Information on EC 3.1.1.29 - aminoacyl-tRNA hydrolase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota

EC NUMBER
COMMENTARY
3.1.1.29
-
RECOMMENDED NAME
GeneOntology No.
aminoacyl-tRNA hydrolase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
-
N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA
show the reaction diagram
residues K18, D86, and T90 are essential for catalytic activity, they are located in the N-part of alpha1 and in the beta3-beta4 loop. K18 and D86, which form a salt bridge, might play a role in the catalysis thanks to their acid and basic functions, whereas the OH group of T90 could act as a nucleophile
N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA
show the reaction diagram
structure-function relationship, residues Asp95 and His115 are involved in catalysis, overview
N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA
show the reaction diagram
reaction mechanism, active-site residues N10, H20 and D93 are crucial for catalysis
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-asparagine biosynthesis III (tRNA-dependent)
-
-
L-cysteine biosynthesis II (tRNA-dependent)
-
-
SYSTEMATIC NAME
IUBMB Comments
aminoacyl-tRNA aminoacylhydrolase
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
alanyl-tRNA editing protein AlaX-M
-
AlaX-M trans-editing enzyme
-
aminoacyl-transfer ribonucleate hydrolase
-
-
-
-
hydrolase, aminoacyl-transfer ribonucleate
-
-
-
-
ICT1
immature colon carcinoma transcript-1 with PTH activity
N-substituted aminoacyl transfer RNA hydrolase
-
-
-
-
peptidyl-tRNA hydrolase
-
-
-
-
peptidyl-tRNA hydrolase
-
-
peptidyl-tRNA hydrolase
-
peptidyl-tRNA hydrolase
-
-
peptidyl-tRNA hydrolase
-
peptidyl-tRNA hydrolase
-
-
peptidyl-tRNA hydrolase
-
peptidyl-tRNA hydrolase
-
peptidyl-tRNA hydrolase
-
-
peptidyl-tRNA hydrolase
-
peptidyl-tRNA hydrolase
-
;
-
peptidyl-tRNA hydrolase
-
-
peptidyl-tRNA hydrolase
-
peptidyl-tRNA hydrolase
-
peptidyl-tRNA hydrolase
-
peptidyl-tRNA hydrolase
Pyrococcus horikoshii OT-3
-
-
peptidyl-tRNA hydrolase
Salmonella enterica subsp. enterica serovar Typhimurium 14028s
D0ZJ57
-
-
peptidyl-tRNA hydrolase
-
-
peptidyl-tRNA hydrolase
-
peptidyl-tRNA hydrolase
-
-
peptidyl-tRNA hydrolase
-
-
-
peptidyl-tRNA hydrolase
-
-
peptidyl-tRNA hydrolase 1
-
-
peptidyl-tRNA hydrolase 1
-
-
-
peptidyl-tRNA hydrolase 2
-
-
PH1539
locus name
PH1539
Pyrococcus horikoshii OT-3
locus name
-
PTH
-
-
-
-
Pth1
Salmonella enterica subsp. enterica serovar Typhimurium 14028s
D0ZJ57
-
-
SSO0175
-
locus name
SSO0175
-
locus name
-
yHR189W
-
open reading frame on chromosome VIII
CAS REGISTRY NUMBER
COMMENTARY
9054-98-2
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
essential gene required for both vegetative growth and sporulation
-
-
Manually annotated by BRENDA team
construction of a bacterial strain overexpressing the enzyme
-
-
Manually annotated by BRENDA team
essential gene
-
-
Manually annotated by BRENDA team
MRE 600
-
-
Manually annotated by BRENDA team
mutant strain AA7852 with temperature-sensitive Pth, gene pthTs
-
-
Manually annotated by BRENDA team
mutant strain with temperature-sensitive Pth, gene pth
-
-
Manually annotated by BRENDA team
wild-type and mutant enzymes N10A, H20A, M67A, F66A, D93A, H113A, K142A
UniProt
Manually annotated by BRENDA team
Escherichia coli MRE 600
MRE 600
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
colon carcinoma HeLa cells
UniProt
Manually annotated by BRENDA team
strain H37Rv, gene pth, orf Rv1014c
-
-
Manually annotated by BRENDA team
strain H37Rv, gene pth, orf Rv1014c
Uniprot
Manually annotated by BRENDA team
strain H37Rv, gene pth, orf Rv1014c
-
-
Manually annotated by BRENDA team
strain H37Rv, gene pth, orf Rv1014c
Uniprot
Manually annotated by BRENDA team
strain OT3
SwissProt
Manually annotated by BRENDA team
Pyrococcus horikoshii OT-3
-
SwissProt
Manually annotated by BRENDA team
Pyrococcus horikoshii OT-3
strain OT3
SwissProt
Manually annotated by BRENDA team
Rattus norvegicus Wistar
Wistar
-
-
Manually annotated by BRENDA team
YHR189w and YBL057c gene products
-
-
Manually annotated by BRENDA team
Salmonella enterica subsp. enterica serovar Typhimurium 14028s
-
D0ZJ57
UniProt
Manually annotated by BRENDA team
; gene SSO0175
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
since build-up of peptidyl-tRNAs is toxic, defects in enzyme function result in cell death
physiological function
ICT1 is a member of the large mitoribosomal subunit: it behaves as an integral member of the 39S mt-LSU and a component of the intact 55S monosome
physiological function
-
azithromycin stationary-phase killing is decreased in enzyme-overexpressing Pseudomonas aeruginosa cells. Overexpressing the enzyme counteracts the azithromycin-mediated effect on rhamnolipid production and partially restores swarming activity
physiological function
-
peptidyl-tRNA hydrolase is an essential enzyme which acts as one of the rescue factors of the stalled ribosomes. This enzyme is required for rapid clearing of the peptidyl-tRNAs, the accumulation of which in the cell leads to cell death
physiological function
peptidyl-tRNA hydrolase is an essential enzyme which acts as one of the rescue factors of the stalled ribosomes. This enzyme is required for rapid clearing of the peptidyl-tRNAs, the accumulation of which in the cell leads to cell death
physiological function
-
peptidyl-tRNA hydrolase is an essential enzyme which acts as one of the rescue factors of the stalled ribosomes. This enzyme is required for rapid clearing of the peptidyl-tRNAs, the accumulation of which in the cell leads to cell death
physiological function
peptidyl-tRNA hydrolase is an essential enzymewhich acts as one of the rescue factors of the stalled ribosomes. This enzyme is required for rapid clearing of the peptidyl-tRNAs, the accumulation of which in the cell leads to cell death
physiological function
-
peptidyl-tRNA hydrolase is an essential enzyme which acts as one of the rescue factors of the stalled ribosomes. This enzyme is required for rapid clearing of the peptidyl-tRNAs, the accumulation of which in the cell leads to cell death
physiological function
-
isoform Pth4 can help recycling stalled ribosomes. High dosage of isoform Pth4 can compensate for the absence of the ribosomal release factor Mrf1
physiological function
-
the enzyme removes the peptide portion from peptidyl-tRNA, returning free tRNAs to participate in translation
physiological function
Pyrococcus horikoshii OT-3
-
peptidyl-tRNA hydrolase is an essential enzymewhich acts as one of the rescue factors of the stalled ribosomes. This enzyme is required for rapid clearing of the peptidyl-tRNAs, the accumulation of which in the cell leads to cell death
-
physiological function
-
peptidyl-tRNA hydrolase is an essential enzyme which acts as one of the rescue factors of the stalled ribosomes. This enzyme is required for rapid clearing of the peptidyl-tRNAs, the accumulation of which in the cell leads to cell death
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'(3')-O-L-(N,N-diacetyl-lysinyl)adenosine + H2O
?
show the reaction diagram
minimalist substrate
-
-
?
acetyl-histidine-tRNA + H2O
acetyl-histidine + tRNA
show the reaction diagram
-
-
-
?
acetyl-histidyl-tRNAHis + H2O
acetyl-histidine + tRNAHis
show the reaction diagram
-
-
-
?
Ala-tRNA + H2O
Ala + tRNA
show the reaction diagram
-
-
-
?
bulk peptidyl-tRNA + H2O
?
show the reaction diagram
-
-
-
-
?
D-tyrosine-tRNA + H2O
D-tyrosine + tRNA
show the reaction diagram
-
-
-
?
dephosphorylated diacetyl-lysine-tRNA + H2O
dephosphorylated diacetyl-lysine + tRNA
show the reaction diagram
-
-
-
?
dephosporylated formyl-methionine-tRNA + H2O
dephosphorylated formyl-methionine + tRNA
show the reaction diagram
-
-
-
?
diacetyl-Lys-tRNALys + H2O
diacetyl-Lys + tRNA
show the reaction diagram
-
-
?
diacetyl-Lys-tRNALys + H2O
diacetyl-Lys + tRNA
show the reaction diagram
-
-
-
?
diacetyl-Lys-tRNALys + H2O
diacetyl-Lys + tRNA
show the reaction diagram
-
-
-
?
diacetyl-Lys-tRNALys + H2O
diacetyl-Lys + tRNA
show the reaction diagram
-
-
?
diacetyl-Lys-tRNALys + H2O
diacetyl-Lys + tRNA
show the reaction diagram
-
diacetyl-Lys-tRNALys from E. coli
-
?
diacetyl-lysine-tRNA + H2O
diacetyl-lysine + tRNA
show the reaction diagram
-
-
-
?
diacetyl-lysine-tRNA + H2O
diacetyl-lysine + tRNA
show the reaction diagram
-
-
-
?
diacetyl-lysine-tRNA + H2O
diacetyl-lysine + tRNA
show the reaction diagram
-
-
-
?
diacetyl-lysine-tRNA + H2O
diacetyl-lysine + tRNA
show the reaction diagram
-
-
-
?
diacetyl-lysine-tRNA + H2O
diacetyl-lysine + tRNA
show the reaction diagram
-
-
-
?
diacetyl-lysine-tRNA + H2O
diacetyl-lysine + tRNA
show the reaction diagram
-
-
?
diacetyl-lysine-tRNA + H2O
diacetyl-lysine + tRNA
show the reaction diagram
-
-
?
diacetyl-lysyl-tRNALys
diacetyl-Lys + tRNALys
show the reaction diagram
-
-
-
?
diacetyl-lysyl-tRNALys + H2O
diacetyl-lysine + tRNALys
show the reaction diagram
-
-
-
?
diacetyl-lysyl-tRNALys + H2O
diacetyl-lysine + tRNALys
show the reaction diagram
-
Escherichia coli diacetyl-lysyl-tRNALys, phosphorylated and dephosphorylated substrate
-
?
diacetyl-lysyl-tRNALys + H2O
diacetyl-lysine + tRNALys
show the reaction diagram
diacetyl-lysyl-tRNALys is hydrolyzed by the wild type enzyme 360fold more efficiently than Lys-tRNALys
-
?
diacetyl-lysyl-tRNALys + H2O
diacetyl-lysine + tRNALys
show the reaction diagram
-
-
-
?
formyl-Met-tRNAfMet + H2O
formyl-Met + tRNAfMet
show the reaction diagram
-
-
-
?
formyl-methionine-tRNA + H2O
formyl-methionine + tRNA
show the reaction diagram
-
-
-
?
formyl-methionyl-tRNAfMet + H2O
formyl-methionine + tRNAfMet
show the reaction diagram
-
Escherichia coli formyl-methionyltRNAfMet, phosphorylated and dephosphorylated substrate
-
?
Glu-tRNA + H2O
Glu + tRNA
show the reaction diagram
-
-
-
?
Gly-tRNA + H2O
Gly + tRNA
show the reaction diagram
-
-
-
?
Gly-tRNAAla + H2O
Gly + tRNAAla
show the reaction diagram
-
-
?
L-Lys-tRNALys + H2O
L-lysine + tRNALys
show the reaction diagram
-
-
?
Leu-tRNA + H2O
Leu + tRNA
show the reaction diagram
-
-
-
?
Leu-tRNA + H2O
Leu + tRNA
show the reaction diagram
-
-
-
?
Lys-tRNA + H2O
Lys + tRNA
show the reaction diagram
-
-
-
?
Lys-tRNA + H2O
Lys + tRNA
show the reaction diagram
-
-
-
?
Met-tRNA + H2O
Met + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-Ala-tRNA + H2O
N-acetyl-Ala + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-Ala-tRNA(Ala) + H2O
N-acetyl-Ala + tRNA(Ala)
show the reaction diagram
-
-
-
?
N-acetyl-Glu-tRNA + H2O
N-acetyl-Glu + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-His-tRNA + H2O
N-acetyl-His + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-Leu-Gly-tRNA + H2O
N-acetyl-Leu-Gly + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-Leu-tRNA + H2O
N-acetyl-Leu + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-Leu-tRNA + H2O
N-acetyl-Leu + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-Leu-tRNA + H2O
N-acetyl-Leu + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-Leu-tRNA + H2O
N-acetyl-Leu + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-Leu-tRNA + H2O
N-acetyl-Leu + tRNA
show the reaction diagram
Escherichia coli MRE 600
-
-
-
?
N-acetyl-Lys-tRNA + H2O
N-acetyl-Lys + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-Lys-tRNA + H2O
N-acetyl-Lys + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-Lys-tRNA + H2O
N-acetyl-Lys + tRNA
show the reaction diagram
-
-
?
N-acetyl-Lys-tRNA + H2O
N-acetyl-Lys + tRNA
show the reaction diagram
-
-
?
N-acetyl-Met-tRNA + H2O
N-acetyl-Met + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-Phe-Phe-tRNA + H2O
N-acetyl-Phe-Phe + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-Phe-tRNA + H2O
N-acetyl-Phe + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-Phe-tRNA + H2O
N-acetyl-Phe + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-Phe-tRNA + H2O
N-acetyl-Phe + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-Phe-tRNA + H2O
N-acetyl-Phe + tRNA
show the reaction diagram
-
enzyme with broad specificity
-
?
N-acetyl-Phe-tRNA + H2O
N-acetyl-Phe + tRNA
show the reaction diagram
-
enzyme with broad specificity
-
?
N-acetyl-Phe-tRNA + H2O
N-acetyl-Phe + tRNA
show the reaction diagram
-
enzyme from encysted embryos is specific for acetyl-Phe-tRNA
-
?
N-acetyl-Phe-tRNA + H2O
N-acetyl-Phe + tRNA
show the reaction diagram
Escherichia coli MRE 600
-
enzyme with broad specificity
-
?
N-acetyl-Phe-tRNA + H2O
N-acetyl-L-Phe + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-Phe-Val-tRNA + H2O
N-acetyl-Phe-Val + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-Ser-tRNA + H2O
N-acetyl-Ser + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-Ser-tRNA + H2O
N-acetyl-Ser + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-Trp-tRNA + H2O
N-acetyl-Trp + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-Tyr-tRNA + H2O
N-acetyl-Tyr + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-Val-tRNA + H2O
N-acetyl-Val + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-Val-tRNA + H2O
N-acetyl-Val + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-Val-tRNA + H2O
N-acetyl-Val + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-Val-tRNA + H2O
N-acetyl-Val + tRNA
show the reaction diagram
-
-
-
?
N-acetyl-Val-tRNA + H2O
N-acetyl-Val + tRNA
show the reaction diagram
Escherichia coli MRE 600
-
-
-
?
N-benzoyl-Gly-Gly-Phe-tRNA + H2O
N-benzoyl-Gly-Gly-Phe + tRNA
show the reaction diagram
-
-
-
?
N-benzoyl-Gly-GlyGly-Phe-tRNA + H2O
N-benzoyl-Gly-Gly-Gly-Phe + tRNA
show the reaction diagram
-
-
-
?
N-carbobenzyloxy-Phe-tRNA + H2O
N-carbobenzyloxy-Phe + tRNA
show the reaction diagram
-
-
-
?
N-formyl-Val-tRNA + H2O
N-formyl-Val + tRNA
show the reaction diagram
Escherichia coli, Escherichia coli MRE 600
-
reaction at a lower rate than with the N-acetyl derivative
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
the enzyme or an element directly controlled by the enzyme, is the target for the lethal effect by bacterophage lambda
-
-
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
Pth recycles N-acetyl-aminoacyl tRNAs and peptidyl-tRNAs by cleaving the ester bond between tRNA and peptide
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
Pyrococcus horikoshii OT-3
-
-
?
oligolysyl-tRNA + H2O
oligo-Lys + tRNA
show the reaction diagram
-
-
-
?
Oregon Green-methionine-tRNA + H2O
Oregon Green-methionine + tRNA
show the reaction diagram
-
-
-
?
peptidyl-tRNA + H2O
peptide + tRNA
show the reaction diagram
peptidyl-tRNA hydrolase cleaves the ester bond between tRNA and the attached peptide in peptidyl-tRNA in order to avoid the toxicity resulting from its accumulation and to free the tRNA available for further rounds in protein synthesis
-
?
peptidyl-tRNA + H2O
?
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium 14028s
D0ZJ57
-
-
-
?
peptidyl-tRNAL + H2O
peptide + tRNA
show the reaction diagram
-
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
-
?
peptidyl-tRNAL + H2O
peptide + tRNA
show the reaction diagram
cleavage of the ester bond between tRNA and the attached peptide in peptidyl-tRNA, substrate binding channel structure, overview
-
?
peptidyl-tRNAL + H2O
peptide + tRNA
show the reaction diagram
-
Pth prefers substrates with two or more peptide bonds compared to those with a single peptide bond
-
?
peptidyl-tRNALys + H2O
peptide + tRNALys
show the reaction diagram
-
accumulation of peptidyl-tRNA due to enzyme misfunction is toxic to the cells, overproduction of tRNALys suppresses the effects of pthTs mutation at 41C but not at 43C, and increases the levels of aminoacyl-tRNA
-
?
Phe-Phe-tRNA + H2O
Phe-Phe + tRNA
show the reaction diagram
-
-
-
?
Phe-tRNA + H2O
Phe + tRNA
show the reaction diagram
-
-
-
?
Phe-tRNA + H2O
Phe + tRNA
show the reaction diagram
-
-
-
?
phenyllactyl-Phe-tRNA + H2O
phenyllactyl-Phe + tRNA
show the reaction diagram
-
-
-
?
poly-Val-tRNA + H2O
poly-Val + tRNA
show the reaction diagram
-
-
-
?
Ser-tRNA + H2O
Ser + tRNA
show the reaction diagram
-
-
-
?
Ser-tRNA + H2O
Ser + tRNA
show the reaction diagram
-
-
-
?
Ser-tRNAAla + H2O
Ser + tRNAAla
show the reaction diagram
-
-
?
Tyr-tRNA + H2O
Tyr + tRNA
show the reaction diagram
-
-
-
?
Val-tRNA + H2O
Val + tRNA
show the reaction diagram
-
-
-
?
Val-tRNA + H2O
Val + tRNA
show the reaction diagram
-
-
-
?
Val-tRNAVal + H2O
Val + tRNAVal
show the reaction diagram
-
-
-
?
Met-tRNAMet + H2O
Met + tRNAMet
show the reaction diagram
-
-
-
?
additional information
?
-
-
very slow hydrolysis of denatured N-acetyl-aminoacyl-tRNA, no hydrolysis of partly deaminated N-acetyl-Val-tRNA
-
-
-
additional information
?
-
-
enzyme shows species specificity. Aminoacyl-tRNAs in which the tRNA comes from eucaryotes are equally efficient as substrates of the enzyme, when tRNA comes from procaryotic organisms it is hydrolyzed 40% less efficiently
-
-
-
additional information
?
-
-
N-acetyl-Val-adenosine is not a substrate, N-acetyl-Val-oligonucleotide is hydrolyzed very slowly. The specificity for the tRNA moiety does not seem to be directed towards a particular species of organism
-
-
-
additional information
?
-
-
derivatives of tRNAMetf with various combinations of bases at position 1 and 72 in the acceptor stem have been produced, aminoacylated and chemically acetylated. TrNAmetd derivatives with either C1A72, c1C72, U1G72, U1C72 or A1C72 behave as poor substrates of the enzyme compared to those with C1G72, U1A72, G1C72, A1U72 or G1U72
-
-
-
additional information
?
-
-
the enzyme plays a central role and is indispensable in Escherichia coli
-
-
-
additional information
?
-
-
genetic interactions and the mechanism of peptidyl-tRNA drop-off of translating ribosomes leading to accumutaion of peptidyl-tRNA, overview
-
-
-
additional information
?
-
-
the enzyme and its conserved active-site residues N12, H22 and D95 are essential for the viability of the bacteria
-
-
-
additional information
?
-
-
the enzyme salvages tRNA from peptidyl-tRNA by hydrolyzing the ester link between the peptide and the 2'-or 3'-OH of the sugar at the end of tRNA, since accumulation of peptidyl-tRNA, due to drop-off of translating ribosomes, is toxic to the cell, overview
-
-
-
additional information
?
-
-
the enzyme is involved in the recycling of peptidyl-tRNA, it shows poor D-aminoacyl-tRNA hydrolysis
-
-
-
additional information
?
-
no activity with N-formyl-methionyl-tRNA
-
-
-
additional information
?
-
no activity with N-formyl-methionyl-tRNA
-
-
-
additional information
?
-
Escherichia coli MRE 600
-
very slow hydrolysis of denatured N-acetyl-aminoacyl-tRNA, no hydrolysis of partly deaminated N-acetyl-Val-tRNA
-
-
-
additional information
?
-
-
the enzyme salvages tRNA from peptidyl-tRNA by hydrolyzing the ester link between the peptide and the 2'-or 3'-OH of the sugar at the end of tRNA, since accumulation of peptidyl-tRNA, due to drop-off of translating ribosomes, is toxic to the cell, overview
-
-
-
additional information
?
-
-
the enzyme and its conserved active-site residues N12, H22 and D95 are essential for the viability of the bacteria
-
-
-
additional information
?
-
-
no activity with N-formyl-methionyl-tRNA
-
-
-
additional information
?
-
Pyrococcus horikoshii OT-3
no activity with N-formyl-methionyl-tRNA
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
diacetyl-lysyl-tRNALys + H2O
diacetyl-lysine + tRNALys
show the reaction diagram
-
-
-
?
diacetyl-lysyl-tRNALys + H2O
diacetyl-lysine + tRNALys
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
Q9Y3E5
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
Q6YP15
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
P9WHN7
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
O74017
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
D0C9L6
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
Q60363
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
the enzyme or an element directly controlled by the enzyme, is the target for the lethal effect by bacterophage lambda
-
-
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
Pth recycles N-acetyl-aminoacyl tRNAs and peptidyl-tRNAs by cleaving the ester bond between tRNA and peptide
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
Pyrococcus horikoshii OT-3
O74017
-
-
?
peptidyl-tRNA + H2O
peptide + tRNA
show the reaction diagram
P9WHN7
peptidyl-tRNA hydrolase cleaves the ester bond between tRNA and the attached peptide in peptidyl-tRNA in order to avoid the toxicity resulting from its accumulation and to free the tRNA available for further rounds in protein synthesis
-
?
peptidyl-tRNAL + H2O
peptide + tRNA
show the reaction diagram
-
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
-
?
peptidyl-tRNALys + H2O
peptide + tRNALys
show the reaction diagram
-
accumulation of peptidyl-tRNA due to enzyme misfunction is toxic to the cells, overproduction of tRNALys suppresses the effects of pthTs mutation at 41C but not at 43C, and increases the levels of aminoacyl-tRNA
-
?
diacetyl-lysyl-tRNALys + H2O
diacetyl-lysine + tRNALys
show the reaction diagram
-
-
-
?
additional information
?
-
-
the enzyme plays a central role and is indispensable in Escherichia coli
-
-
-
additional information
?
-
-
genetic interactions and the mechanism of peptidyl-tRNA drop-off of translating ribosomes leading to accumutaion of peptidyl-tRNA, overview
-
-
-
additional information
?
-
-
the enzyme and its conserved active-site residues N12, H22 and D95 are essential for the viability of the bacteria
-
-
-
additional information
?
-
-
the enzyme salvages tRNA from peptidyl-tRNA by hydrolyzing the ester link between the peptide and the 2'-or 3'-OH of the sugar at the end of tRNA, since accumulation of peptidyl-tRNA, due to drop-off of translating ribosomes, is toxic to the cell, overview
-
-
-
additional information
?
-
-
the enzyme and its conserved active-site residues N12, H22 and D95 are essential for the viability of the bacteria
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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+
-
0.001-0.01 MgCl2 activates
Mg2+
-
40 mM MgCl2, about 88fold activation; activates about 80fold, optimally at 40 mM
Mg2+
-
the enzyme is maximally active in presence of divalent cations, Mg2+ or Mn2+. Maximal activity with 20 mM Mg2+
Mg2+
-
maximal activity is obtained with 20 mM Mg2+ or Mn2+
Mg2+
maximal activity at 5 mM
MgCl2
-
40 mM, approx. 88fold activation
Mn2+
-
the enzyme is maximally active in presence of divalent cations, Mg2+ or Mn2+. Maximal activity with 2.5 mM, 50% of the activation with Mg2+
Mn2+
-
maximal activity is obtained with 20 mM Mg2+ or Mn2+
Mn2+
-
the enzyme almost completely inactive in absence of divalent cations. Mn2+ is partly effective, optimal concentration is about 0.2-0.5 mM
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3'-deoxy-N[(O-methyl-L-tyrosyl)amino]adenosine
-
-
3'-L-(N,N-diacetyl-lysinyl)amino-3'-deoxyadenosine
-
-
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
-
deacetylated tRNA
-
-
-
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
-
5 mM, complete inhibition
EDTA
-
5 mM, complete inhibition
non-esterified tRNALys
-
-
-
tRNA
-
uncharged yeast tRNA, competitive
tRNA
-
unfractionated Escherichia coli tRNA; unfractionated from Escherichia coli
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
spermidine
-
0.1 mM spermidine HCl, 73fold activation
spermidine-HCl
-
0.1 mM, 73fold activation; activates about 80fold, optimally at 0.1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000016
acetyl-His-tRNAHis
-
pH 7.5, 50C
0.000016
acetyl-histidyl-tRNA
-
50C, pH 7.5
0.000016
acetyl-histidyl-tRNAHis
-
pH 7.5, 50C, recombinant enzyme
0.008
bulk peptidyl-tRNA
-
at pH 5.0 and 25C
-
0.000003
dephosphorylated diacyl-lysine-tRNA
-
50C, pH 7.5
-
0.00003
dephosphorylated formyl-methioninyl-tRNA
-
50C, pH 7.5
-
0.0000028
diacetyl-Lys-tRNALys
-
pH 7.5, 50C, dephosphorylated diacetyl-Lys-tRNALys
-
0.000011
diacetyl-Lys-tRNALys
-
pH 7.5, 50C
-
0.0041
diacetyl-Lys-tRNALys
pH 7.5, 28C, mutant enzyme M67A
-
0.006
diacetyl-Lys-tRNALys
pH 7.5, 28C, wild-type enzyme
-
0.0066
diacetyl-Lys-tRNALys
pH 7.5, 28C, mutant enzyme N10A
-
0.0069
diacetyl-Lys-tRNALys
pH 7.5, 28C, mutant enzyme F66A
-
0.0088
diacetyl-Lys-tRNALys
pH 7.5, 28C, mutant enzyme H113A
-
0.01
diacetyl-Lys-tRNALys
pH 7.5, 28C, mutant enzyme D93A
-
0.024
diacetyl-Lys-tRNALys
pH 7.5, 28C, 5'-dephosphoylated diacetyl-Lys-tRNALys, wild-type enzyme
-
0.000011
diacetyl-lysine-tRNA
-
27C, pH 7.5
-
0.000011
diacetyl-lysine-tRNA
-
50C, pH 7.5
-
0.00022
diacetyl-lysine-tRNA
27C, pH 7.5
-
0.0028
diacetyl-lysine-tRNA
23-24C, pH 7.2
-
0.006
diacetyl-lysine-tRNA
-
27C, pH 7.5
-
0.0000028
diacetyl-lysyl-tRNALys
-
dephosphorylated substrate, pH 7.5, 50C, recombinant enzyme
0.000011
diacetyl-lysyl-tRNALys
-
pH 7.5, 50C, recombinant enzyme
0.0007
diacetyl-lysyl-tRNALys
-
-
0.9
diacetyl-lysyl-tRNALys
-
pH 7.5, 50C, mutant enzyme T98A
1.6
diacetyl-lysyl-tRNALys
-
pH 7.5, 50C, mutant enzyme Q22A
2.9
diacetyl-lysyl-tRNALys
-
pH 7.5, 50C, mutant enzyme Q54A
3.2
diacetyl-lysyl-tRNALys
-
pH 7.5, 50C, mutant enzyme K56A
4.4
diacetyl-lysyl-tRNALys
-
pH 7.5, 50C, mutant enzyme H25A
5.3
diacetyl-lysyl-tRNALys
-
pH 7.5, 50C, mutant enzyme K18A
5.4
diacetyl-lysyl-tRNALys
-
pH 7.5, 50C, mutant enzyme D86A
6.7
diacetyl-lysyl-tRNALys
-
pH 7.5, 50C, mutant enzyme D86A/K18A
7.2
diacetyl-lysyl-tRNALys
-
pH 7.5, 50C, mutant enzyme T90A
9.1
diacetyl-lysyl-tRNALys
-
pH 7.5, 50C, wild-type enzyme
12.8
diacetyl-lysyl-tRNALys
-
pH 7.5, 50C, mutant enzyme K118A
0.000012
formyl-Met-tRNAfMet
-
pH 7.5, 50C
0.00003
formyl-Met-tRNAfMet, dephosphorylated
-
pH 7.5, 50C, dephosphorylated formyl-Met-tRNAfMet
-
0.000012
formyl-methionyl-tRNA
-
50C, pH 7.5
0.000012
formyl-methionyl-tRNAfMet
-
pH 7.5, 50C, recombinant enzyme
0.00471
N-acetyl-Ala-tRNA(Ala)
-
wild type enzyme, in 20 mM HEPES-KOH (pH 7.6), 10 mM MgCl2, at 28C
-
0.0134
N-acetyl-Ala-tRNA(Ala)
-
mutant enzyme N185A, in 20 mM HEPES-KOH (pH 7.6), 10 mM MgCl2, at 28C
-
0.0171
N-acetyl-Ala-tRNA(Ala)
-
mutant enzyme H188A, in 20 mM HEPES-KOH (pH 7.6), 10 mM MgCl2, at 28C
-
0.0269
N-acetyl-Ala-tRNA(Ala)
-
mutant enzyme N185A/H188A, in 20 mM HEPES-KOH (pH 7.6), 10 mM MgCl2, at 28C
-
0.0022
N-acetyl-Met-tRNA
-
pH 7.0, 37C
0.0008
N-acetyl-Phe-tRNA
-
pH 7.5, 30C
0.000001
N-acetyl-phenylalanyl-tRNA
-
pH 7.0, 30C
0.0055
Oregon Green-methionine-tRNA
-
25C, pH 7.5
-
0.0008
Phe-tRNA
-
pH 7.5, 30C
0.00003
formyl-methionyl-tRNAfMet
-
dephosphorylated substrate, pH 7.5, 50C, recombinant enzyme
additional information
additional information
-
effect of mutations altering the 1-72 pair of E. coli tRNAMetf on the Km-value
-
additional information
additional information
-
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.4
acetyl-His-tRNA
Sulfolobus solfataricus
-
pH 7.5, 50C
3.4
acetyl-histidyl-tRNA
Sulfolobus solfataricus
-
50C, pH 7.5
3.4
acetyl-histidyl-tRNAHis
Sulfolobus solfataricus
-
pH 7.5, 50C, recombinant enzyme
0.86
dephosphorylated diacyl-lysine-tRNA
Sulfolobus solfataricus
-
50C, pH 7.5
-
6.08
dephosphorylated diacyl-lysine-tRNA
Sulfolobus solfataricus
-
50C, pH 7.5
-
3
dephosphorylated formyl-methioninyl-tRNA
Sulfolobus solfataricus
-
50C, pH 7.5
-
1.3
diacetyl-Lys-tRNA
Homo sapiens
Q9Y3E5
pH 7.5, 27C
0.028
diacetyl-Lys-tRNALys
Escherichia coli
P0A7D1
pH 7.5, 28C, mutant enzyme N10A
-
0.05
diacetyl-Lys-tRNALys
Escherichia coli
P0A7D1
pH 7.5, 28C, mutant enzyme D93A
-
0.17
diacetyl-Lys-tRNALys
Escherichia coli
P0A7D1
pH 7.5, 28C, mutant enzyme M67A
-
0.85
diacetyl-Lys-tRNALys
Escherichia coli
P0A7D1
pH 7.5, 28C, 5'-dephosphoylated diacetyl-Lys-tRNALys, wild-type enzyme
-
0.86
diacetyl-Lys-tRNALys
Sulfolobus solfataricus
-
pH 7.5, 50C, dephosphorylated diacetyl-Lys-tRNALys
-
0.9
diacetyl-Lys-tRNALys
Escherichia coli
P0A7D1
pH 7.5, 28C, mutant enzyme F66A
-
1.2
diacetyl-Lys-tRNALys
Escherichia coli
P0A7D1
pH 7.5, 28C, mutant enzyme H113A
-
1.8
diacetyl-Lys-tRNALys
Sulfolobus solfataricus
-
pH 7.5, 50C
-
3.6
diacetyl-Lys-tRNALys
Escherichia coli
P0A7D1
pH 7.5, 28C, wild-type enzyme
-
1.3
diacetyl-lysine-tRNA
Homo sapiens
Q9Y3E5
27C, pH 7.5
-
1.8
diacetyl-lysine-tRNA
Sulfolobus solfataricus
-
27C, pH 7.5
-
1.8
diacetyl-lysine-tRNA
Sulfolobus solfataricus
-
50C, pH 7.5
-
3.6
diacetyl-lysine-tRNA
Escherichia coli
-
27C, pH 7.5
-
0.002
diacetyl-lysyl-tRNALys
Sulfolobus solfataricus
-
pH 7.5, 50C, mutant enzyme D86A/K18A; pH 7.5, 50C, mutant enzyme K18A
0.0025
diacetyl-lysyl-tRNALys
Sulfolobus solfataricus
-
pH 7.5, 50C, mutant enzyme D86A
0.02
diacetyl-lysyl-tRNALys
Sulfolobus solfataricus
-
pH 7.5, 50C, mutant enzyme T90A
0.06
diacetyl-lysyl-tRNALys
Sulfolobus solfataricus
-
pH 7.5, 50C, mutant enzyme Q22A; pH 7.5, 50C, mutant enzyme T98A
0.07
diacetyl-lysyl-tRNALys
Sulfolobus solfataricus
-
pH 7.5, 50C, mutant enzyme K56A
0.1
diacetyl-lysyl-tRNALys
Sulfolobus solfataricus
-
pH 7.5, 50C, mutant enzyme H25A
0.27
diacetyl-lysyl-tRNALys
Sulfolobus solfataricus
-
pH 7.5, 50C, mutant enzyme Q54A
0.86
diacetyl-lysyl-tRNALys
Sulfolobus solfataricus
-
dephosphorylated substrate, pH 7.5, 50C, recombinant enzyme
1.22
diacetyl-lysyl-tRNALys
Mycobacterium tuberculosis
-
-
1.8
diacetyl-lysyl-tRNALys
Sulfolobus solfataricus
-
pH 7.5, 50C, recombinant enzyme
1.8
diacetyl-lysyl-tRNALys
Sulfolobus solfataricus
-
pH 7.5, 50C, wild-type enzyme
2.2
diacetyl-lysyl-tRNALys
Sulfolobus solfataricus
-
pH 7.5, 50C, mutant enzyme K118A
3
formyl-Met-tRNAfMet
Sulfolobus solfataricus
-
pH 7.5, 50C
3
formyl-methionyl-tRNA
Sulfolobus solfataricus
-
50C, pH 7.5
5.8
N-acetyl-Ala-tRNA(Ala)
Escherichia coli
-
mutant enzyme N185A, in 20 mM HEPES-KOH (pH 7.6), 10 mM MgCl2, at 28C
-
7.93
N-acetyl-Ala-tRNA(Ala)
Escherichia coli
-
mutant enzyme H188A, in 20 mM HEPES-KOH (pH 7.6), 10 mM MgCl2, at 28C
-
8.7
N-acetyl-Ala-tRNA(Ala)
Escherichia coli
-
mutant enzyme N185A/H188A, in 20 mM HEPES-KOH (pH 7.6), 10 mM MgCl2, at 28C
-
11.7
N-acetyl-Ala-tRNA(Ala)
Escherichia coli
-
wild type enzyme, in 20 mM HEPES-KOH (pH 7.6), 10 mM MgCl2, at 28C
-
0.7
N-acetyl-Met-tRNA
Escherichia coli
-
pH 7.0, 37C
3
o-hydroxycinnamic acid
Sulfolobus solfataricus
-
50C, pH 7.5
9.3
Oregon Green-methionine-tRNA
Escherichia coli
-
25C, pH 7.5
-
3
formyl-methionyl-tRNAfMet
Sulfolobus solfataricus
-
phosphorylated and dephosphorylated substrate, pH 7.5, 50C, recombinant enzyme
additional information
additional information
Escherichia coli
-
effect of mutations altering the 1-72 pair of E. coli tRNAMetf on the turnover-number
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.51
2'(3')-O-L-(N,N-diacetyl-lysinyl)adenosine
Escherichia coli
-
wild type enzyme, 28C, 20 mM Tris-HCl (pH 7.5), 10 mM MgCl2, 0.1 mM EDTA, 0.1 mM dithiothreitol
166174
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
12
3'-L-(N,N-diacetyl-lysinyl)amino-3'-deoxyadenosine
-
at pH 6.0, with 50 mM sodium acetate and 200 mM NaCl, at 28C
0.00005
non-esterified tRNALys
-
pH 7.5, 50C, recombinant enzyme
-
0.000095
tRNA
-
pH 7.5, 50C, unfractionated Escherichia coli tRNA; unfractionated tRNA from Escherichia coli, 50C, pH 7.5
0.0001
tRNA-formyl-methionine
-
tRNA-ormyl-methionine from Escherichia coli, 50C, pH 7.5
-
0.00005
tRNA-lysine
-
tRNA-lysine from Escherichia coli, 50C, pH 7.5
-
0.00011
tRNAfMet
-
pH 7.5, 50C, recombinant enzyme
0.00011
tRNAformylMet
-
pH 7.5, 50C, tRNAformylMet from Escherichia coli
-
0.00005
tRNALys
-
pH 7.5, 50C, tRNALys from Escherichia coli
0.0001
Uncharged tRNA
-
pH 7.5, 50C, recombinant enzyme
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0149
-
-
0.078
-
substrate D-tyrosyl-tRNA, 37C, pH 7.5
0.15
-
substrae D-tyrosyl-tRNA
4.14
-
; purified recombinant enzyme
30
-
substrate diacetyl-lysine-tRNA
31.8
-
substrate diacetyl-lysine tRNA, 37C, pH 7.5
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
N-acetyl-Val-tRNA or N-acetyl-Trp as substrate
7 - 7.5
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.5
approx. 38% at pH 6.0, approx. 20% of maximal activity at pH 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
paraproerythroblast, low activity
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
additional information
-
mutant strain AA7852 with temperature-sensitive Pth grown at 32C and at 41C
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
mitochondiral ribosome
Manually annotated by BRENDA team
-
firmly bound, not an integral part of the ribosomal subunit
Manually annotated by BRENDA team
mitochondiral ribosome
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Salmonella typhimurium (strain 14028s / SGSC 2262)
Streptococcus pyogenes serotype M49 (strain NZ131)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Vibrio cholerae serotype O1 (strain M66-2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12700
SDS-PAGE
710503
20460
calculated from amino acid sequence
693637
23000
SDS-PAGE
708331
25000
-
gel filtration; recombinant enzyme, gel filtration
648112
25000
gel filtration
721151
25300
dynamic light-scattering
690236
46000
-
gel filtration
648114
55000
-
gel filtration
648113
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 15000, SDS-PAGE
?
-
x * 12700, deduced from nucleotide sequence; x * 13500, SDS-PAGE
?
x * 23000, SDS-PAGE
?
-
x * 20455, sequence calculation
?
-
x * 21978, sequence calculation
?
x * 24000, SDS-PAGE
?
-
x * 20000, SDS-PAGE
?
-
x * 20455, sequence calculation; x * 21978, sequence calculation
-
?
Salmonella enterica subsp. enterica serovar Typhimurium 14028s
-
x * 25000, SDS-PAGE
-
dimer
-
2 * 13100, deduced from nucleotide sequence; 2 * 15000, recombinant enzyme, SDS-PAGE
dimer
crystal structure analysis, three-dimensional structure, each protomer is made of a mixed five-stranded beta-sheet surrounded by two groups of two alpha-helices, the dimer interface is mainly formed by van der Waals interactions between hydrophobic residues belonging to the two N-terminal R1 helices contributed by two protomers, overview
dimer
x-ray crystallography
monomer
1 * 20455, calculated from amino acid sequence
monomer
gel-filtration followed by a combination of static light scattering and refractive index
monomer
1 * 25300, calculated from sequence
monomer
-
1 * 21000, SDS-PAGE
monomer
Pyrococcus horikoshii OT-3, Sulfolobus solfataricus P2
-
-
-
additional information
-
3D fold based on NMR and a structural model based on the Escherichia coli Pth crystal structure are generated for Mycobacterium tuberculosis Pth, structure comparison, molecular modeling, construction of a model of structural changes associated with enzyme action on the basis of the plasticity of the molecule, overview
additional information
-
3D fold based on NMR and a structural model based on the Escherichia coli Pth crystal structure are generated for Mycobacterium tuberculosis Pth, structure comparison, molecular modeling, construction of a model of structural changes associated with enzyme action on the basis of the plasticity of the molecule, overview
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
crystal structure analysis
-
crystal structure at 1.3 A resolution
-
crystallization by using polyethylene glycol as precipitant, recombinant enzyme
-
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 20C
-
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
hanging drop vapor diffusion method, using 30% (w/v) PEG-1500 and 10% (v/v) isopropanol in 100 mM HEPES buffer, pH 6.5
-
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
purified recombinant enzyme, X-ray diffraction structure determination and analysis at 1.98 A, 2.35 A, and 2.49 A resolution, molecular replacement
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
-
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
hanging-drop vapour-diffusion method at 20C, crystal structure is determined at 2.7 A resolution
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
-
purified recombinant enzyme, hanging drop vapour diffusion method, 24C, 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
sitting drop vapor diffusion method, using 100 mM phosphate-citrate buffer pH 4.2, and 50% (w/v) 2-methyl-2,4-pentanediol
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7.5
-
4C, 24 h, stable
648113
6 - 8
-
30C, 30 min, stable
648114
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
-
10 min, 70% loss of activity
648114
50
-
10 min, 85% loss of activity
648113
52
-
stable up to
678535
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, 25C, overview
678535
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
urea/guanidinium chloride-induced unfolding curve for MtPth indicates a simple two-state unfolding process without any intermediates, pH 6.5, 25C
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10C, 50% glycerol, purified enzyme is stable for several months
-
22C, 20 mM sodium acetate, 150 mM sodium chloride, 2 mM dithiothreitol, pH 5.0, several months, minimal loss of activity
-
-10C, in presence of 1 mg/ml bovine serum albumin, no loss of activity
-
-20C, 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
-
22C, 20 mM Bis-Tris pH 6.6, 50 mM NaCl, 2 mM dithiothreitol, several weeks, without loss of activity or precipitation
D0ZJ57
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA affinity resin column chromatography and Superdex G50 gel filtration
HisTrap nickel affinity column chromatography and Superdex 75 gel filtration
-
ammonium sulfate precipitation
-
Ni-chelating column chromatography
-
recombinant Pth
-
wild-type and mutant enzymes N10A, H20A, M67A, F66A, D93A, H113A, K142A
recombinant His-tagged Pth
Ni-NTA column chromatography and Superdex G-75 gel filtration
-
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
-
Ni-NTA column chromatography and Superdex G-75 gel filtration
Super Q Toyopearl 650M column chromatography, Resource Q column chromatography, and Superdex 75 gel filtration
Ni2+-chelating affinity column chromatography and Superose 12 gel filtration
D0ZJ57
recombinant His-tagged Pth
; 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
-
wild-type and mutant enzymes
-
HisTrap column chromatography, Ni-NTA agarose column chromatography, and Q Sepharose column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)pLysS cells
-
expression in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli strain K37DELTArecAlambdaDE3
-
expression in Escherichia coli
-
expressed as GST-fusion protein in Escherichia coli Rosetta pLysS (GST later cleaved), or in human HEK293T cells as FLAG-tagged protein
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
expression in Escherichia coli
-
expressed in Escherichia coli BL21(lambdaDE3) cells
-
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 42C, at 39C, 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)
-
expressed in Escherichia coli BL21(lambdaDE3) cells
expressed in Escherichia coli BL21 (DE3) pMGK cells with eight nonnative residues at the C-terminus (LEHHHHHH) to facilitate protein purification
expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL cells
expression in Escherichia coli
expression in Escherichia coli
-
expressed in Escherichia coli BL21 pLysS cells
D0ZJ57
expression in Escherichia coli
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
-
pth2 gene, expression in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
no activity measurable with diacetyl-Lys-tRNALys
H20A
-
the mutant is unable to hydrolyze 2'(3')-O-L-(N,N-diacetyl-lysinyl)adenosine
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
N10A
turnover-number is 0.7% of the turnover-number for wild-type enzyme, Km-value for diacetyl-Lys-tRNALys is 1.1fold higher than the Km-value for the wild-type enzyme
N10A
-
the mutant shows strongly reduced activity with diacetyl-lysyl-tRNALys and L-Lys-tRNALys compared to the wild type enzyme
N10D
-
0.05% of wild-type kcat
N10D
-
the mutant shows strongly reduced activity with diacetyl-lysyl-tRNALys and L-Lys-tRNALys compared to the wild type enzyme
N185A
-
the mutation results in a 5.7fold 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 42C
C67S
-
site-directed mutagenesis, the mutant effectively complements the enzyme-defective thermosensitive Escherichia coli mutant strain AA7852 for growth at 42C
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 42C
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 42C; 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 42C
C166A
-
site-directed mutagenesis, the mutant effectively complements the enzyme-defective thermosensitive Escherichia coli mutant strain AA7852 for growth at 42C
-
C67S
-
site-directed mutagenesis, the mutant effectively complements the enzyme-defective thermosensitive Escherichia coli mutant strain AA7852 for growth at 42C
-
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 42C
-
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 42C; site-directed mutagenesis, the mutation affects the enzyme structure, overview
-
C703A
mutation abolishes editing activity
D86A
-
kcat/Km for diacetyl-lysyl-tRNALys is 0.22% of wild-type value
D86A/K18A
-
kcat/Km for diacetyl-lysyl-tRNALys is 0.17% of wild-type value
H25A
-
kcat/Km for diacetyl-lysyl-tRNALys is 13% of wild-type value
K118A
-
kcat/Km for diacetyl-lysyl-tRNALys is 87% of wild-type value
K18A
-
kcat/Km for diacetyl-lysyl-tRNALys is 0.2% of wild-type value
K56A
-
kcat/Km for diacetyl-lysyl-tRNALys is 12% of wild-type value
Q22A
-
kcat/Km for diacetyl-lysyl-tRNALys is 20% of wild-type value
Q54A
-
kcat/Km for diacetyl-lysyl-tRNALys is 47% of wild-type value
T90A
-
kcat/Km for diacetyl-lysyl-tRNALys is 1.4% of wild-type value
T98A
-
kcat/Km for diacetyl-lysyl-tRNALys is 34% of wild-type value
M67E
-
0.5% of wild-type kcat
additional information
-
excess of charged tRNALys maintains low levels of peptidyl-tRNA hydrolase in pth mutants at a non-permissive temperature, strain AA7852 phenotype and levels of aminoacyl- and peptidyl-tRNAs, overproduction of tRNALys suppresses the effects of pthTs mutation at 41C but not at 43C, and increases the levels of aminoacyl-tRNA, overview
N185A/H188A
-
the mutation results in a 7.7fold decrease in the kcat/Km value compared to the wild type enzyme
additional information
truncated ICT1 form lacking the N-terminal 29 residues leads to reduction in mitochondrial protein synthesis, a mutation of the GGQ domain of ICT1 by site-directed mutagenesis causes loss of cell viability
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
Pth is a potential drug target to control eubacterial infections