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Ligand tRNA

Basic Ligand Information

Molecular Structure

Related pathways

Show all BRENDA pathways known for tRNA

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Natural Substrate (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.7.7.87

L-threonylcarbamoyl-AMP + tRNA = t6A37-tRNA

721678

-

4.6.1.16

tRNA + H2O = ?

699518, 682189

-

4.6.1.16

tRNA + H2O = tRNA containing 5'hydroxy and 2',3'-cyclic phosphate termini

697209

-

4.6.1.16

2 entries

4.6.1.18

tRNA + H2O = ?

771017

-

In Vivo Product in Enzyme-catalyzed Reactions (14 results)

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Show Natural Product (14 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.2.12

peptidyl-tRNA1 + alpha-aminoacyl-tRNA2 = tRNA1 + peptidyl-amino-tRNA2

487795, 487796, 487797, 487798, 487800, 487802, 487803

-

2.3.2.12

peptidyl-tRNA1 + aminoacyl-tRNA2 = tRNA1 + peptidyl(aminoacyl-tRNA2)

-

-

2.3.2.12

2 entries

2.3.2.6

L-phenylalanyl-tRNA + protein = tRNA + L-phenylalanyl-protein

-

-

2.7.7.56

tRNAn+1 + phosphate = tRNA + a nucleoside diphosphate

643526, 643522, 643523, 643524, 643528, 643525

-

3.1.1.29

N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA

653271, 650249, 648110, 648112, 648116, 653741, 653153, -

-

3.1.1.29

peptidyl-tRNA + H2O = peptide + tRNA

-

-

3.1.1.29

peptidyl-tRNAL + H2O = peptide + tRNA

-

-

3.1.1.96

D-aminoacyl-tRNA + H2O = D-amino acid + tRNA

-

-

3.1.1.96

D-Tyr-tRNA + H2O = D-Tyr + tRNA

-

-

3.1.1.29

3 entries

3.1.1.96

2 entries

3.1.13.5

tRNA containing extra residues at the 3'-terminus = 5'-mononucleotide + tRNA

-

-

3.1.26.5

pre-tRNA + H2O = tRNA

-

-

3.1.26.5

pre-tRNA + H2O = tRNA + 5'-oligoribonucleotide

-

-

3.1.26.7

pre-tRNA + H2O = tRNA + pre-part nucleotides

-

-

3.1.26.7

tRNA precursor + H2O = tRNA + 5'-terminal oligonucleotide

-

-

3.1.26.5

2 entries

3.1.26.7

2 entries

Substrate in Enzyme-catalyzed Reactions (20 results)

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Show Substrate (20 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.1.1.34

S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + 2-methylthio N6(gamma,gamma,dimethylallyl)adenosine in tRNA

637156

-

2.1.1.34

S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing 2'-O-methylguanine

662141, 663410, 674692, 676232

-

2.4.2.29

pre-queuine 0 + tRNA guanine = guanine + tRNA pre-queuine 0

688390

-

2.4.2.29

7-aminomethyl-7-carbaguanine + [tRNA]-guanine = guanine + [tRNA]-pre Q1

702263, 703226

-

2.1.1.34

2 entries

2.4.2.29

2 entries

2.7.7.87

L-threonylcarbamoyl-AMP + tRNA = t6A37-tRNA

721678

-

2.8.1.4

L-cysteine + tRNA = ?

643807

-

3.1.13.1

tRNA + H2O = ?

134050, 134062, 134051

-

3.1.13.1

tRNA = ?

657199

-

3.1.13.1

2 entries

3.1.16.1

tRNA + H2O = tRNA fragments + nucleoside 3'-phosphates

134137, 134148, 134145, 134149, 134147

-

3.1.26.3

tRNA + H2O = 5'-phosphooligonucleotides

134349, 134339, 134360, 134356, 134342, 134336

-

3.1.26.5

tRNA + H2O = ?

680594

-

3.1.30.1

tRNA + H2O = 5'-phosphomononucleotides + 5'-phosphooligonucleotides

134969, 134985, 134965

-

3.2.2.22

tRNA + H2O = ?

666621

-

4.6.1.16

tRNA + H2O = ?

699518, 682189, 697170

-

4.6.1.16

tRNA + H2O = tRNA containing 5'hydroxy and 2',3'-cyclic phosphate termini

697209

-

4.6.1.18

tRNA + H2O = 3'-phosphomononucleotides + 3'-phosphooligonucleotides

134557, 134556, 666332, 663854, 681841

-

4.6.1.18

tRNA + H2O = ?

680679, 771017

-

4.6.1.16

2 entries

4.6.1.18

2 entries

6.1.1.15

ATP + L-cysteine + tRNA = AMP + diphosphate + L-cysteinyl-tRNA

728126, 653662, 727456, 650058

-

6.1.1.7

ATP + L-alanine + tRNA = ?

514

-

6.1.1.B3

ATP + L-glutamate + tRNA = AMP + diphosphate + L-glutamyl-tRNA

722945

-

Product in Enzyme-catalyzed Reactions (110 results)

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Show Product (110 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.11.33

tRNA-1-methylguanine + 2-oxoglutarate + O2 = tRNA-guanine + formaldehyde + succinate + CO2

-

-

2.3.2.12

acetylphenylalanyl-tRNA + puromycin = acetylphenylalanyl-puromycin + tRNA

-

-

2.3.2.12

AcPhe-tRNA + pCpCp-puromycin = tRNA + AcPhe-pCpCp-puromycin

-

-

2.3.2.12

AcPhe-tRNA + puromycin = tRNA + AcPhe-puromycin

487795, 487805, 487807, 487815, 487799, 487817, 487818, 487811, 487813, 487814, 487798, 487806, 487808, 487809, 487810, 487812, -

-

2.3.2.12

formyl-Met-tRNA + puromycin = tRNA + formyl-Met-puromycin

-

-

2.3.2.12

formylmethionyl-tRNA + alpha-hydroxy-puromycin = tRNA + formylmethionyl-alpha-hydroxy-puromycin

487800

-

2.3.2.12

formylmethionyl-tRNA + puromycin = tRNA + formylmethionyl-puromycin

487800, 487809

-

2.3.2.12

L-Phe-tRNA + puromycin = tRNA + L-Phe-puromycin

-

-

2.3.2.12

Met-tRNA + cytidine-cytidine-hydroxypuromycin = tRNA + Met-cytidine-cytidine-hydroxypuromycin

-

-

2.3.2.12

Met-tRNA + cytidine-hydroxypuromycin = tRNA + Met-cytidine-hydroxypuromycin

-

-

2.3.2.12

Met-tRNA + cytidine-puromycin = tRNA + Met-cytidine-puromycin

-

-

2.3.2.12

Met-tRNA + puromycin = tRNA + Met-puromycin

-

-

2.3.2.12

N-AcMet-tRNA + puromycin = tRNA + N-AcMet-puromycin

487816

-

2.3.2.12

N-AcPhe-tRNA + puromycin = tRNA + N-AcPhe-puromycin

487803, -

-

2.3.2.12

phenylalanyl-tRNA + puromycin = tRNA + phenylalanyl-puromycin

487802

-

2.3.2.12

polylysyl-tRNA + puromycin = tRNA + polylysyl-puromycin

487797, 487798

-

2.3.2.12

polyphenylalanyl-tRNA + puromycin = tRNA + polyphenylalanyl-puromycin

487796

-

2.3.2.12

peptidyl-tRNA1 + alpha-aminoacyl-tRNA2 = tRNA1 + peptidyl-amino-tRNA2

487795, 487796, 487797, 487798, 487800, 487802, 487803, -

-

2.3.2.12

peptidyl-tRNA1 + aminoacyl-tRNA2 = tRNA1 + peptidyl(aminoacyl-tRNA2)

-

-

2.3.2.12

peptidyl-tRNA1 + aminoacyl-tRNA2 = tRNA1 + peptidyl-aminoacyl-tRNA2

-

-

2.3.2.12

19 entries

2.3.2.17

N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine + 2 glycyl-tRNA = N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-triglycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine + 2 tRNA

-

-

2.3.2.18

N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-triglycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine + 2 glycyl-tRNA = N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-pentaglycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine + 2 tRNA

-

-

2.3.2.6

L-phenylalanyl-tRNA + REPGLCTWQSLR = t-RNA + FREPGLCTWQSLR

-

-

2.3.2.6

1-naphthylalanyl-tRNA + L-Lys-SoCBM13 = 1-naphthylalanyl-L-Lys-SoCBM13 + tRNA

-

-

2.3.2.6

2-naphthylalanyl-tRNA + L-Lys-SoCBM13 = 2-naphthylalanyl-L-Lys-SoCBM13 + tRNA

-

-

2.3.2.6

3-nitrotyrosyl-tRNA + L-Arg-casein = 3-nitrotyrosyl-L-Arg-casein + tRNA

-

-

2.3.2.6

3-nitrotyrosyl-tRNA + L-Lys-glutathione S-transferase = 3-nitrotyrosyl-L-Lys-glutathione S-transferase + tRNA

-

-

2.3.2.6

3-nitrotyrosyl-tRNA + L-Lys-SoCBM13 = 3-nitrotyrosyl-L-Lys-SoCBM13 + tRNA

-

-

2.3.2.6

L-leucyl-tRNA + REPGLCTWQSLR = tRNA + LREPGLCTWQSLR

-

-

2.3.2.6

L-methionyl-tRNA + acceptor protein = tRNA + L-methionyl-protein

-

-

2.3.2.6

L-phenylalanyl + acceptor protein = tRNA + L-phenylalanyl-protein

-

-

2.3.2.6

L-phenylalanyl-tRNA + acceptor protein = tRNA + L-phenylalanyl-protein

-

-

2.3.2.6

L-phenylalanyl-tRNA + KAC-acrydonylalanine = tRNA + L-phenylalanyl-KAC-acrydonylalanine

-

-

2.3.2.6

L-phenylalanyl-tRNA + KPC-acrydonylalanine = tRNA + L-phenylalanyl-KPC-acrydonylalanine

-

-

2.3.2.6

L-phenylalanyl-tRNA + KQC-acrydonylalanine = tRNA + L-phenylalanyl-KQC-acrydonylalanine

-

-

2.3.2.6

L-phenylalanyl-tRNA + Lys-Ala-Ala = Phe-Lys-Ala-Ala + tRNA

488003

-

2.3.2.6

L-phenylalanyl-tRNA + protein = tRNA + L-phenylalanyl-protein

-

-

2.3.2.6

L-phenylalanyl-tRNA + putrescine aminotransferase = tRNA + L-phenylalanyl-putrescine aminotransferase

-

-

2.3.2.6

L-phenylalanyl-tRNA + REPGLCTWQSLR = tRNA + FREPGLCTWQSLR

-

-

2.3.2.6

L-phenylalanyl-tRNA + RGPCRAFI = tRNA + L-phenylalanyl-RGPCRAFI

-

-

2.3.2.6

L-Trp + acceptor protein = tRNA + L-Trp

-

-

2.3.2.6

O-(2-fluoroethyl)- L-tyrosyl-tRNA + acceptor protein = tRNA + O-(2-fluoroethyl)-L-tyrosyl-protein

-

-

2.3.2.6

O-(2-fluoromethyl)-L-tyrosinyl-tRNA + N-terminal L-leucyl-[protein] = tRNA + N-terminal O-(2-fluoromethyl)-L-tyrosinyl-L-leucyl-[protein]

-

-

2.3.2.6

21 entries

2.3.2.8

L-arginyl-tRNA + L-Asp-beta-galactosidase = tRNA + L-arginyl-L-Asp-beta-galactosidase

-

-

2.3.2.B1

ditrans,ocatacis-undecaprenyl diphosphoryl (GlcNAc-beta-(1->4))MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine + L-Ala-tRNa = ditrans,ocatacis-undecaprenyl diphosphoryl (GlcNAc-beta-(1->4))MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-alanyl)-D-alanyl-D-alanine + tRNA

-

-

2.3.2.B1

ditrans,ocatacis-undecaprenyl diphosphoryl MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine + L-alanyl-tRNA = ? + tRNA

-

-

2.3.2.B1

ditrans,ocatacis-undecaprenyl diphosphoryl MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanyl-L-alanyl-gamma-D-glutamyl-L-lysine + alanyl-tRNA = ? + tRNA

-

-

2.3.2.B1

UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine + L-alanyl-tRNA = UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-alanyl)-D-alanyl-D-alanine + tRNA

-

-

2.3.2.B1

UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine + L-seryl-tRNA = UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-seryl)-D-alanyl-D-alanine + tRNA

-

-

2.3.2.B14

AcPhe-tRNA + puromycin = tRNA + AcPhe-puromycin

-

-

2.3.2.B14

peptidyl-tRNA1 + alpha-aminoacyl-tRNA2 = tRNA1 + peptidyl-amino-tRNA2

-

-

2.3.2.B2

UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-alanyl)-D-alanyl-D-alanine + L-alanyl-tRNA = UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-alanyl-L-alanyl)-D-alanyl-D-alanine + tRNA

-

-

2.3.2.B2

UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-seryl)-D-alanyl-D-alanine + L-alanyl-tRNA = UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-seryll-L-alanyl)-D-alanyl-D-alanine + tRNA

-

-

2.3.2.B1

5 entries

2.3.2.B14

2 entries

2.3.2.B2

2 entries

2.7.7.56

tRNAn+1 + phosphate = tRNA + a nucleoside diphosphate

643522, 643528, 643525, 643526, 643523, 643524

-

3.1.1.29

acetyl-histidine-tRNA + H2O = acetyl-histidine + tRNA

648112

-

3.1.1.29

Ala-tRNA + H2O = Ala + tRNA

-

-

3.1.1.29

D-tyrosine-tRNA + H2O = D-tyrosine + tRNA

648112

-

3.1.1.29

diacetyl-Lys-tRNA + H2O = diacetyl-Lys + tRNA

-

-

3.1.1.29

diacetyl-Lys-tRNALys + H2O = diacetyl-Lys + tRNA

-

-

3.1.1.29

diacetyl-lysine-tRNA + H2O = diacetyl-lysine + tRNA

648110, 648112, 648116, 653741

-

3.1.1.29

Flag-tagged CRPNSKn-tRNA + H2O = Flag-tagged CRPNSKn + tRNA

-

-

3.1.1.29

formyl-methionine-tRNA + H2O = formyl-methionine + tRNA

648112

-

3.1.1.29

formyl-methioninyl-tRNA + H2O = formyl-methionine + tRNA

-

-

3.1.1.29

Glu-tRNA + H2O = Glu + tRNA

-

-

3.1.1.29

Gly-tRNA + H2O = Gly + tRNA

-

-

3.1.1.29

Leu-tRNA + H2O = Leu + tRNA

-

-

3.1.1.29

Lys-tRNA + H2O = Lys + tRNA

-

-

3.1.1.29

Met-tRNA + H2O = Met + tRNA

-

-

3.1.1.29

N-acetyl-Ala-tRNA + H2O = N-acetyl-Ala + tRNA

-

-

3.1.1.29

N-acetyl-Glu-tRNA + H2O = N-acetyl-Glu + tRNA

-

-

3.1.1.29

N-acetyl-His-tRNA + H2O = N-acetyl-His + tRNA

-

-

3.1.1.29

N-acetyl-Leu-Gly-tRNA + H2O = N-acetyl-Leu-Gly + tRNA

-

-

3.1.1.29

N-acetyl-Leu-tRNA + H2O = N-acetyl-Leu + tRNA

-

-

3.1.1.29

N-acetyl-Lys-tRNA + H2O = N-acetyl-Lys + tRNA

-

-

3.1.1.29

N-acetyl-Met-tRNA + H2O = N-acetyl-Met + tRNA

-

-

3.1.1.29

N-acetyl-Phe-Phe-tRNA + H2O = N-acetyl-Phe-Phe + tRNA

-

-

3.1.1.29

N-acetyl-Phe-tRNA + H2O = N-acetyl-L-Phe + tRNA

648116

-

3.1.1.29

N-acetyl-Phe-tRNA + H2O = N-acetyl-Phe + tRNA

-

-

3.1.1.29

N-acetyl-Phe-Val-tRNA + H2O = N-acetyl-Phe-Val + tRNA

-

-

3.1.1.29

N-acetyl-Ser-tRNA + H2O = N-acetyl-Ser + tRNA

-

-

3.1.1.29

N-acetyl-Trp-tRNA + H2O = N-acetyl-Trp + tRNA

-

-

3.1.1.29

N-acetyl-Tyr-tRNA + H2O = N-acetyl-Tyr + tRNA

-

-

3.1.1.29

N-acetyl-Val-tRNA + H2O = N-acetyl-Val + tRNA

-

-

3.1.1.29

N-benzoyl-Gly-Gly-Phe-tRNA + H2O = N-benzoyl-Gly-Gly-Phe + tRNA

-

-

3.1.1.29

N-benzoyl-Gly-GlyGly-Phe-tRNA + H2O = N-benzoyl-Gly-Gly-Gly-Phe + tRNA

-

-

3.1.1.29

N-carbobenzyloxy-Phe-tRNA + H2O = N-carbobenzyloxy-Phe + tRNA

-

-

3.1.1.29

N-formyl-Val-tRNA + H2O = N-formyl-Val + tRNA

-

-

3.1.1.29

N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA

653271, 650249, 653153, 648110, 648112, 648116, 653741, -

-

3.1.1.29

oligolysyl-tRNA + H2O = oligo-Lys + tRNA

-

-

3.1.1.29

Oregon Green-methionine-tRNA + H2O = Oregon Green-methionine + tRNA

650249

-

3.1.1.29

peptidyl-tRNA + H2O = peptide + tRNA

-

-

3.1.1.29

peptidyl-tRNAL + H2O = peptide + tRNA

-

-

3.1.1.29

Phe-Phe-tRNA + H2O = Phe-Phe + tRNA

-

-

3.1.1.29

Phe-tRNA + H2O = Phe + tRNA

-

-

3.1.1.29

phenyllactyl-Phe-tRNA + H2O = phenyllactyl-Phe + tRNA

-

-

3.1.1.29

poly-Val-tRNA + H2O = poly-Val + tRNA

-

-

3.1.1.29

Ser-tRNA + H2O = Ser + tRNA

-

-

3.1.1.29

Tyr-tRNA + H2O = Tyr + tRNA

-

-

3.1.1.29

Val-tRNA + H2O = Val + tRNA

-

-

3.1.1.96

D-aminoacyl-tRNA + H2O = D-amino acid + tRNA

-

-

3.1.1.96

D-Tyr-tRNA + H2O = D-Tyr + tRNA

-

-

3.1.1.29

45 entries

3.1.1.96

2 entries

3.1.13.5

tRNA containing extra residues at the 3'-terminus = 5'-mononucleotide + tRNA

-

-

3.1.26.11

precursor tRNATyr + H2O = tRNA + 3' trailer

-

-

3.1.26.5

pre-tRNA + H2O = tRNA

-

-

3.1.26.5

pre-tRNA + H2O = tRNA + 5' leader of tRNA

-

-

3.1.26.5

pre-tRNA + H2O = tRNA + 5'-oligoribonucleotide

-

-

3.1.26.5

pre-tRNA + H2O = tRNA + RNA sequence

-

-

3.1.26.5

pre-tRNA precursor + H2O = tRNA + 5'-oligoribonucleotide

134427, -

-

3.1.26.7

pre-tRNA + H2O = tRNA + pre-part nucleotides

-

-

3.1.26.7

tRNA precursor + H2O = tRNA + 5'-terminal oligonucleotide

-

-

3.1.26.5

5 entries

3.1.26.7

2 entries

Activator in Enzyme-catalyzed Reactions (6 results)

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Show Activating Compound (6 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.7.6.5

uncharged or charged, stimulation, level of stimulation is greater in presence of RNA and poly(U) together than with either RNA alone

642775

-

3.4.21.B1

-

772346

-

5.6.2.6

-

693208

-

5.6.2.6

stimulates

693208

-

5.6.2.6

2 entries

6.1.1.15

stimulates l-cysteine activation 2-3fold

651296

-

6.1.1.17

GluRS is one of the aminoacyl-tRNA synthetases that require the cognate tRNA for specific amino acid recognition and activation, tRNA serves as the enzyme activator in the first step, and as the substrate in the second step of aminoacylation, overview, On the other hand, the main chain of the glutamate is immature glutamate-binding site in the absence of tRNA

677157

-

Inhibitor in Enzyme-catalyzed Reactions (17 results)

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Show Inhibitors (17 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.7.7.84

-

721471

-

3.1.1.29

uncharged yeast tRNA, competitive

648107

-

3.1.1.29

unfractionated Escherichia coli tRNA; unfractionated from Escherichia coli

648112

-

3.1.1.29

2 entries

3.1.21.7

half-maximal inhibition rate at 0.08 mM

288788

-

3.1.22.1

from E. coli, little effect on activity

134292

-

3.1.22.1

specific competitive inhibition

134308

-

3.1.22.1

2 entries

3.1.26.3

inhibits enzyme activity and inhibition by ethidium bromide

656877

-

3.1.26.5

-

134415, 134430, 134435

-

3.1.26.5

bulk tRNA

134445

-

3.1.26.5

mature tRNA is a competitive inhibitor of pre-tRNA cleavage

134415

-

3.1.26.5

3 entries

3.1.4.16

-

652555

-

3.1.4.37

10 nM, strong competitive inhibition of 2',3'-cyclic phosphodiesterase activity, inhibition is abolished by addition of Mg2+, Mn2+ or Ca2+, but not of Ni2+

652555

-

4.2.1.70

wild-type RNA, 50% inhibition at a concentration of 0.005 mM

5848

-

5.4.99.12

activity is inhibited by single tRNAs or bulk tRNA from all sources tested, and by ribosomal RNA

648848

-

6.1.1.12

above 0.4 mg/ml

114

-

6.1.1.18

above 0.6 mg/ml

114

-

6.1.1.5

partly inhibits the binding of diphosphate

454

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (10 results)

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Show Turnover Number (10 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.4.2.29

0.005

-

mutant Y106F

703226

2.4.2.29

0.014

-

wild-type

703226

2.4.2.29

0.054

-

wild type enzyme

688390

2.4.2.29

0.07

-

mutant enzyme E235Q

688390

2.4.2.29

0.71

-

histidine-tagged mutant enzyme D89E, pH 7.3

644933

2.4.2.29

0.93

-

histidine-tagged mutant enzyme D89E, pH 8.5

644933

2.4.2.29

1.21

-

histidine-tagged wild-type enzyme, pH 7.3

644933

2.4.2.29

5.85

-

histidine-tagged wild-type enzyme, pH 8.5

644933

4.6.1.18

0.056

-

pH 7.0

680679

4.6.1.18

2.6

-

pH 7.0

680679

2.4.2.29

8 entries

4.6.1.18

2 entries

K_M Value (15 results)

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Show KM Value (15 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.4.2.29

0.00011

-

histidine-tagged mutant enzyme D89E, pH 7.3

644933

2.4.2.29

0.00012

-

histidine-tagged wild-type enzyme, pH 7.3

644933

2.4.2.29

0.00036

-

mutant Y106F

703226

2.4.2.29

0.00039

-

histidine-tagged wild-type enzyme, pH 8.5

644933

2.4.2.29

0.00051

-

histidine-tagged mutant enzyme D89E, pH 8.5

644933

2.4.2.29

0.0009

-

wild type enzyme, in 200 mM HEPES, pH 7.3, 20 mM MgCl2

688390

2.4.2.29

0.001

-

mutant enzyme E235Q, in 200 mM HEPES, pH 7.3, 20 mM MgCl2

688390

2.4.2.29

0.001

-

wild-type

703226

2.4.2.29

8 entries

2.8.1.4

0.0027

-

pH 7.5, 37°C, sulfur deficient tRNA

643807

3.1.26.5

0.00025

-

pH 7.5, 77°C

680594

4.6.1.18

0.0005

-

pH 7.0

680679

4.6.1.18

0.0172

-

pH 7.0

680679

4.6.1.18

4

-

pH 7.5, 37°C, wild-type enzyme

666332

4.6.1.18

5

-

pH 7.5, 37°C, mutant enzyme D121A

666332

4.6.1.18

4 entries

6.1.1.7

0.023

-

mutant AlaRS(K73E), aminoacylation

514

K_i Value (10 results)

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Show KI Value (10 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.1.1.29

0.000095

-

pH 7.5, 50°C, unfractionated Escherichia coli tRNA

648112

3.1.1.29

0.000095

-

unfractionated tRNA from Escherichia coli, 50°C, pH 7.5

648112

3.1.4.16

0.29

-

with ATP

652555

3.1.4.16

1.08

-

with 2'-AMP

652555

3.1.4.16

1.68

-

with 2',3'-cAMP

652555

3.1.4.37

0.00000168

-

hydrolysis of cyclic 2',3'-AMP

652555

3.1.4.37

0.29

-

with ATP

652555

3.1.4.37

1.08

-

with 2'-AMP

652555

3.1.4.37

1.68

-

with 2',3'-cAMP

652555

3.1.1.29

2 entries

3.1.4.16

3 entries

3.1.4.37

4 entries

4.2.1.70

0.005

-

wild-type RNA

5848

References & Links

Literature References (105)

top print hide

Show Reference (105 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

114

-

Amino acid substrate specificity of asparaginyl-, aspartyl- and glutaminyl-tRNA synthetase isolated from higher plants

1973

Lea, P.J.; Fowden, L.

Phytochemistry

12

1903-1916

454

1459130

Analysis of the isoleucyl-tRNA synthetase reaction by total rate equation. Magnesium and spermidine in the tRNA kinetics

1992

Airas, R.K.

Eur. J. Biochem.

210

451-454

514

8239663

Amino acid substitutions at position 73 in motif 2 of Escherichia coli alanyl-tRNA synthetase

1993

Filley, S.J.; Hill, K.A.W.

Arch. Biochem. Biophys.

307

46-51

5848

370771

Purification of pseudouridylate synthetase I from Salmonella typhimurium

1978

Arena, F.; Ciliberto, G.; Ciampi, S.; Cortese, R.

Nucleic Acids Res.

5

4523-4536

134050

4867942

The processive degradation of individual polyribonucleotide chains. I. Escherichia coli ribonuclease II

1968

Nossal, N.G.; Singer, M.F.

J. Biol. Chem.

243

913-922

134051

364422

An Escherichia coli ribonuclease which removes an extra nucleotide from a biosynthetic intermediate of bacteriophage T4 proline transfer RNA

1978

Schmidt, F.J.; McClain, W.H.

Nucleic Acids Res.

5

4129-4139

134062

7509797

The role of individual exoribonucleases in processing at the 3¦end of Escherichia coli tRNA precursors

1994

Li, Z.; Deutscher, M.P.

J. Biol. Chem.

269

6064-6071

134137

4604937

Preparation of transfer RNA fragments by limited degradation with spleen exonuclease

1974

Philippsen, P.; Zachau, H.G.

Methods Enzymol.

29E

473-477

134145

4341777

Partial degradation of transfer RNAs and transfer RNA fragments by spleen phosphodiesterase as studied by disc electrophoretic methods

1972

Philippsen, P.; Zachau, H.G.

Biochim. Biophys. Acta

277

523-538

134147

5773050

Action of spleen exonuclease on transfer ribonucleic acid

1969

Bernardi, A.; Cantoni, G.L.

J. Biol. Chem.

244

1468-1476

134148

4297867

Action of spleen phosphodiesterase upon soluble ribonucleic acid

1968

Gunther, J.K.; Chang, A.Y.; Clark, J.M.

Arch. Biochem. Biophys.

125

480-487

134149

4295294

Studies on acid hydrolases. IV. Isolation and characterization of spleen exonuclease

1968

Bernardi, A.; Bernardi, G.

Biochim. Biophys. Acta

155

360-370

134292

6630162

Purification and properties of an acid deoxyribonuclease from rat small intestinal mucosa

1983

Anai, M.; Muta, A.; Umeno, M.; Sasaki, M.

J. Biochem.

94

339-344

134308

-

Spleen acid deoxyribonuclease

1971

Bernarde, G.

The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )

4

271-287

134336

3547326

Structure of secondary cleavage sites of E. coli RNAaseIII in A3t RNA from bacteriophage T7

1987

Gross, G.; Dunn, J.J.

Nucleic Acids Res.

15

431-442

134339

6380579

7S RNA, containing 5S ribosomal RNA and the termination stem, is a specific substrate for the two RNA processing enzymes RNase III and RNase E

1984

Szeberenyi, J.; Roy, M.K.; Vaidya, H.C.; Apirion, D.

Biochemistry

23

2952-2957

134342

7161796

Processing of bacteriophage T4 primary transcripts with ribonuclease III

1982

Barkay, T.; Goldfarb, A.

J. Mol. Biol.

162

299-315

134349

781626

Cleavage of T4 species I ribonucleic acid by Escherichia coli ribonuclease III

1976

Paddock, G.V.; Fukada, K.; Abelson, J.; Robertson, H.D.

Nucleic Acids Res.

3

1351-1371

134356

1280810

RNase D, a reported new activity associated with HIV-1 reverse transcriptase, displays the same cleavage specificity as Escherichia coli RNase III

1992

Hostomsky, Z.; Hudson, G.O.; Rahmati, S.; Hostomska, Z.

Nucleic Acids Res.

20

5819-5824

134360

8936814

The multifaceted roles of the RNA processing enzyme ribonuclease III

1996

Srivastava, R.A.; Srivastava, N.

Indian J. Biochem. Biophys.

33

253-260

134415

1689306

Ribonuclease P: function and variation

1990

Pace, N.R.; Smith, D.

J. Biol. Chem.

265

3587-3590

134427

778851

Ribonuclease P substrate specificity: cleavage of a bacteriophage phi80-induced RNA

1976

Bothwell, A.L.M.; Stark, B.C.; Altman, S.

Proc. Natl. Acad. Sci. USA

73

1912-1916

134430

358197

Ribonuclease P: an enzyme with an essential RNA component

1978

Stark, B.C.; Kole, R.; Bowman, E.J.; Altman, S.

Proc. Natl. Acad. Sci. USA

75

3717-3721

134435

10085

Identification of a ribonuclease P-like activity from human KB cells

1976

Koski, R.A.; Bothwell, A.L.M.; Altman, S.

Cell

9

101-116

134445

6160876

Identification of ribonuclease P activity from chick embryos

1980

Bowman, E.J.; Altman, S.

Biochim. Biophys. Acta

613

439-447

134556

8632481

Role of the N terminus in RNase A homologues: differences in catalytic activity, ribonuclease inhibitor interaction and cytotoxicity

1996

Boix, E.; Wu, Y.; Vasandani, V.M.; Saxena, S.K.; Ardelt, W.; Ladner, J.; Youle, R.J.

J. Mol. Biol.

257

992-1007

134557

9314116

Inhibition and substrate competition kinetics in analysis of porcine thyroid alkaline ribonuclease's specificity toward synthetic RNA's and tRNA

1997

Crute, B.E.; Markstein, J.A.; Kull, F.J.

J. Enzyme Inhib.

12

205-226

134965

1096085

Specific cleavage of tRNA by nuclease S1

1975

Harada, F.; Dahlberg, J.E.

Nucleic Acids Res.

2

865-871

134969

-

Endonucleases specific for single-stranded polynucleotides

1981

Lehman, R.I.

The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )

4

193-201

134985

125412

The cleavage of transfer RNA by a single strand specific endonuclease from Neurospora crassa

1975

Tal, J.

Nucleic Acids Res.

2

1073-1082

288788

16001

Endonuclease from Escherichia coli that acts specifically upon duplex DNA damaged by ultraviolet light, osmium tetroxide, acid, or x-rays

1977

Gates III, F.T.; Linn, S.

J. Biol. Chem.

252

2802-2807

487795

8434942

Inhibitory effect of spermine on ribosomal peptidyltransferase

1993

Kalpaxis, D.L.; Drainas D.

Arch. Biochem. Biophys.

300

629-634

487796

14222897

The puromycin reaction and its relation to protein synthesis

1964

Traut, R.R.; Monro, R.E.

J. Mol. Biol.

10

63-72

487797

5329275

Release of lysine peptides by puromycin from polylysyl-transfer ribonucleic acid in the presence of ribosomes

1966

Rychlik, I.

Biochim. Biophys. Acta

114

425-427

487798

11947081

The effect of the aminoacyl-4-aminohexosyl-cytosine group of antibiotics on ribosomal peptidyl transferase

1973

Cerna, J.; Rychlik, I.; Lichtenthaler, F.W.

FEBS Lett.

30

147-150

487799

4819752

Characterization of the peptidyltransferase reaction catalyzed by rat liver 60S ribosomal subunits

1974

Thompson, H.A.; Moldave, K.

Biochemistry

13

1348-1353

487800

-

Assay of ester and polyester formation by the ribosomal peptidyltransferase

1974

Fahnestock, S.; Neumann, H.; Rich, A.

Methods Enzymol.

30 F

489-497

487802

791676

The effect of ribosomal peptidyl-transferase inhibitors is antagonized by elongation factor G with GTP

1976

Spirin, A.S.; Asatryan, L.S.

FEBS Lett.

70

101-104

487803

358982

Inhibition of ribosomal peptidyltransferase with cytidyl-3 leads to 5-[2(3)-O-L-phenylalanyl]-L-adenosine

1978

Bhuta, P.; Zemlicka, J.

Biochem. Biophys. Res. Commun.

83

414-420

487805

-

Phenylboric acids - A new group of peptidyl transferase inhibitors

1980

Cerna, J.; Rychlik, I.

FEBS Lett.

119

342-348

487806

7037056

Inhibition of the peptidyltransferase acceptor site by 2(3)-O-cycloleucyl- and alpha-aminoisobutyryl derivatives of cytidylyl-(3-5)adenosine

1982

Chladek, S.; Bhuta, P.

Biochim. Biophys. Acta

696

212-217

487807

3510869

Kinetic studies on ribosomal peptidyltransferase. The behaviour of the inhibitor blasticidin S

1986

Kalpaxis, D.L.; Theocharis, D.A.; Coutsogeorgopoulos, C.

Eur. J. Biochem.

154

267-271

487808

3549307

Inhibition of ribosomal peptidyltransferase by chloramphenicol. Kinetic studies

1987

Drainas D.; Kalpaxis, D.L.; Coutsogeorgopoulos, C.

Eur. J. Biochem.

164

53-58

487809

3545299

Studies on the catalytic rate constant of ribosomal peptidyltransferase

1987

Synetos, D.; Coutsogeorgopoulos, C.

Biochim. Biophys. Acta

923

275-285

487810

9016356

Aminoacyl and peptidyl analogs of chloramphenicol as slow-binding inhibitors of ribosomal peptidyltransferase: a new approach for evaluating their potency

1997

Michelinaki, M.; Mamos, P.; Coutsogeorgopoulos, C.; Kalpaxis, D.L.

Mol. Pharmacol.

51

139-146

487811

9126380

Determination of eukaryotic peptidyltransferase activity by pseudo-first-order kinetic analysis

1997

Ioannou, M.; Coutsogeorgopoulos, C.; Drainas, D.

Anal. Biochem.

247

115-122

487812

9392527

New aspects on the kinetics of activation of ribosomal peptidyltransferase-catalyzed peptide bond formation by monovalent ions and spermine

1997

Michelinaki, M.; Spanos, A.; Coutsogeorgopoulos, C.; Kalpaxis, D.L.

Biochim. Biophys. Acta

1342

182-190

487813

9308906

Kinetic studies on the activation of eukaryotic peptidyltransferase by potassium

1997

Ioannou, M.; Coutsogeorgopoulos, C.

Arch. Biochem. Biophys.

345

325-331

487814

9614213

Kinetics of inhibition of rabbit reticulocyte peptidyltransferase by anisomycin and sparsomycin

1998

Ioannou, M.; Coutsogeorgopoulos, C.; Synetos, D.

Mol. Pharmacol.

53

1089-1096

487815

9874209

Structure/function correlation of spermine-analog-induced modulation of peptidyltransferase activity

1998

Karahalios, P.; Mamos, P.; Karigiannis, G.; Kalpaxis, D.L.

Eur. J. Biochem.

258

437-444

487816

11470897

Analysis of mutations at residues A2451 and G2447 of 23S rRNA in the peptidyltransferase active site of the 50S ribosomal subunit

2001

Thompson, J.; Kim, D.F.; O'Connor, M.; Lieberman, K.R.; Bayfield, M.A.; Gregory, S.T.; Green, R.; Noller, H.F.; Dahlberg, A.E.

Proc. Natl. Acad. Sci. USA

98

9002-9007

487817

11434779

Yeast Ribosomal Protein Deletion Mutants Possess Altered Peptidyltransferase Activity and Different Sensitivity to Cycloheximide

2001

Dresios, J.; Panopoulos, P.; Frantziou, C.P.; Synetos, D.

Biochemistry

40

8101-8108

487818

12433929

A dispensable yeast ribosomal protein optimizes peptidyltransferase activity and affects translocation

2003

Dresios, J.; Panopoulos, P.; Suzuki, K.; Synetos, D.

J. Biol. Chem.

278

3314-3322

488003

4587124

Peptide acceptors in the leucine, phenylalanine transfer reaction

1973

Soffer, R.L.

J. Biol. Chem.

248

8424-8428

637156

4898378

The in vitro synthesis of 2-methylguanosine and 2-methylthio 6N(gamma,gamma, dimethylallyl)adenosine in transfer RNA of Escherichia coli

1969

Gefter, M.L.

Biochem. Biophys. Res. Commun.

36

435-441

642775

8113190

Activation of ATP:GTP 3-pyrophosphotransferase (guanosine pentaphosphate synthetase) in Streptomyces antibioticus

1994

Jones, G.H.

J. Bacteriol.

176

1482-1487

643522

3275667

3 Processing of tRNA precursors in ribonuclease-deficient Escherichia coli. Development and characterization of an in vitro processing system and evidence for a phosphate requirement

1988

Cudny, H.; Deutscher, M.P.

J. Biol. Chem.

263

1518-1523

643523

2455297

RNase PH: an Escherichia coli phosphate-dependent nuclease distinct from polynucleotide phosphorylase

1988

Deutscher, M.P.; Marshall, G.T.; Cudney, H.

Proc. Natl. Acad. Sci. USA

85

4710-4714

643524

1512252

Overexpression and rapid purification of the orfE/rph gene product, RNase PH of Escherichia coli

1992

Jensen, K.F.; Andersen, J.T.; Poulsen, P.

J. Biol. Chem.

267

17147-17152

643525

1512253

Characterization of Escherichia coli RNase PH

1992

Kelly, K.O.; Deutscher, M.P.

J. Biol. Chem.

267

17153-17158

643526

1707683

RNase PH catalyzes a synthetic reaction, the addition of nucleotides to the 3 end of RNA

1990

Ost, K.A.; Deutscher, M.P.

Biochimie

72

813-818

643528

11796219

Running rings around RNA: a superfamily of phosphate-dependent RNases

2002

Symmons, M.F.; Williams, M.G.; Luisi, B.F.; Jones, G.H.; Carpousis, A.J.

Trends Biochem. Sci.

27

11-18

643807

4942454

Sulfur-deficient transfer ribonucleic acid. The natural substrate for ribonucleic acid sulfurtransferase from Escherichia coli

1971

Harris, C.L.; Titchener, E.B.

Biochemistry

10

4207-4212

644933

11714265

tRNA-guanine transglycosylase from Escherichia coli: Molecular mechanism and role of aspartate 89

2001

Kittendorf, J.D.; Barcomb, L.M.; Nonekowski, S.T.; Garcia, G.A.

Biochemistry

40

14123-14133

648107

4981785

Enzymatic hydrolysis of N-substituted aminoacyl transfer ribonucleic acid in yeast

1969

Jost, J.P.; Bock, R.M.

J. Biol. Chem.

244

5866-5873

648110

14660562

Crystral structure of a human peptidyl-tRNA hydrolase eveals a new fold and suggests basis for a bifunctional activity

2003

de Pereda, J.M.; Waas, W.F.; Jan, Y.; Ruoslathi, E.; Schimmel, P.; Pascual, J.

J. Biol. Chem.

279

8111-8115

648112

12799450

Peptidyl-tRNA hydrolase from Sulfolobus solfataricus

2003

Fromant, M.; Ferri-Fioni, M.L.; Plateau, P.; Blanquet, S.

Nucleic Acids Res.

31

3227-3235

648116

12475929

Orthologs of a novel archaeal and of the bacterial peptidyl-tRNA hydrolase are nonessential in yeast

2002

Rosas-Sandoval, G.; Amrogelly, A.; Rinehart, J.; Wei, D.; Cruz-Vera, L.R.; Graham, D.E.; Stetter, K.O.; Guarneros, G.; Soell, D.

Proc. Natl. Acad. Sci. USA

99

16707-16712

648848

7037778

Purification and properties of a mammalian tRNA pseudouridine synthase

1982

Green, C.; Kammen, H.; Penhoet, E.

J. Biol. Chem.

257

3045-3052

650058

11141055

Methanococcus jannaschii prolyl-cysteinyl-tRNA synthetase possesses overlapping amino acid binding sites

2001

Stathopoulos, C.; Jacquin-Becker, C.; Becker, H.D.; Li, T.; Ambrogelly, A.; Longman, R.; Soll, D.

Biochemistry

40

46-52

650249

15078105

Essential role of histidine 20 in the catalytic mechanism of Escherichia coli peptidyl-tRNA hydrolase

2004

Goodall, J.J.; Chen, G.J.; Page, M.G.

Biochemistry

43

4583-4591

651296

11904177

Cysteinyl-tRNA formation and prolyl-tRNA synthetase

2002

Jacquin-Becker, C.; Ahel, I.; Ambrogelly, A.; Ruan, B.; Soll, D.; Stathopoulos, C.

FEBS Lett.

514

34-36

652555

15210699

The HD domain of the E. coli tRNA nucleotidyltransferase has 2',3'-cyclic phosphodiesterase, 2'-nucleotidase, and phosphatase activities

2004

Yakunin, A.F.; Proudfoot, M.; Kuznetsova, E.; Savchenko, A.; Brown, G.; Arrowsmith, C.H.; Edwards, A.M.

J. Biol. Chem.

279

36819-36827

653153

11390689

Suppression of thermosensitive peptidyl-tRNA hydrolase mutation in Escherichia coli by gene duplication

2001

Menez, J.; Remy, E.; Buckingham, R.H.

Microbiology

147

1581-1589

653271

12100553

Peptidyl-tRNA hydrolase in Bacillus subtilis, encoded by spoVC, is essential to vegetative growth, whereas the homologous enzyme in Saccharomyces cerevisiae is dispensable

2002

Menez, J.; Buckingham, R.H.; de Zamaroczy, M.; Campelli, C.K.

Mol. Microbiol.

45

123-129

653662

11717392

Cysteinyl-tRNA synthetase is not essential for viability of the archaeon Methanococcus maripaludis

2001

Stathopoulos, C.; Kim, W.; Li, T.; Anderson, I.; Deutsch, B.; Palioura, S.; Whitman, W.; Soll, D.

Proc. Natl. Acad. Sci. USA

98

14292-14297

653741

11812233

Expression, purification, and characterization of peptidyl-tRNA hydrolase from Staphylococcus aureus

2002

Bonin, P.D.; Choi, G.H.; Trepod, C.M.; Mott, J.E.; Lyle, S.B.; Cialdella, J.I.; Sarver, R.W.; Marshall, V.P.; Erickson, L.A.

Protein Expr. Purif.

24

123-130

656877

11328875

Ethidium-dependent uncoupling of substrate binding and cleavage by Escherichia coli ribonuclease III

2001

Calin-Jageman, I.; Amarasinghe, A.K.; Nicholson, A.W.

Nucleic Acids Res.

29

1915-1925

657199

11929972

A protein subunit of human RNase P, Rpp14, and its interacting partner, OIP2, have 3'->5' exoribonuclease activity

2002

Jiang, T.; Altman, S.

Proc. Natl. Acad. Sci. USA

99

5295-5300

662141

12704200

Aquifex aeolicus tRNA (Gm18) methyltransferase has unique substrate specificity: tRNA recognition mechanism of the enzyme

2003

Hori, H.; Kubota, S.; Watanabe, K.; Kim, J.M.; Ogasawara, T.; Sawasaki, T.; Endo, Y.

J. Biol. Chem.

278

25081-25090

663410

15062082

Deep knot structure for construction of active site and cofactor binding site of tRNA modification enzyme

2004

Nureki, O.; Watanabe, K.; Fukai, S.; Ishii, R.; Endo, Y.; Hori, H.; Yokoyama, S.

Structure

12

593-602

663854

15541362

Green tea polyphenols as inhibitors of ribonuclease A

2004

Ghosh, K.S.; Maiti, T.K.; Dasgupta, S.

Biochem. Biophys. Res. Commun.

325

807-811

666332

16335788

Role of aspartic acid 121 in human pancreatic ribonuclease catalysis

2005

Gaur, D.; Batra, J.K.

Mol. Cell. Biochem.

275

95-101

666621

14671015

Isolation and characterization of an RIP (ribosome-inactivating protein)-like protein from tobacco with dual enzymatic activity

2004

Sharma, N.; Park, S.W.; Vepachedu, R.; Barbieri, L.; Ciani, M.; Stirpe, F.; Savary, B.J.; Vivanco, J.M.

Plant Physiol.

134

171-181

674692

16963456

Functional categorization of the conserved basic amino acid residues in TrmH (tRNA (Gm18) methyltransferase) enzymes

2006

Watanabe, K.; Nureki, O.; Fukai, S.; Endo, Y.; Hori, H.

J. Biol. Chem.

281

34630-34639

676232

17150753

Structural change of tRNA (Gm18) methyltransferase by binding of methyl donor analogues

2005

Watanabe, K.; Nureki, O.; Fukai, S.; Endo, Y.; Hori, H.

Nucleic Acids Symp. Ser.

49

301-302

677157

17161369

Structural bases of transfer RNA-dependent amino acid recognition and activation by glutamyl-tRNA synthetase

2006

Sekine, S.; Shichiri, M.; Bernier, S.; Chenevert, R.; Lapointe, J.; Yokoyama, S.

Structure

14

1791-1799

680594

2115885

Characterization of ribonuclease P from the archaebacterium Sulfolobus solfataricus.

1990

Darr, S.C.; Pace, B.; Pace, N.R.

J. Biol. Chem.

265

12927-12932

680679

16803891

Evolution and function of leukocyte RNase A ribonucleases of the avian species, Gallus gallus

2006

Nitto, T.; Dyer, K.D.; Czapiga, M.; Rosenberg, H.F.

J. Biol. Chem.

281

25622-25634

681841

17347156

Zebrafish ribonucleases are bactericidal: implications for the origin of the vertebrate RNase A superfamily

2007

Cho, S.; Zhang, J.

Mol. Biol. Evol.

24

1259-1268

682189

18096622

Kluyveromyces lactis gamma-toxin, a ribonuclease that recognizes the anticodon stem loop of tRNA

2008

Lu, J.; Esberg, A.; Huang, B.; Bystroem, A.S.

Nucleic Acids Res.

36

1072-1080

688390

17949745

Glutamate versus glutamine exchange swaps substrate selectivity in tRNA-guanine transglycosylase: insight into the regulation of substrate selectivity by kinetic and crystallographic studies

2007

Tidten, N.; Stengl, B.; Heine, A.; Garcia, G.A.; Klebe, G.; Reuter, K.

J. Mol. Biol.

374

764-776

693208

18096702

Characterization of the essential activities of Saccharomyces cerevisiae Mtr4p, a 3'->5' helicase partner of the nuclear exosome

2008

Bernstein, J.; Patterson, D.N.; Wilson, G.M.; Toth, E.A.

J. Biol. Chem.

283

4930-4942

697170

17786051

hClp1: a novel kinase revitalizes RNA metabolism

2007

Weitzer, S.; Martinez, J.

Cell Cycle

6

2133-2137

697209

18217203

RNA-splicing endonuclease structure and function

2008

Calvin, K.; Li, H.

Cell. Mol. Life Sci.

65

1176-1185

699518

17174977

Achieving specific RNA cleavage activity by an inactive splicing endonuclease subunit through engineered oligomerization

2007

Calvin, K.; Li, H.

J. Mol. Biol.

366

642-649

702263

19874048

Identification of the rate-determining step of tRNA-guanine transglycosylase from Escherichia coli

2009

Garcia, G.A.; Chervin, S.M.; Kittendorf, J.D.

Biochemistry

48

11243-11251

703226

19894214

How to replace the residual solvation shell of polar active site residues to achieve nanomolar inhibition of tRNA-guanine transglycosylase

2009

Ritschel, T.; Kohler, P.C.; Neudert, G.; Heine, A.; Diederich, F.; Klebe, G.

ChemMedChem

4

2012-2023

721471

6268077

The 2'5' oligoadenylate synthetase has a multifunctional 2',5' nucleotidyl-transferase activity

1981

Ferbus, D.; Justesen, J.; Besancon, F.; Thang, M.

Biochem. Biophys. Res. Commun.

100

847-856

721678

23072323

Mechanism of N6-threonylcarbamoyladenonsine (t6A) biosynthesis: isolation and characterization of the intermediate threonylcarbamoyl-AMP

2012

Lauhon, C.T.

Biochemistry

51

8950-8963

722945

15003446

The Escherichia coli YadB gene product reveals a novel aminoacyl-tRNA synthetase like activity

2004

Campanacci, V.; Dubois, D.Y.; Becker, H.D.; Kern, D.; Spinelli, S.; Valencia, C.; Pagot, F.; Salomoni, A.; Grisel, S.; Vincentelli, R.; Bignon, C.; Lapointe, J.; Giege, R.; Cambillau, C.

J. Mol. Biol.

337

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727456

12013438

Aminoacyl-tRNA formation in the extreme thermophile Thermus thermophilus

2002

Feng, L.; Stathopoulos, C.; Ahel, I.; Mitra, A.; Tumbula-Hansen, D., Hartsch, T.; Söll, D.

Extremophiles

6

167-174

728126

11866507

Amino acid activation of a dual-specificity tRNA synthetase is independent of tRNA

2002

Lipman, R.S.; Beuning, P.J.; Musier-Forsyth, K.; Hou, Y.M.

J. Mol. Biol.

316

421-427

771017

37360940

Enhancement of the activity of the antimicrobial peptides HNP1 and LL-37 by bovine pancreatic ribonuclease A

2022

Ericksen, B.

F1000Res.

11

933

772346

36982544

Factor VII activating protease (FSAP) and its importance in hemostasis-part I FSAP structure, synthesis and activity regulation A narrative review

2023

Kwiatkowska, I.; Zekanowska, E.; Lattanzi, S.; Alexandre, A.M.; Kister-Kowalska, A.; Slomka, A.

Int. J. Mol. Sci.

24

5473

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