Information on EC 3.1.1.29 - aminoacyl-tRNA hydrolase

peptidyl-tRNALys + H2O

peptide + tRNALys

Phe-Phe-tRNA + H2O

Phe-Phe + tRNA

648106

Phe-tRNA + H2O

Phe + tRNA

phenyllactyl-Phe-tRNA + H2O

phenyllactyl-Phe + tRNA

648106

poly-Val-tRNA + H2O

poly-Val + tRNA

648106

Ser-tRNA + H2O

Ser + tRNA

Ser-tRNAAla + H2O

Ser + tRNAAla

Tyr-tRNA + H2O

Tyr + tRNA

Val-tRNA + H2O

Val + tRNA

Val-tRNAVal + H2O

Val + tRNAVal

additional information

23 entries

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diacetyl-lysyl-tRNALys + H2O

diacetyl-lysine + tRNALys

N-substituted aminoacyl-tRNA + H2O

N-substituted amino acid + tRNA

28 entries

peptidyl-tRNA + H2O

peptide + tRNA

P9WHN7

681450

peptidyl-tRNAL + H2O

peptide + tRNA

Pth is a key protein at the crossroads to the function of several translational factors, accumulation of peptidyl-tRNA in the cells leads to depletion of aminoacyl-tRNA pools and halts protein biosynthesis, it is vital for cells to maintain Pth activity to deal with the pollution of peptidyl-tRNAs generated during the initiation, elongation and termination steps of protein biosynthesis, overview

681789

peptidyl-tRNALys + H2O

peptide + tRNALys

accumulation of peptidyl-tRNA due to enzyme misfunction is toxic to the cells, overproduction of tRNALys suppresses the effects of pthTs mutation at 41°C but not at 43°C, and increases the levels of aminoacyl-tRNA

682160

additional information

6 entries

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Ca2+

activation is 25% lower than with Mg2+ or Mn2+

K+

0.3 mM, 77fold activation

KCl

300 mM, 77fold activation; activates about 80fold, optimally at 300 mM

Mg2+

5 entries

MgCl2

40 mM, approx. 88fold activation

Mn2+

Zn2+

a zinc ion is coordinated by the conserved zinc-binding cluster in the C-domain, which is expected to be the enzymatic active site

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3'-deoxy-N[(O-methyl-L-tyrosyl)amino]adenosine

729170

3'-L-(N,N-diacetyl-lysinyl)amino-3'-deoxyadenosine

5-azacytidine

729170

70 S ribosome

free N-carbobenzyloxy-Phe-tRNA is rapidly cleaved by the enzyme. When bound to a 30 S ribosome in the presence of poly(U), the substrate is hydrolyzed rapidly as when free. The addition of 50 S ribosomal subunits to form the 70S ribosomal binding complex protects the bound substrate from the enzyme

648108

deacetylated tRNA

diethyldicarbonate

0.5 mM, 90% inactivation after 10 min, activity can be recovered to 41% of initial activity by treatment wit 200 mM hydroxylamine

EDTA

Mg2+

0.1 mM

non-esterified tRNALys

tRNA

tRNA-formyl-methionine

from Escherichia coli

tRNA-lysine

from Escherichia coli

tRNAfMet

; tRNAfMet from Escherichia coli

tRNALys

tRNALys from Escherichia coli

Uncharged tRNA

e.g. from Escherichia coli, at concentrations of 0.01 mM or above

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spermidine

0.1 mM spermidine HCl, 73fold activation

spermidine-HCl

0.1 mM, 73fold activation; activates about 80fold, optimally at 0.1 mM

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0.000016

acetyl-His-tRNAHis

pH 7.5, 50°C

0.000016

acetyl-histidyl-tRNA

50°C, pH 7.5

0.000016

acetyl-histidyl-tRNAHis

pH 7.5, 50°C, recombinant enzyme

0.008

bulk peptidyl-tRNA

at pH 5.0 and 25°C

0.000003

dephosphorylated diacyl-lysine-tRNA

50°C, pH 7.5

0.00003

dephosphorylated formyl-methioninyl-tRNA

50°C, pH 7.5

0.0000028 - 0.024

diacetyl-Lys-tRNALys

9 entries

0.000011 - 0.006

diacetyl-lysine-tRNA

5 entries

0.0000028 - 12.8

diacetyl-lysyl-tRNALys

14 entries

0.000012

formyl-Met-tRNAfMet

pH 7.5, 50°C

0.00003

formyl-Met-tRNAfMet, dephosphorylated

pH 7.5, 50°C, dephosphorylated formyl-Met-tRNAfMet

0.000012

formyl-methionyl-tRNA

50°C, pH 7.5

0.000012 - 0.00003

formyl-methionyl-tRNAfMet

0.00471 - 0.0269

N-acetyl-Ala-tRNA(Ala)

4 entries

0.0022

N-acetyl-Met-tRNA

pH 7.0, 37°C

0.0008

N-acetyl-Phe-tRNA

pH 7.5, 30°C

0.000001

N-acetyl-phenylalanyl-tRNA

pH 7.0, 30°C

0.0055

Oregon Green-methionine-tRNA

25°C, pH 7.5

0.0008

Phe-tRNA

pH 7.5, 30°C

additional information

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3.4

acetyl-His-tRNA

pH 7.5, 50°C

3.4

acetyl-histidyl-tRNA

50°C, pH 7.5

3.4

acetyl-histidyl-tRNAHis

pH 7.5, 50°C, recombinant enzyme

0.86 - 6.08

dephosphorylated diacyl-lysine-tRNA

dephosphorylated formyl-methioninyl-tRNA

50°C, pH 7.5

1.3

diacetyl-Lys-tRNA

Q9Y3E5;

pH 7.5, 27°C

648110

0.028 - 3.6

diacetyl-Lys-tRNALys

9 entries

1.3 - 3.6

diacetyl-lysine-tRNA

4 entries

0.002 - 2.2

diacetyl-lysyl-tRNALys

12 entries

formyl-Met-tRNAfMet

pH 7.5, 50°C

formyl-methionyl-tRNA

50°C, pH 7.5

formyl-methionyl-tRNAfMet

phosphorylated and dephosphorylated substrate, pH 7.5, 50°C, recombinant enzyme

5.8 - 11.7

N-acetyl-Ala-tRNA(Ala)

4 entries

0.7

N-acetyl-Met-tRNA

pH 7.0, 37°C

o-hydroxycinnamic acid

50°C, pH 7.5

9.3

Oregon Green-methionine-tRNA

25°C, pH 7.5

additional information

effect of mutations altering the 1-72 pair of E. coli tRNAMetf on the turnover-number

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0.51

2'(3')-O-L-(N,N-diacetyl-lysinyl)adenosine

wild type enzyme, 28°C, 20 mM Tris-HCl (pH 7.5), 10 mM MgCl2, 0.1 mM EDTA, 0.1 mM dithiothreitol

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3'-L-(N,N-diacetyl-lysinyl)amino-3'-deoxyadenosine

at pH 6.0, with 50 mM sodium acetate and 200 mM NaCl, at 28°C

0.00005

non-esterified tRNALys

pH 7.5, 50°C, recombinant enzyme

0.000095

tRNA

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

0.0001

tRNA-formyl-methionine

tRNA-ormyl-methionine from Escherichia coli, 50°C, pH 7.5

0.00005

tRNA-lysine

tRNA-lysine from Escherichia coli, 50°C, pH 7.5

0.00011

tRNAfMet

pH 7.5, 50°C, recombinant enzyme

0.00011

tRNAformylMet

pH 7.5, 50°C, tRNAformylMet from Escherichia coli

0.00005

tRNALys

pH 7.5, 50°C, tRNALys from Escherichia coli

0.0001

Uncharged tRNA

pH 7.5, 50°C, recombinant enzyme

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0.0051

0.0149

0.07

Staphylococcus aureus

Q6YP15;

653741

0.078

substrate D-tyrosyl-tRNA, 37°C, pH 7.5

0.15

substrae D-tyrosyl-tRNA

4.14

; purified recombinant enzyme

substrate diacetyl-lysine-tRNA

31.8

substrate diacetyl-lysine tRNA, 37°C, pH 7.5

additional information

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7 - 7.5

7.5

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6 - 8.5

Staphylococcus aureus

Q6YP15;

approx. 38% at pH 6.0, approx. 20% of maximal activity at pH 8.5

653741

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assay at

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isoelectric focusing

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Q14197;

enzyme from encysted embryos is specific for acetyl-Phe-tRNA. An unspecific hydrolase active on several N-substituted amiinoacyl-tRNAs is practically absent in the encysted embryos and during embryogenesis and appears abruptly during larval development

648111

erythroblast

uterine adenocarcinoma cell

paraproerythroblast, low activity

Q14197;

low activity

low activity

648109

additional information

mutant strain AA7852 with temperature-sensitive Pth grown at 32°C and at 41°C

682160

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cytosol

Schizosaccharomyces pombe

5829

693637

mitochondrial membrane

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16 entries

Acinetobacter baumannii (strain ATCC 19606 / DSM 30007 / CIP 70.34 / JCM 6841 / NBRC 109757 / NCIMB 12457 / NCTC 12156 / 81);

Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126);

3v2i, download, 3D-view

SCOPe (3v2i)

CATH (3v2i)

Q2T1B9

Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264);

Escherichia coli (strain K12);

3ofv, download, 3D-view

SCOPe (3ofv)

CATH (3ofv)

D6J9H8

Escherichia coli B354;

3nea, download, 3D-view

SCOPe (3nea)

CATH (3nea)

Q5NGZ6

Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4);

2zv3, download, 3D-view

SCOPe (2zv3)

CATH (2zv3)

Q60363

Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440);

5 entries

Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155);

8 entries

Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv);

9 entries

Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1);

Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3);

4p7b, download, 3D-view

SCOPe (4p7b)

CATH (4p7b)

A0A0F6B281

Salmonella typhimurium (strain 14028s / SGSC 2262);

4yly, download, 3D-view

SCOPe (4yly)

CATH (4yly)

Q6YP15

Staphylococcus aureus;

4qt4, download, 3D-view

SCOPe (4qt4)

CATH (4qt4)

B5XIP6

Streptococcus pyogenes serotype M49 (strain NZ131);

1xty, download, 3D-view

SCOPe (1xty)

CATH (1xty)

Q980V1

Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2);

Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579);

7 entries

Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961);

Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395);

2mjl, download, 3D-view

SCOPe (2mjl)

CATH (2mjl)

C3LPI9

Vibrio cholerae serotype O1 (strain M66-2);

1ryb, download, 3D-view

SCOPe (1ryb)

CATH (1ryb)

Q9M5P4

Zea mays;

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12700

13100

2 * 13100, deduced from nucleotide sequence

Methanocaldococcus jannaschii

13500

x * 13500, SDS-PAGE

648116

15000

2 * 15000, recombinant enzyme, SDS-PAGE; x * 15000, SDS-PAGE

Schizosaccharomyces pombe

20000

x * 20000, SDS-PAGE

730350

20455

20460

calculated from amino acid sequence

693637

21000

Mycobacterium smegmatis

1 * 21000, SDS-PAGE

729836

21978

x * 21978, sequence calculation

23000

24000

x * 24000, SDS-PAGE

25000

25300

46000

gel filtration

55000

gel filtration

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10 entries

dimer

monomer

15 entries

additional information

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native enzyme and in complex with cytidine or uridine, hanging drop vapor diffusion method, using 25% (w/v) PEG 10000, 0.3 M MgCl2 and 0.1 M HEPES buffer at pH 6.0

Acinetobacter baumannii

D0C9L6;

730738

crystal structure analysis

681789

crystal structure at 1.3 A resolution

crystallization by using polyethylene glycol as precipitant, recombinant enzyme

648119

crystallization using polyethylene glycol as precipitant and isopropanol as additive, crystal structure at 1.2 A

in complex with the tRNA CCA-acceptor-TpsiC domain of tRNAAla, sitting drop vapor diffusion method, using 100 mM sodium acetate buffer (pH 5.2), 20% (w/v) 1,4-butanediol and 30 mM glycyl-glycylglycine, at 20°C

recombinant enzyme, sitting drop vapor diffusion techniques; sitting-drop vapor diffusion at room temperature, 10 mg/ml protein in 100 mM HEPES, pH 7.5 and 20% polyethylene glycol 10000 is equilibrated against a reservoir of the same solution, crystals diffract to 2.0 A

Q9Y3E5;

648110

hanging drop vapor diffusion method, using 30% (w/v) PEG-1500 and 10% (v/v) isopropanol in 100 mM HEPES buffer, pH 6.5

Mycobacterium smegmatis

729836

microbatch-under-oil method, using 0.1 M HEPES pH 7.5, 15% (w/v) PEG 8000, 5% (v/v) isopropanol or 0.1 M HEPES pH 7.5 and 5% (v/v) dioxane with 25% (w/v) PEG 8000

728894

purified recombinant enzyme, X-ray diffraction structure determination and analysis at 1.98 A, 2.35 A, and 2.49 A resolution, molecular replacement

P9WHN7;

681450

purified recombinant His-tagged enzyme, microbatch method, 0.002 ml each of the protein solution, containing 6 mg/ml protein, 20 mM Tris-HCl, pH 7.5, 100 mM NaCl and 2 mM 2-mercaptoethanol, and the precipitant solution, containing 20% w/v PEG 8000 in 0.1 M HEPES, pH 7.5, and 5% v/v 2-propanol or dioxane or 25% w/v PEG 8000, 100 mM sodium cacodylate, pH 6.6, and 5% v/v 2-propanol, are mixed, 5 days to 2 weeks, X-ray diffraction structure determination and analysis at 1.97-2.49 A resolution

677362

native enzyme and in complex with 3'-deoxy-N[(O-methyl-L-tyrosyl)amino]adenosine or 5-azacytidine, hanging drop vapor diffusion method, using 25% (w/v) PEG 4000, 5% (v/v) propan-2-ol and 0.1 M HEPES buffer, pH 7.5

729170

hanging-drop vapour-diffusion method at 20°C, crystal structure is determined at 2.7 A resolution

Salmonella enterica subsp. enterica serovar Typhimurium

hanging drop vapor diffusion method, using 0.03 M citric acid, 0.05 M Bis-Tris propane, 1% (v/v) glycerol, 3% (w/v) sucrose, 25% (w/v) PEG 6000 pH 7.6

D0ZJ57;

hanging drop vapour diffusion method, 1.8 A resolution

664102

purified recombinant enzyme, hanging drop vapour diffusion method, 24°C, 0.0027 ml of 1.3 mg/ml protein in 20 mM Tris-HCl, pH 7.0, 0.1 mM EDTA, and 10 mM 2-mercaptoethanol are mixed with 0.0007 ml of 11 mg/ml tRNAfMet solution and 0.002 ml of reservoir solution containing 0.8 M LiSO4 and 1.6% PEG 8000, crystallization of tRNA free crystals within a few days, X-ray diffraction structure determination and analysis of native and HgBr2-containing crystals at 1.8-3.0 A resolution, modeling

Q980V1;

678132

sitting drop vapor diffusion method, using 100 mM phosphate-citrate buffer pH 4.2, and 50% (w/v) 2-methyl-2,4-pentanediol

Thermus thermophilus

728907

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6 - 7.5

Artemia sp.

4°C, 24 h, stable

648113

6 - 8

30°C, 30 min, stable

648114

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10 min, 70% loss of activity

Artemia sp.

10 min, 85% loss of activity

648113

stable up to

additional information

thermally-induced unfolding curve for MtPth indicates a simple two-state unfolding process without any intermediates, thermodynamic stability of the enzyme, pH 6.5, 25°C, overview

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urea/guanidinium chloride-induced unfolding curve for MtPth indicates a simple two-state unfolding process without any intermediates, pH 6.5, 25°C

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-10°C, 50% glycerol, purified enzyme is stable for several months

Artemia sp.

648113

-10°C, in presence of 1 mg/ml bovine serum albumin, no loss of activity

-20°C, buffer solution: 0.05 M Tris-HCl, pH 7.0, 0.01 M 2-mercaptoethanol, 0.01 M magnesium acetate, or as an ammonium sulfate precipitate, 2 months without significant loss of activity

Salmonella enterica subsp. enterica serovar Typhimurium

22°C, 20 mM Bis-Tris pH 6.6, 50 mM NaCl, 2 mM dithiothreitol, several weeks, without loss of activity or precipitation

D0ZJ57;

22°C, 20 mM sodium acetate, 150 mM sodium chloride, 2 mM dithiothreitol, pH 5.0, several months, minimal loss of activity

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8 entries

; recombinant PTH, heat, ammonium sulfate, Superdex 75, HI-Propyl, SP-Sepharose; recomninant PTH from Escherichia coli strain XL 1-Blue 8500fold by ultracentrifugation, heat treatment, ammonium sulfate fractionation, gel filtration, hydrophobic interaction chromatography, and ion exchange chromatography to homogeneity

ammonium sulfate precipitation

HisTrap column chromatography, Ni-NTA agarose column chromatography, and Q Sepharose column chromatography

Thermus thermophilus

728907

HisTrap nickel affinity column chromatography and Superdex 75 gel filtration

Ni-chelating column chromatography

Ni-NTA affinity resin column chromatography and Superdex G50 gel filtration

Acinetobacter baumannii

D0C9L6;

730738

Ni-NTA column chromatography and Superdex G-75 gel filtration

Salmonella enterica subsp. enterica serovar Typhimurium

Ni2+-chelating affinity column chromatography and Superose 12 gel filtration

D0ZJ57;

partial

recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography

recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis

677362

recombinant His-tagged Pth

recombinant Pth

Super Q Toyopearl 650M column chromatography, Resource Q column chromatography, and Superdex 75 gel filtration

O74017;

690236

wild-type and mutant enzymes

664102

wild-type and mutant enzymes N10A, H20A, M67A, F66A, D93A, H113A, K142A

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expressed as GST-fusion protein in Escherichia coli Rosetta pLysS (GST later cleaved), or in human HEK293T cells as FLAG-tagged protein

Pseudomonas syringae pv. tomato

Q14197;

708331

expressed in Escherichia coli BL21 (DE3) pMGK cells with eight nonnative residues at the C-terminus (LEHHHHHH) to facilitate protein purification

Q885L4;

710503

expressed in Escherichia coli BL21 pLysS cells

Salmonella enterica subsp. enterica serovar Typhimurium

D0ZJ57;

expressed in Escherichia coli BL21(DE3) cells

expressed in Escherichia coli BL21(DE3)pLysS cells

expressed in Escherichia coli BL21(lambdaDE3) cells

expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL cells

O74017;

690236

expressed in Escherichia coli strain K37DELTArecAlambdaDE3

expression in Escherichia coli

6 entries

expression in Escherichia coli; full length human Pth2 clone as tempolate , subcloned into the NcoI/BamHI sites of the pET15b bacterial expression vector. The ligated plasmid is transfoirmed into Escherichia coli BL21(DE3) strain

Q9Y3E5;

648110

expression in Escherichia coli; gene SS00175, DNA and amino acid sequence determination and analysis, complementation of an enzyme-deficient Escherichia coli mutant strain, and of two Saccharomyces cerevisiae gene YHR189w or YBL057c disruption mutants, overview, expression of PTH in Escherichia coli strain XL 1-Blue

gene pth, orf Rv1014c, DNA and amino acid sequence determination and analysis, expression of wild-type and mutant C-terminally His-tagged enzymes in Escherichia coli strain BL21(DE3) and in Escherichia coli thermosensitive strain AA7852, the mutant strain is able to grow at the nonpermissive temperature of 42°C, at 39°C, overexpression of MtPth in AA7852 cells allowed the cells to remain viable in the presence of up to 200 mg/ml erythromycin, overview

gene pth, orf Rv1014c, DNA and amino acid sequence determination, expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)

677362

pth2 gene, expression in Escherichia coli

Q980V1;

678132

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D93A

turnover-number is 0.1% of the turnover-number for wild-type enzyme, Km-value for diacetyl-Lys-tRNALys is 1.67fold higher than the Km-value for the wild-type enzyme

D93N

4% of wild-type kcat

F66A

turnover-number is 26% of the turnover-number for wild-type enzyme, Km-value for diacetyl-Lys-tRNALys is 1.15fold higher than the Km-value for the wild-type enzyme

H113A

turnover-number is 33% of the turnover-number for wild-type enzyme, Km-value for diacetyl-Lys-tRNALys is 1.46fold higher than the Km-value for the wild-type enzyme

H188A

the mutation results in a 5.4fold decrease in the kcat/Km value compared to the wild type enzyme

H20A

H20N

no activity

H20Q

no activity

K103Q

54% of wild-type kcat

K103R

68% of wild-type kcat

K103S

28% of wild-type kcat

K105Q

20% of wild-type kcat

K105R

26% of wild-type kcat

K105S

16% of wild-type kcat

K113Q

98% of wild-type kacat

K142A

turnover-number is 24% of the turnover-number for wild-type enzyme, Km-value for diacetyl-Lys-tRNALys is 4fold higher than the Km-value for the wild-type enzyme

M67A

turnover-number is 4.7% of the turnover-number for wild-type enzyme, Km-value for diacetyl-Lys-tRNALys is 70% of the Km-value for the wild-type enzyme

M67E

0.5% of wild-type kcat

N10A

N10D

N185A

the mutation results in a 5.7fold decrease in the kcat/Km value compared to the wild type enzyme

N185A/H188A

the mutation results in a 7.7fold decrease in the kcat/Km value compared to the wild type enzyme

C166A

site-directed mutagenesis, the mutant effectively complements the enzyme-defective thermosensitive Escherichia coli mutant strain AA7852 for growth at 42°C

C67S

site-directed mutagenesis, the mutant effectively complements the enzyme-defective thermosensitive Escherichia coli mutant strain AA7852 for growth at 42°C

D95N

site-directed mutagenesis, the catalytic residue mutant is not able to complement the enzyme-defective thermosensitive Escherichia coli mutant strain AA7852 for growth at 42°C

H22N

site-directed mutagenesis, the catalytic residue mutant is not able to complement the enzyme-defective thermosensitive Escherichia coli mutant strain AA7852 for growth at 42°C; site-directed mutagenesis, the mutation affects the enzyme structure, overview

N12D

site-directed mutagenesis, the catalytic residue mutant is not able to complement the enzyme-defective thermosensitive Escherichia coli mutant strain AA7852 for growth at 42°C

C166A

site-directed mutagenesis, the mutant effectively complements the enzyme-defective thermosensitive Escherichia coli mutant strain AA7852 for growth at 42°C

C67S

site-directed mutagenesis, the mutant effectively complements the enzyme-defective thermosensitive Escherichia coli mutant strain AA7852 for growth at 42°C

D95N

site-directed mutagenesis, the catalytic residue mutant is not able to complement the enzyme-defective thermosensitive Escherichia coli mutant strain AA7852 for growth at 42°C

H22N

C703A

mutation abolishes editing activity

D86A