction.

218 Primosomes are multienzyme replication machines that contribute both th

219 ascent DNA chains during synthesis by the T4 multienzyme replication system in vitro.

220 DEAD-box helicase RhlB is a component of the multienzyme RNA degradosome assembly, and its interactio

221 xoribonuclease and integral component of the multienzyme RNA degradosome complex.

222 amphipathic helix at the N terminus of each multienzyme subunit which may promote dimerisation into

223 lyketide synthase composed of eight separate multienzyme subunits housing a total of 12 extension mod

224 The multienzyme system (creatininase, creatinase, sarcosine

225 ro-protease to its active form in a coupled, multienzyme system.

226 tructural and functional modularity of these multienzyme systems has raised the possibility that poly

227 bility, and selectivity compared to the same multienzyme systems immobilized to solvent cast Nafion a

228 protein) is an integral component of several multienzyme systems involved in the tricarboxylic acid (

229 parallel interplay of evolutionary events in multienzyme systems leading to functional group diversit

230 n liquid-liquid or solid-liquid extractions, multienzyme systems linked to lactate dehydrogenase and

231 feasibility of investigating the effects of multienzyme systems on the structure of final glycan pro

232 s for individual substrates are modular, and multienzyme systems that can catalyse programmable metab

233 II polyketide synthases (PKSs) are bacterial multienzyme systems that catalyze the biosynthesis of a

234 polyketide synthases (PKSs) are a family of multienzyme systems that catalyze the biosynthesis of po

235 Biofuel cell researchers have studied multienzyme systems, but they have not investigated the

236 sferase (trans-AT) polyketide synthase (PKS) multienzyme that was hypothesized to assemble gladiolin.

237 xyerythronolide B synthase (DEBS), are giant multienzymes that biosynthesize a number of clinically i

238 Such multienzymes typically use malonyl and methylmalonyl-CoA

239 Next, we developed a multienzyme workflow suitable for analysis of the differ