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EC Tree
The taxonomic range for the selected organisms is: Homo sapiens The enzyme appears in selected viruses and cellular organisms
Synonyms
peptidyl-trna hydrolase, ankzf1, ptrhd1, spovc, mspth, bacterial peptidyl-trna hydrolase, yhr189w, peptidyl-trna hydrolase 2, abpth, mj0051,
more
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aminoacyl-transfer ribonucleate hydrolase
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hydrolase, aminoacyl-transfer ribonucleate
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ICT1
immature colon carcinoma transcript-1 with PTH activity
N-substituted aminoacyl transfer RNA hydrolase
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peptidyl-tRNA hydrolase
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peptidyl-tRNA hydrolase
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peptidyl-tRNA hydrolase
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PTH
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hydrolysis of carboxylic ester
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aminoacyl-tRNA aminoacylhydrolase
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diacetyl-Lys-tRNA + H2O
diacetyl-Lys + tRNA
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diacetyl-Lys-tRNALys + H2O
diacetyl-Lys + tRNA
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diacetyl-lysine-tRNA + H2O
diacetyl-lysine + tRNA
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
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Flag-tagged CRPNSKn-tRNA + H2O
Flag-tagged CRPNSKn + tRNA
purified recombinant Ankzf1 catalyzes deacylation
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N-acetyl-Leu-tRNA + H2O
N-acetyl-Leu + tRNA
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peptidyl-tRNA + H2O
peptide + tRNA
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additional information
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additional information
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weak binding to peptidyl-tRNA for PTRHD1, binding to tRNA is detected but also the absence of peptidyl-tRNA hydrolase activity. Thus, PTRHD1 is not a Pth and the functional consequence of nucleotide binding remains undefined
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additional information
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weak binding to peptidyl-tRNA for PTRHD1, binding to tRNA is detected but also the absence of peptidyl-tRNA hydrolase activity. Thus, PTRHD1 is not a Pth and the functional consequence of nucleotide binding remains undefined
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
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peptidyl-tRNA + H2O
peptide + tRNA
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Bacterial Infections
Crystal structure of peptidyl-tRNA hydrolase from mycobacterium smegmatis reveals novel features related to enzyme dynamics.
Carcinoma
Knockdown of immature colon carcinoma transcript 1 induces suppression of proliferation, S-phase arrest and apoptosis in leukemia cells.
Colonic Neoplasms
High ANKZF1 expression is associated with poor overall survival and recurrence-free survival in colon cancer.
Colorectal Neoplasms
High ANKZF1 expression is associated with poor overall survival and recurrence-free survival in colon cancer.
Infections
Peptidyl-tRNA hydrolase and its critical role in protein biosynthesis.
Intellectual Disability
Lack of PTRHD1 mutation in patients with young-onset and familial Parkinson's disease in a Taiwanese population.
Intellectual Disability
PTRHD1 (C2orf79) mutations lead to autosomal-recessive intellectual disability and parkinsonism.
Intellectual Disability
PTRHD1 and possibly ADORA1 mutations contribute to Parkinsonism with intellectual disability.
Intellectual Disability
PTRHD1 Loss-of-function mutation in an african family with juvenile-onset Parkinsonism and intellectual disability.
Lyme Disease
Microbial genes homologous to the peptidyl-tRNA hydrolase-encoding gene of Escherichia coli.
Movement Disorders
PTRHD1 (C2orf79) mutations lead to autosomal-recessive intellectual disability and parkinsonism.
Movement Disorders
PTRHD1 Loss-of-function mutation in an african family with juvenile-onset Parkinsonism and intellectual disability.
Neoplasms
High ANKZF1 expression is associated with poor overall survival and recurrence-free survival in colon cancer.
Pancreatic Diseases
Infantile-Onset Multisystem Neurologic, Endocrine, and Pancreatic Disease: Case and Review.
Pancreatic Diseases
Phenotype variability of infantile-onset multisystem neurologic, endocrine, and pancreatic disease IMNEPD.
Parkinson Disease
Analysis of PTRHD1 common and rare variants in European patients with Parkinson's disease.
Parkinson Disease
Lack of PTRHD1 mutation in patients with young-onset and familial Parkinson's disease in a Taiwanese population.
Parkinsonian Disorders
Analysis of PTRHD1 common and rare variants in European patients with Parkinson's disease.
Parkinsonian Disorders
Lack of PTRHD1 mutation in patients with young-onset and familial Parkinson's disease in a Taiwanese population.
Parkinsonian Disorders
PTRHD1 (C2orf79) mutations lead to autosomal-recessive intellectual disability and parkinsonism.
Parkinsonian Disorders
PTRHD1 and possibly ADORA1 mutations contribute to Parkinsonism with intellectual disability.
Parkinsonian Disorders
PTRHD1 Loss-of-function mutation in an african family with juvenile-onset Parkinsonism and intellectual disability.
Pulmonary Disease, Chronic Obstructive
Mining novel cell glycolysis related gene markers that can predict the survival of colon adenocarcinoma patients.
Starvation
Origins of minigene-dependent growth inhibition in bacterial cells.
Starvation
Protein Synthesis Factors (RF1, RF2, RF3, RRF, and tmRNA) and Peptidyl-tRNA Hydrolase Rescue Stalled Ribosomes at Sense Codons.
Starvation
Role of methionine 71 in substrate recognition and structural integrity of bacterial peptidyl-tRNA hydrolase.
Starvation
The growth defect in Escherichia coli deficient in peptidyl-tRNA hydrolase is due to starvation for Lys-tRNA(Lys).
Starvation
Unraveling the stereochemical and dynamic aspects of the catalytic site of bacterial peptidyl-tRNA hydrolase.
Tuberculosis
Characterization of peptidyl-tRNA hydrolase encoded by open reading frame Rv1014c of Mycobacterium tuberculosis H37Rv.
Tuberculosis
Cloning, expression, purification, crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase from Mycobacterium tuberculosis.
Tuberculosis
Crowding, molecular volume and plasticity: an assessment involving crystallography, NMR and simulations.
Tuberculosis
NMR assignment of peptidyl-tRNA hydrolase from Mycobacterium tuberculosis H37Rv.
Tuberculosis
Solution structure and dynamics of peptidyl-tRNA hydrolase from Mycobacterium tuberculosis H37Rv.
Tuberculosis
Structural plasticity and enzyme action: crystal structures of mycobacterium tuberculosis peptidyl-tRNA hydrolase.
Tuberculosis
Structures of new crystal forms of Mycobacterium tuberculosis peptidyl-tRNA hydrolase and functionally important plasticity of the molecule.
Tularemia
Structure of Francisella tularensis peptidyl-tRNA hydrolase.
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0.00022
diacetyl-lysine-tRNA
27°C, pH 7.5
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1.3
diacetyl-Lys-tRNA
pH 7.5, 27°C
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diacetyl-lysine-tRNA
27°C, pH 7.5
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SwissProt
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paraproerythroblast, low activity
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low activity
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low activity
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mitochondiral ribosome
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firmly bound, not an integral part of the ribosomal subunit
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mitochondiral ribosome
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evolution
Ankzf1 is Saccharomyces cerevisiae Vms1 homologue
evolution
performing the essential function of recycling peptidyl-tRNAs, peptidyl-tRNA hydrolases are ubiquitous in all domains of life. The multicomponent eukaryotic Pth system differs greatly from the bacterial system composed predominantly of a single Pth1 enzyme
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
Ankzf1 is a peptidyl-tRNA hydrolase
physiological function
the enzyme is unable to complement a Pth1-deficient Salmonella typhimurium mutant strain. PTRHD1 does bind RNA but is not a peptidyl-tRNA hydrolase and its function needs to be determined for reclassification
additional information
PTRHD1 lacks the conserved, catalytically essential His20
additional information
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PTRHD1 lacks the conserved, catalytically essential His20
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PTH2_HUMAN
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1
19194
Swiss-Prot
Secretory Pathway (Reliability: 5 )
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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
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Q246L
site-directed mutagenesis, inactive active site mutant
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
additional information
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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
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PTRHD1 storage buffer is optimized in two stages using hanging microdrop screening, overview. The most favorable buffer for long-term storage and stability of PTRHD1 is 20 mM MES, 150 mM sodium chloride, pH 6.5. This buffer extends the soluble half-life at 4°C from days to many months for PTRHD1 concentrated to 0.5 mM or greater. The addition of other stabilizers (i.e. glycerol, PEG, etc.) is not pursued due to the tremendous increase in ability to store soluble PTRHD1 in solution
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recombinant His-tagged Pth
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by metal chelating affinity chromatography, dialysis, and ultrafiltration
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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
expressed as GST-fusion protein in Escherichia coli Rosetta pLysS (GST later cleaved), or in human HEK293T cells as FLAG-tagged protein
gene ANKZF1, transient recombinant expression of His-tagged wild-type and mutant enzymes in HEK-293 cells
gene pth, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
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Neth, R.; Dunlop, N.; Heller-Schch, G.; Winkler, K.
Hydrolase activity for N-substituted aminoacyl-tRNA in ribosomes and supernatant fractions from human tissues and tumors
Hoppe-Seyler's Z. Physiol. Chem.
353
117-121
1972
Homo sapiens, Rattus norvegicus, Rattus norvegicus Wistar
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de Pereda, J.M.; Waas, W.F.; Jan, Y.; Ruoslathi, E.; Schimmel, P.; Pascual, J.
Crystral structure of a human peptidyl-tRNA hydrolase eveals a new fold and suggests basis for a bifunctional activity
J. Biol. Chem.
279
8111-8115
2003
Escherichia coli, Homo sapiens (Q9Y3E5), Homo sapiens, Saccharolobus solfataricus
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Richter, R.; Rorbach, J.; Pajak, A.; Smith, P.M.; Wessels, H.J.; Huynen, M.A.; Smeitink, J.A.; Lightowlers, R.N.; Chrzanowska-Lightowlers, Z.M.
A functional peptidyl-tRNA hydrolase, ICT1, has been recruited into the human mitochondrial ribosome
EMBO J.
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1116-1125
2010
Homo sapiens (Q14197), Homo sapiens
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Verma, R.; Reichermeier, K.M.; Burroughs, A.M.; Oania, R.S.; Reitsma, J.M.; Aravind, L.; Deshaies, R.J.
Vms1 and ANKZF1 peptidyl-tRNA hydrolases release nascent chains from stalled ribosomes
Nature
557
446-451
2018
Homo sapiens (Q9H8Y5), Saccharomyces cerevisiae (Q04311), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (Q04311)
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Burks, G.L.; McFeeters, H.; McFeeters, R.L.
Expression, purification, and buffer solubility optimization of the putative human peptidyl-tRNA hydrolase PTRHD1
Protein Expr. Purif.
126
49-54
2016
Homo sapiens (Q6GMV3), Homo sapiens
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