scholarly journals How evolution shapes enzyme selectivity – lessons from aminoacyl‐tRNA synthetases and other amino acid utilizing enzymes

FEBS Journal ◽  
2020 ◽  
Vol 287 (7) ◽  
pp. 1284-1305 ◽  
Author(s):  
Dan S. Tawfik ◽  
Ita Gruic‐Sovulj
Keyword(s):  
Amino Acid ◽  
Trna Synthetases ◽  
Aminoacyl Trna Synthetases ◽  
Enzyme Selectivity

scholarly journals Aminoacyl-tRNA synthetases catalyze AMP----ADP----ATP exchange reactions, indicating labile covalent enzyme-amino-acid intermediates.

1987 ◽  
Vol 84 (22) ◽  
pp. 7891-7895 ◽  
Author(s):  
E. Rapaport ◽  
P. Remy ◽  
H. Kleinkauf ◽  
J. Vater ◽  
P. C. Zamecnik
Keyword(s):  
Amino Acid ◽  
Exchange Reactions ◽  
Trna Synthetases ◽  
Aminoacyl Trna Synthetases

scholarly journals The structural basis of the genetic code: amino acid recognition by aminoacyl-tRNA synthetases

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Florian Kaiser ◽  
Sarah Krautwurst ◽  
Sebastian Salentin ◽  
V. Joachim Haupt ◽  
Christoph Leberecht ◽  
...  
Keyword(s):  
Amino Acid ◽  
Genetic Code ◽  
Structural Basis ◽  
Trna Synthetases ◽  
Aminoacyl Trna Synthetases ◽  
Amino Acid Recognition

Modification of aminoacyl-tRNA synthetases with pyridoxal-5′-phosphate. Identification of the labeled amino acid residues

Biochimie ◽  
1994 ◽  
Vol 76 (1) ◽  
pp. 33-44 ◽  
Author(s):  
T. Kalogerakos ◽  
C. Hountondji ◽  
P.F. Berne ◽  
S. Dutka ◽  
S. Blanquet
Keyword(s):  
Amino Acid ◽  
Amino Acid Residues ◽  
Trna Synthetases ◽  
Aminoacyl Trna Synthetases

Amino acid biogenesis, evolution of the genetic code and aminoacyl-tRNA synthetases

2004 ◽  
Vol 228 (3) ◽  
pp. 389-396 ◽  
Author(s):  
Liron Klipcan ◽  
Mark Safro
Keyword(s):  
Amino Acid ◽  
Genetic Code ◽  
Trna Synthetases ◽  
Aminoacyl Trna Synthetases

Structure of nondiscriminating glutamyl-tRNA synthetase fromThermotoga maritima

2010 ◽  
Vol 66 (7) ◽  
pp. 813-820 ◽  
Author(s):  
Takuhiro Ito ◽  
Noriko Kiyasu ◽  
Risa Matsunaga ◽  
Seizo Takahashi ◽  
Shigeyuki Yokoyama
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Thermotoga Maritima ◽  
Trna Synthetase ◽  
Characteristic Structure ◽  
Trna Synthetases ◽  
Aminoacyl Trna Synthetases ◽  
Rossmann Fold

Aminoacyl-tRNA synthetases produce aminoacyl-tRNAs from the substrate tRNA and its cognate amino acid with the aid of ATP. Two types of glutamyl-tRNA synthetase (GluRS) have been discovered: discriminating GluRS (D-GluRS) and nondiscriminating GluRS (ND-GluRS). D-GluRS glutamylates tRNAGluonly, while ND-GluRS glutamylates both tRNAGluand tRNAGln. ND-GluRS produces the intermediate Glu-tRNAGln, which is converted to Gln-tRNAGlnby Glu-tRNAGlnamidotransferase. Two GluRS homologues fromThermotoga maritima, TM1875 and TM1351, have been biochemically characterized and it has been clarified that only TM1875 functions as an ND-GluRS. Furthermore, the crystal structure of theT. maritimaND-GluRS, TM1875, was determined in complex with a Glu-AMP analogue at 2.0 Å resolution. TheT. maritimaND-GluRS contains a characteristic structure in the connective-peptide domain, which is inserted into the catalytic Rossmann-fold domain. The glutamylation ability of tRNAGlnby ND-GluRS was measured in the presence of the bacterial Glu-tRNAGlnamidotransferase GatCAB. Interestingly, the glutamylation efficiency was not affected even in the presence of excess GatCAB. Therefore, GluRS avoids competition with GatCAB and glutamylates tRNAGln.

scholarly journals A novel pathway for the conversion of homocysteine to methionine in eukaryotes

1997 ◽  
Vol 328 (1) ◽  
pp. 165-170 ◽  
Author(s):  
M. Celia ANTONIO ◽  
C. Marta NUNES ◽  
Helga REFSUM ◽  
K. Abraham ABRAHAM
Keyword(s):  
Amino Acid ◽  
Crude Extract ◽  
Trna Synthetase ◽  
Synthetase Activity ◽  
Enzyme Complex ◽  
Homocysteine Thiolactone ◽  
Initiator Trna ◽  
Trna Synthetases ◽  
Aminoacyl Trna Synthetases ◽  
Reticulocyte Lysates

Activation of amino acid homocysteine was compared with that of methionine in rabbit crude liver extracts and purified multi-enzyme complex of aminoacyl-tRNA synthetases. Activation was studied by measuring the incorporation of radioactive amino acid into unlabelled trichloroacetic-acid insoluble materials in the absence of protein synthesis. Homocysteine synthetase activity was found in the crude extract and in the purified multi-enzyme complex of aminoacyl-tRNA synthetases. On a molar basis, the activation of methionine by the crude extract was five times higher than the activation of homocysteine. There was a partial loss of Hcy-tRNA synthetase activity in the purified multi-enzyme complex. Preliminary reconstitution experiments indicated a requirement for an additional factor for Hcy-tRNA synthetase activity. TLC of the amino acid released from tRNA charged with [14C]homocysteine, revealed radioactivity in homocysteine, methionine and homocysteine thiolactone, indicating a conversion of tRNA-attached homocysteine to methionine. Total tRNA was separated on a benzoylated cellulose column into a fraction enriched in initiator tRNA and a methionine-accepting, but initiator tRNA-deficient, fraction. Homocysteine-accepting activity was present only in the initiator tRNA-enriched fraction. Based on the above data we propose that homocysteine activation in reticulocyte lysates, reported previously, also occurs in liver. Activated homocysteine is attached to initiator tRNA and then converted to methionine by a methylating enzyme. In the absence of methylation, tRNA-attached homocysteine is hydrolysed to produce homocysteine thiolactone.

scholarly journals tRNA and amino acid recognition by class II aminoacyl-tRNA synthetases

1996 ◽  
Vol 52 (a1) ◽  
pp. C164-C164
Author(s):  
S. Cusack ◽  
A. Åberg ◽  
A. Yaremchuk ◽  
C. Berthet ◽  
L. Seignovert ◽  
...  
Keyword(s):  
Amino Acid ◽  
Class Ii ◽  
Trna Synthetases ◽  
Aminoacyl Trna Synthetases ◽  
Amino Acid Recognition

Non‐canonical amino acid substrates of E. coli aminoacyl‐tRNA synthetases

ChemBioChem ◽  
2021 ◽  
Author(s):  
Matthew Charles Tomandl Hartman
Keyword(s):  
Amino Acid ◽  
Trna Synthetases ◽  
E Coli ◽  
Aminoacyl Trna Synthetases ◽  
Canonical Amino Acid
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