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1  Glu462 increases the thermostability of the multienzyme complex.
2 estigate the role that beta-Gal plays in the multienzyme complex.
3 , which confer quaternary flexibility to the multienzyme complex.
4 mbly of the cellulosomal components into the multienzyme complex.
5 mponents of the 2-oxoglutarate dehydrogenase multienzyme complex.
6 onents of the E. coli pyruvate dehydrogenase multienzyme complex.
7 omponent of the human pyruvate dehydrogenase multienzyme complex.
8 pyruvate by the pyruvate dehydrogenase (PDH) multienzyme complex.
9 ications are believed to be carried out by a multienzyme complex.
10 ributing to allosteric signal propagation in multienzyme complexes.
11 gluconeogenesis, supporting the formation of multienzyme complexes.
12 tute for mtLPD2 and associate with all these multienzyme complexes.
13 (E3) components, of 2-oxo acid dehydrogenase multienzyme complexes.
14 rix, are interchangeable among the different multienzyme complexes.
15  integral component of the function of these multienzyme complexes.
16 cal role in stabilizing and regulating these multienzyme complexes.
17  that react with components of mitochondrial multienzyme complexes.
18 e additional flexibility in highly populated multienzyme complexes.
19 the quaternary structure of highly populated multienzyme complexes.
20 ote cell proliferation often proceed through multienzyme complexes.
21 mes, but via one or more membrane-associated multienzyme complexes.
22 ns catalysed by the 2-oxo acid dehydrogenase multienzyme complexes.
23 utarate dehydrogenase, and glycine reductase multienzyme complexes.
24 utarate dehydrogenase, and glycine reductase multienzyme complexes.
25 scherichia coli 1-lip pyruvate dehydrogenase multienzyme complex (1-lip PDHc) with the C259N and C259
26  is an independent folding domain of a large multienzyme complex, 2-oxoglutarate dehydrogenase.
27 lation of biotin and is one component of the multienzyme complex acetyl-CoA carboxylase that catalyze
28 lation of biotin and is one component of the multienzyme complex acetyl-CoA carboxylase that catalyze
29 lation of biotin and is one component of the multienzyme complex acetyl-CoA carboxylase, which cataly
30 th variants displayed pyruvate dehydrogenase multienzyme complex activity at levels of 11% (Y177A E1)
31 us stearothermophilus pyruvate dehydrogenase multienzyme complex adopts a unique, compact structure.
32 ated the composition and organization of the multienzyme complex alpha-ketoglutarate dehydrogenase (a
33 ering the understanding of its function in a multienzyme complex and in the membrane-bound P64K prote
34  performs two functions: It is a respiratory multienzyme complex and it recognizes a mitochondrial ta
35 dmark structure was the first structure of a multienzyme complex and the first structure revealing an
36 r ROS generation, compromised affinities for multienzyme complexes and eventually clinical symptoms.
37 s about the functional significance of these multienzyme complexes and whether they might play a more
38  branched chain alpha-ketoacid dehydrogenase multienzyme complex (approximately 4-5 x 10(3) kDa) is a
39 t of Escherichia coli pyruvate dehydrogenase multienzyme complex are essential for several catalytic
40                   The pyruvate dehydrogenase multienzyme complexes are among the largest multifunctio
41  and disassembly of such naturally occurring multienzyme complexes are controlled.
42 he pyruvate and 2-oxoglutarate dehydrogenase multienzyme complexes are specifically recognised by the
43 ch probably have consequences in the overall multienzyme complex assembly.
44 utida and P. aeruginosa encode the inducible multienzyme complex branched-chain keto acid dehydrogena
45 type activity levels for E3 and all affected multienzyme complexes but are phenotypically normal.
46 nd E2 enzymes of the 2-oxoacid dehydrogenase multienzyme complexes by a previous model.
47 for its growth and produces an extracellular multienzyme complex called the cellulosome, which is inv
48 he entire assembly and characterization of a multienzyme complex can be completed within 1-2 weeks.
49                                          The multienzyme complex catalyzes the reversible oxidation o
50 iffer considerably from those of the larger, multienzyme complexes (cellulosomes).
51 nformation regarding recognition within this multienzyme complex class with an alpha(2) E1 assembly.
52 the entire family of homodimeric (alpha2) E1 multienzyme complex components, and should serve as a mo
53 lar eukaryotes, one of these assemblies is a multienzyme complex composed of eight proteins that have
54                         RNA degradosomes are multienzyme complexes composed of ribonucleases, RNA hel
55  integral component of T4 dNTP synthetase, a multienzyme complex containing phage-coded enzymes, whic
56  The Escherichia coli pyruvate dehydrogenase multienzyme complex contains multiple copies of three en
57 s by E3 or E1, respectively, showed that the multienzyme complex does not behave as a simple competit
58  domains of E1p relative to heterotetrameric multienzyme complex E1 components operating on branched
59 gnment of the E. coli pyruvate dehydrogenase multienzyme complex E1 subunit and yeast transketolase c
60  two enzymes are found in dNTP synthetase, a multienzyme complex for deoxyribonucleotide biosynthesis
61 virus (mORV) core particle is an icosahedral multienzyme complex for viral mRNA synthesis and provide
62 ipoyl cofactor, which is employed by several multienzyme complexes for the oxidative decarboxylation
63  from the family of 2-oxo acid dehydrogenase multienzyme complexes form large protein scaffolds, to w
64 cetyl-CoA decarbonylase/synthase (ACDS) is a multienzyme complex found in methanogens and certain oth
65 (E2) component of the pyruvate dehydrogenase multienzyme complex from Bacillus stearothermophilus is
66                   The pyruvate dehydrogenase multienzyme complex from Bacillus stearothermophilus was
67 ranscarboxylase is a 1.2 million Dalton (Da) multienzyme complex from Propionibacterium shermanii tha
68 ins both en route to the lysosome and in the multienzyme complex has remained elusive.
69 nucleotide kinase (PNK) Grc3 assemble into a multienzyme complex, herein designated RNase PNK, to orc
70       In nature, the catalytic efficiency of multienzyme complexes highly depends on their spatial or
71 ence that cell wall synthesis is mediated by multienzyme complexes; however, our results suggest that
72 the acetyl-CoA decarbonylase/synthase (ACDS) multienzyme complex in Archaea.
73   beta-Gal and neuraminidase 1 (NEU1) form a multienzyme complex in lysosomes along with the molecula
74             It is the first structure of any multienzyme complex in pyrimidine biosynthesis and is a
75 restingly, GSK3beta can be released from the multienzyme complex in response to PKA phosphorylation o
76 viding biophysical evidence for a diffusible multienzyme complex in the mitochondrial matrix.
77 quivalent domain in a pyruvate dehydrogenase multienzyme complex in which the domain remains of const
78 hesis seems to be spatially regulated by the multienzyme complexes in a cluster-size-dependent manner
79 bition method may be a powerful way to study multienzyme complexes in their physiological context.
80 anched-chain keto acid dehydrogenase (BCKAD) multienzyme complex involved in branched-chain fatty aci
81 n ketoacid dehydrogenase (BCKD) complex is a multienzyme complex involved in the catabolism of branch
82 ofactor required for the function of several multienzyme complexes involved in the oxidative decarbox
83  the Escherichia coli pyruvate dehydrogenase multienzyme complex is an outcome of redistribution of a
84 omponent of the 2-oxoglutarate dehydrogenase multienzyme complex is composed of 24 subunits arranged
85                                         This multienzyme complex is itself regulated through reversib
86 tion are still unknown, but the formation of multienzyme complexes is considered a feasible Golgi pro
87  encoding three alpha-ketoacid dehydrogenase multienzyme complexes (KADHs) that have central metaboli
88 ne-depleted conditions, these enzymes form a multienzyme complex known as the purinosome.
89 l and functional organization of the largest multienzyme complex known.
90 rogenase complex (PDC) is one of the largest multienzyme complexes known and consists of a dodecahedr
91                   The pyruvate dehydrogenase multienzyme complex (Mr of 5-10 million) is assembled ar
92  polypeptide from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus assem
93 omponent of the pyruvate dehydrogenase (PDH) multienzyme complex of Bacillus stearothermophilus has i
94                In the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus, the
95 n interactions in the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus.
96 tyltransferase in the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus.
97 rase component of the pyruvate dehydrogenase multienzyme complex of Escherichia coli is catalysed spe
98 de chain of the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli was over-express
99     Glu139 of the large alpha-subunit of the multienzyme complex of fatty acid oxidation from Escheri
100     His450 of the large alpha-subunit of the multienzyme complex of fatty acid oxidation from Escheri
101 f the branched-chain keto acid dehydrogenase multienzyme complex of Pseudomonas putida.
102                                              Multienzyme complexes of fatty acid oxidation from Esche
103 es of the human 2-oxoglutarate dehydrogenase multienzyme complex (OGDHc), a rate-limiting enzyme in t
104 shown that glycolytic enzymes (GEs) exist as multienzyme complexes on the inner surface of human eryt
105 ic enzymes (GEs) have been shown to exist in multienzyme complexes on the inner surface of the human
106 2) phosphorylates the pyruvate dehydrogenase multienzyme complex (PDC) and thereby controls the rate
107                   The pyruvate dehydrogenase multienzyme complex (PDC) is a key regulatory point in c
108 s the activity of the pyruvate dehydrogenase multienzyme complex (PDC).
109  (E3) subunits of the pyruvate dehydrogenase multienzyme complex (PDH).
110  the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDHc) and its E1 (ThDP-dependent) c
111  the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDHc) by its coenzyme thiamin dipho
112  the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDHc) has been determined at a reso
113  the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDHc) has been determined with phos
114  the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDHc), as a representative of the P
115  the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDHc), binds to the enzyme with gre
116  The Escherichia coli pyruvate dehydrogenase multienzyme complex (PDHc), consisting of multiple copie
117 dihydrolipoyl moieties of four mitochondrial multienzyme complexes: pyruvate dehydrogenase, alpha-ket
118 essential cofactor for several mitochondrial multienzyme complexes required for oxidative metabolism.
119                             Cellulosomes are multienzyme complexes responsible for efficient degradat
120 mpromised tRNAs is unexpectedly rescued by a multienzyme complex shaped by constructive neutral evolu
121 ferential regulation of the sulfur-oxidation multienzyme complex (SOX), which in S. denitrificans is
122           Through anchoring and formation of multienzyme complexes, specific, localized signal transd
123 quired for the function of several essential multienzyme complexes, such as pyruvate dehydrogenase (P
124 H are structurally and catalytically similar multienzyme complexes, suggesting a common mode of inhib
125 acteria, where they are assembled into large multienzyme complexes termed cellulosomes.
126 herichia coli's 2-oxoglutarate dehydrogenase multienzyme complex (termed BBL) with a combination of s
127 icrobes, cellulases are assembled into large multienzymes complexes, termed "cellulosomes," which all
128 th subunits of the fatty acid beta-oxidation multienzyme complex that are normally present in the mat
129 rom Propionibacterium shermanii is a 1.2 MDa multienzyme complex that couples two carboxylation react
130 oduces the prototypical cellulosome, a large multienzyme complex that efficiently hydrolyzes plant ce
131        Tryptophan synthase is an alpha2beta2 multienzyme complex that exhibits coupling of the alpha-
132 al gene copies of the pyruvate dehydrogenase multienzyme complex that have evolved into a pyruvate de
133 Resection is catalyzed by the resectosome, a multienzyme complex that includes bloom syndrome helicas
134                           Component A3a is a multienzyme complex that includes the mcrC gene product,
135 troviral protease is a key enzyme in a viral multienzyme complex that initiates an ordered sequence o
136 dy, we demonstrate that this pathway forms a multienzyme complex that is associated with the nuclear
137 etases examined can be isolated as part of a multienzyme complex that is more stable, and consequentl
138 SAHH associates with DAO as part of a larger multienzyme complex that may function in planta as a nic
139 cetyl-CoA decarbonylase/synthase (ACDS) is a multienzyme complex that plays a central role in energy
140 s still carried out, but in the context of a multienzyme complex that remains structurally intact dur
141 onucleoside triphosphate biosynthesis form a multienzyme complex that we call T4 deoxyribonucleoside
142 component of the three functional classes of multienzyme complexes that catalyze the oxidative decarb
143 drogenase is a common component of mammalian multienzyme complexes that decarboxylate alpha-ketoacids
144                              Proteasomes are multienzyme complexes that maintain protein homeostasis
145 tabolism have long been hypothesized to form multienzyme complexes that regulate glucose flux in livi
146 sembles its catalytic apparatus into a large multienzyme complex, the cellulosome.
147       The reaction is catalyzed by a 0.8 MDa multienzyme complex, the editosome.
148  Evidence has been presented for a metabolic multienzyme complex, the purinosome, that participates i
149 y visualize de novo purine biosynthesis by a multienzyme complex, the purinosome.
150 e assembly of one of Nature's most elaborate multienzyme complexes, the cellulosome, results from the
151 e assembly of one of nature's most elaborate multienzyme complexes, the cellulosome.
152  By linking the MAP3K, MAP2K and MAPK into a multienzyme complex, these MAPK-specific scaffold protei
153  novo purine biosynthetic pathway may form a multienzyme complex to facilitate substrate flux through
154 esized and posttranslationally modified by a multienzyme complex to their biologically active forms.
155 ies (ROS) generation and impaired binding to multienzyme complexes were also addressed according to t
156 ang et al.(1) uncovers the pyrimidinosome, a multienzyme complex where enzymes from different subcell
157 A (PPCA), a serine carboxypeptidase, forms a multienzyme complex with beta-galactosidase and neuramin
158     Lysosomal neuraminidase-1 (NEU1) forms a multienzyme complex with beta-galactosidase and protecti
159        The Escherichia coli degradosome is a multienzyme complex with four major protein components:
160                              NAC assembles a multienzyme complex with MetAP1 and NatA early during tr
161                  The study revealed that the multienzyme complex with the active sites directed towar
162 n-regulated chloroplast protein CP12 forms a multienzyme complex with the Calvin-Benson cycle enzymes
163 he nucleus during S-phase, where they form a multienzyme complex with thymidylate synthase (TYMS) and
164  the Escherichia coli pyruvate dehydrogenase multienzyme complex with Y177A and Y177F substitutions w
165 tly involved in the hydratase catalysis, the multienzyme complexes with either an alpha/Asp69 --> Asn
166 oprotein in at least two major mitochondrial multienzyme complexes would be consistent with a role in

 
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