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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 Carbamoyl-phosphate synthetase 2, aspartate transcarbamoylase, and dihydroorotase (CAD) is a key enz
12 te carbamoyl-phosphate synthetase, aspartate transcarbamoylase, and dihydroorotase (CAD) that catalyz
13 oyl phosphate synthetase (CPSase), aspartate transcarbamoylase, and dihydroorotase activities, cataly
14 ts receptor, three sets of tRNA synthetases, transcarbamoylases, and an internal duplication in carba
15 n, aspartate aminotransferase, and aspartate transcarbamoylase are considered as specific examples.
16 nary structure of Escherichia coli aspartate transcarbamoylase, as monitored by time-resolved small-a
18 bamoyl phosphate synthetase (CPS), aspartate transcarbamoylase (ATC), and dihydroorotase (DHO), are c
21 phate synthetase (CPSase) and both aspartate transcarbamoylase (ATCase) and ornithine transcarbamoyla
25 simplified purification scheme for aspartate transcarbamoylase (ATCase) from wheat-germ is reported,
26 trimeric, catalytic (C) subunit of aspartate transcarbamoylase (ATCase) has impeded understanding of
27 ragine (PALI), of Escherichia coli aspartate transcarbamoylase (ATCase) is reported, as well as struc
28 The A. aeolicus pyrB gene encoding aspartate transcarbamoylase (ATCase) was cloned, overexpressed in
29 of a cooperative Escherichia coli aspartate transcarbamoylase (ATCase) without regulatory subunits.
30 ay structures of Bacillus subtilis aspartate transcarbamoylase (ATCase), an enzyme that catalyzes one
31 to our initial research on E. coli aspartate transcarbamoylase (ATCase), led to the discovery of dist
35 talytic chains of Escherichia coli aspartate transcarbamoylase (ATCase; EC 2.1.3.2) and to select clo
37 roduct release from the R state of aspartate transcarbamoylase (ATCase; EC 2.1.3.2, aspartate carbamo
39 ugh structurally very similar, the aspartate transcarbamoylases (ATCase) of Serratia marcescens and E
40 ugh structurally very similar, the aspartate transcarbamoylases (ATCase) of Serratia marcescens and E
41 10 which is present in prokaryotic ornithine transcarbamoylases but has a C-terminal extension of 10
42 ion of homotropic cooperativity in aspartate transcarbamoylase by the stabilization of the T state of
45 (carbamoyl-phosphate synthetase 2, aspartate transcarbamoylase, dihydroorotase), the enzyme that cata
46 as carbamoyl phosphate synthetase/aspartate transcarbamoylase/dihydroorotase (CAD), a multienzymatic
47 of carbamoyl phosphate synthetase/aspartate transcarbamoylase/dihydroorotase (CAD), a multienzymatic
48 The holoenzyme is trimeric, and as in other transcarbamoylases, each subunit contains an N-terminal
49 ve been used to show that a mutant aspartate transcarbamoylase exists in an intermediate quaternary s
50 reliminary characterization of the aspartate transcarbamoylase from M. jannaschii cell-free extract r
52 etic analysis of the M. jannaschii aspartate transcarbamoylase from the cell-free extract indicates t
53 roline residue in Escherichia coli aspartate transcarbamoylase has been replaced by alanine using sit
54 tic cycle of the allosteric enzyme aspartate transcarbamoylase have been obtained via X-ray crystallo
55 lso a concomitant up-regulation of aspartate transcarbamoylase, however, dihydroorotase and dihydroor
57 ate crystallographic structures of aspartate transcarbamoylase in the presence of the heterotropic ef
60 mutant version of Escherichia coli aspartate transcarbamoylase in which Thr82 in the regulatory chain
62 osteric states of Escherichia coli aspartate transcarbamoylase is governed by specific intra- and int
64 many other proteins, for example, ornithine transcarbamoylase (OTC), a cytosolic homotrimeric enzyme
65 ate transcarbamoylase (ATCase) and ornithine transcarbamoylase (OTCase) from the deep sea hyperthermo
67 stal structure of Escherichia coli ornithine transcarbamoylase (OTCase, EC 2.1.3.3) complexed with th
68 tween the two catalytic trimers of aspartate transcarbamoylase provide a global set of interlocking i
69 of CP to the enzymes aspartate and ornithine transcarbamoylase reduces the rate of thermal decomposit
71 gulatory chain in Escherichia coli aspartate transcarbamoylase resides close to the effector binding
72 cooperativity in Escherichia coli aspartate transcarbamoylase results from the substrate-induced tra
73 he active site of Escherichia coli aspartate transcarbamoylase revealed a specific interaction with t
74 rgininosuccinate synthetase and/or ornithine transcarbamoylase, several types of tumor are auxotrophi
76 In common with other ureotelic ornithine transcarbamoylases, the human enzyme lacks a loop of app
77 to residue 241 in the 240s loop of aspartate transcarbamoylase to monitor changes in conformation by
80 hybrid version of Escherichia coli aspartate transcarbamoylase was investigated in which one catalyti
82 udy a series of hybrid versions of aspartate transcarbamoylase was studied to determine the minimum n
84 catalytic and regulatory chains of aspartate transcarbamoylase were expressed at high levels in Esche
85 ybrid versions of Escherichia coli aspartate transcarbamoylase were studied to determine the influenc
86 he stabilization of the T state of aspartate transcarbamoylase were tested by replacement of Lys-244
87 activity only when complexed with aspartate transcarbamoylase, whereas the E.coli dihydroorotase and
88 tional changes of the 240s loop of aspartate transcarbamoylase, which are tightly correlated with the
89 the structure of Escherichia coli aspartate transcarbamoylase with CTP bound Lys-6 and Glu-62 form a