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1 oteins copurify with the NRPSs and influence amino acid activation.
2 aRSs, the rate-determining step for ThrRS is amino acid activation.
3 d decreased tRNA-mediated kinetic control of amino acid activation.
4  located approximately 30 A from the site of amino acid activation.
5 or tRNA aminoacylation but played no role in amino acid activation.
6 site that destroys (by hydrolysis) errors of amino acid activation.
7 nctionally separates amino acid editing from amino acid activation.
8 in the valine enzyme which severely affected amino acid activation.
9 ured by these assays: active site titration, amino acid activation, aminoacylation, and posttransfer
10  discrimination occurs at two sites: one for amino acid activation and aminoacylation and one for edi
11  from six auxotrophic strains for changes in amino acid activation and aminoacylation.
12 crete sites in isoleucyl-tRNA synthetase for amino acid activation and editing are about 25 A apart.
13 t ATP-[(32)P]PP(i) exchange assay to monitor amino acid activation and electrospray ionization-Fourie
14 we found that BMAA inhibits both the cognate amino acid activation and the editing functions of AlaRS
15 ic profiles for Class I and II aaRSs in both amino acid activation and tRNA acylation, over a time pe
16 te the capacity of the N-terminal domain for amino acid activation and tRNA aminoacylation through a
17 thetase (ERS) region of EPRS is defective in amino acid activation and tRNA(Glu) charging.
18 t this domain interacts with the tRNA during amino acid activation and/or tRNA aminoacylation.
19                                Errors during amino-acid activation and tRNA esterification are correc
20 ing domain that is distinct from the site of amino acid activation, and the mechanism is believed to
21 icant transition-state stabilization of both amino acid activation, and tRNA acylation.
22     Michaelis-Menten kinetic parameters from amino acid activation assays showed that, compared with
23 sine analogs and testing their reactivity in amino acid activation assays.
24              Transfer RNA can play a role in amino acid activation by aminoacyl-tRNA synthetases.
25                                 Catalysis of amino acid activation by Bacillus stearothermophilus try
26            Although the structural basis for amino acid activation by class I tRNA synthetases is kno
27                Such data are of interest for amino acid activation by class Ic aminoacyl-tRNA synthet
28 upports a biosynthetic model in which in cis amino acid activation competes with in trans activation
29  a catalytically competent configuration for amino acid activation destabilizes the enzyme structure
30 e used Rap1(AS) to map and characterize a 41-amino acid activation domain (AD) within the Rap1 C term
31                    However, deletion of a 14 amino acid activation domain encompassing S742 and S747
32 duced by phosphorylation or deletion of a 14-amino-acid activation domain (AD) located on the linker
33 ning the HSF 1 regulatory domain and this 20-amino-acid activation domain is repressed at the control
34 units have a 310-360-residue insert in their amino acid activation domains that look like defective m
35 ion at serine codons, following a screen for amino acid activation in ATP/PP(i) exchange assays, we o
36               To examine the role of tRNA in amino acid activation more closely, several assays emplo
37           The substitutions affected neither amino acid activation nor aminoacylation, with the cogna
38 n class II histidyl-tRNA synthetase (HisRS), amino acid activation occurs at different rates in the t
39 nd that, although both Rag and Vps34 mediate amino acid activation of mTORC1 in C2C12 myoblasts, they
40 n parallel to, the Rag pathway in regulating amino acid activation of mTORC1.
41 vate PLD1 and that PLD1 is indispensable for amino acid activation of mTORC1.
42  NRPS domains catalyze standard chemistry of amino acid activation, peptide bond formation, and produ
43 jor portion of the selectivity arises in the amino acid activation portion of the reaction, whereas t
44 diting active site that is separate from the amino acid activation site providing two steps or "sieve
45 arly all mutants preferentially affected the amino acid activation step, with only a modest effect on
46 rved role of RNA as a cofactor in optimizing amino acid activation suggests that the tRNAGln-GlnRS co
47 he ATP-PP(i) exchange reaction revealed that amino acid activation, the first reaction step, differs
48                              ATP dependence, amino acid activation, the ribosome as the site of polyp
49   The emergence of polypeptide catalysts for amino acid activation, the slowest step in protein synth
50 overall rate of aminoacylation is limited by amino acid activation to a rate of 3 s(-)(1).
51  discrimination of valine from isoleucine by amino acid activation was functionally independent of di