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1 ng the homotropic cooperativity in aspartate transcarbamoylase.
2 has in the functional mechanism of aspartate transcarbamoylase.
3 eric structure of Escherichia coli aspartate transcarbamoylase.
4 s for the allosteric transition of aspartate transcarbamoylase.
5 anisms of allosteric regulation in aspartate transcarbamoylase.
6 y high-affinity R-state of E. coli aspartate transcarbamoylase.
7 ropic activation and inhibition of aspartate transcarbamoylase.
8 bolite is bound to the active sites of these transcarbamoylases.
9 he quaternary T to R transition of aspartate transcarbamoylase and functionally induced homotropic co
10 pic and heterotropic properties of aspartate transcarbamoylase and that direct pathways for transmiss
11 oyl phosphate synthetase (CPSase), aspartate transcarbamoylase, and dihydroorotase activities, cataly
12 ts receptor, three sets of tRNA synthetases, transcarbamoylases, and an internal duplication in carba
13 n, aspartate aminotransferase, and aspartate transcarbamoylase are considered as specific examples.
14 nary structure of Escherichia coli aspartate transcarbamoylase, as monitored by time-resolved small-a
15 bamoyl phosphate synthetase (CPS), aspartate transcarbamoylase (ATC), and dihydroorotase (DHO), are c
18 phate synthetase (CPSase) and both aspartate transcarbamoylase (ATCase) and ornithine transcarbamoyla
22 simplified purification scheme for aspartate transcarbamoylase (ATCase) from wheat-germ is reported,
23 trimeric, catalytic (C) subunit of aspartate transcarbamoylase (ATCase) has impeded understanding of
24 ragine (PALI), of Escherichia coli aspartate transcarbamoylase (ATCase) is reported, as well as struc
25 The A. aeolicus pyrB gene encoding aspartate transcarbamoylase (ATCase) was cloned, overexpressed in
26 of a cooperative Escherichia coli aspartate transcarbamoylase (ATCase) without regulatory subunits.
27 ay structures of Bacillus subtilis aspartate transcarbamoylase (ATCase), an enzyme that catalyzes one
28 to our initial research on E. coli aspartate transcarbamoylase (ATCase), led to the discovery of dist
32 talytic chains of Escherichia coli aspartate transcarbamoylase (ATCase; EC 2.1.3.2) and to select clo
34 roduct release from the R state of aspartate transcarbamoylase (ATCase; EC 2.1.3.2, aspartate carbamo
36 ugh structurally very similar, the aspartate transcarbamoylases (ATCase) of Serratia marcescens and E
37 ugh structurally very similar, the aspartate transcarbamoylases (ATCase) of Serratia marcescens and E
38 10 which is present in prokaryotic ornithine transcarbamoylases but has a C-terminal extension of 10
39 ion of homotropic cooperativity in aspartate transcarbamoylase by the stabilization of the T state of
42 (carbamoyl-phosphate synthetase 2, aspartate transcarbamoylase, dihydroorotase), the enzyme that cata
43 as carbamoyl phosphate synthetase/aspartate transcarbamoylase/dihydroorotase (CAD), a multienzymatic
44 of carbamoyl phosphate synthetase/aspartate transcarbamoylase/dihydroorotase (CAD), a multienzymatic
45 The holoenzyme is trimeric, and as in other transcarbamoylases, each subunit contains an N-terminal
46 ve been used to show that a mutant aspartate transcarbamoylase exists in an intermediate quaternary s
47 reliminary characterization of the aspartate transcarbamoylase from M. jannaschii cell-free extract r
49 etic analysis of the M. jannaschii aspartate transcarbamoylase from the cell-free extract indicates t
50 roline residue in Escherichia coli aspartate transcarbamoylase has been replaced by alanine using sit
51 tic cycle of the allosteric enzyme aspartate transcarbamoylase have been obtained via X-ray crystallo
52 lso a concomitant up-regulation of aspartate transcarbamoylase, however, dihydroorotase and dihydroor
54 ate crystallographic structures of aspartate transcarbamoylase in the presence of the heterotropic ef
57 mutant version of Escherichia coli aspartate transcarbamoylase in which Thr82 in the regulatory chain
59 osteric states of Escherichia coli aspartate transcarbamoylase is governed by specific intra- and int
61 many other proteins, for example, ornithine transcarbamoylase (OTC), a cytosolic homotrimeric enzyme
62 ate transcarbamoylase (ATCase) and ornithine transcarbamoylase (OTCase) from the deep sea hyperthermo
64 stal structure of Escherichia coli ornithine transcarbamoylase (OTCase, EC 2.1.3.3) complexed with th
65 tween the two catalytic trimers of aspartate transcarbamoylase provide a global set of interlocking i
66 of CP to the enzymes aspartate and ornithine transcarbamoylase reduces the rate of thermal decomposit
68 gulatory chain in Escherichia coli aspartate transcarbamoylase resides close to the effector binding
69 cooperativity in Escherichia coli aspartate transcarbamoylase results from the substrate-induced tra
70 he active site of Escherichia coli aspartate transcarbamoylase revealed a specific interaction with t
71 rgininosuccinate synthetase and/or ornithine transcarbamoylase, several types of tumor are auxotrophi
73 In common with other ureotelic ornithine transcarbamoylases, the human enzyme lacks a loop of app
74 to residue 241 in the 240s loop of aspartate transcarbamoylase to monitor changes in conformation by
77 hybrid version of Escherichia coli aspartate transcarbamoylase was investigated in which one catalyti
79 udy a series of hybrid versions of aspartate transcarbamoylase was studied to determine the minimum n
81 catalytic and regulatory chains of aspartate transcarbamoylase were expressed at high levels in Esche
82 ybrid versions of Escherichia coli aspartate transcarbamoylase were studied to determine the influenc
83 he stabilization of the T state of aspartate transcarbamoylase were tested by replacement of Lys-244
84 activity only when complexed with aspartate transcarbamoylase, whereas the E.coli dihydroorotase and
85 tional changes of the 240s loop of aspartate transcarbamoylase, which are tightly correlated with the
86 the structure of Escherichia coli aspartate transcarbamoylase with CTP bound Lys-6 and Glu-62 form a
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