Histidyl-tRNA synthetase urzymes: Class I and II aminoacyl tRNA synthetase urzymes have comparable catalytic activities for cognate amino acid activation (Q34695757)

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English	Histidyl-tRNA synthetase urzymes: Class I and II aminoacyl tRNA synthetase urzymes have comparable catalytic activities for cognate amino acid activation	scientific article

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

4 August 2017

Histidyl-tRNA synthetase urzymes: Class I and II aminoacyl tRNA synthetase urzymes have comparable catalytic activities for cognate amino acid activation (English)

1 reference

Europe PubMed Central

PubMed publication ID

4 August 2017

author name string

Li Li

1

1 reference

Europe PubMed Central

PubMed publication ID

4 August 2017

Violetta Weinreb

2

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Europe PubMed Central

PubMed publication ID

4 August 2017

Christopher Francklyn

3

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Europe PubMed Central

PubMed publication ID

4 August 2017

Charles W Carter

4

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Europe PubMed Central

PubMed publication ID

4 August 2017

language of work or name

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publication date

26 January 2011

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Europe PubMed Central

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4 August 2017

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

4 August 2017

286

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Europe PubMed Central

PubMed publication ID

4 August 2017

12

1 reference

Europe PubMed Central

PubMed publication ID

4 August 2017

10387-10395

1 reference

Europe PubMed Central

PubMed publication ID

4 August 2017

Tryptophanyl-tRNA synthetase Urzyme: a model to recapitulate molecular evolution and investigate intramolecular complementation

1 reference

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Cofactor binding and enzymatic activity in an unevolved superfamily of de novo designed 4-helix bundle proteins

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Methods for kinetic and thermodynamic analysis of aminoacyl-tRNA synthetases

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Kinetic discrimination of tRNA identity by the conserved motif 2 loop of a class II aminoacyl-tRNA synthetase

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The ribosome as an entropy trap

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The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase

1 reference

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Seryl-tRNA synthetase from Escherichia coli: implication of its N-terminal domain in aminoacylation activity and specificity

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Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate

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Two types of aminoacyl-tRNA synthetases could be originally encoded by complementary strands of the same nucleic acid

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1 reference

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1 reference

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inferred from PubMed ID database lookup

Identifiers

10.1074/JBC.M110.198929

1 reference

Europe PubMed Central

PubMed publication ID

4 August 2017

Internet Archive ID

pubmed-PMC3060492

0 references

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

4 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

4 August 2017

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