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Information on EC 3.1.1.29 - aminoacyl-tRNA hydrolase and Organism(s) Homo sapiens and UniProt Accession Q9Y3E5

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.29 aminoacyl-tRNA hydrolase
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This record set is specific for:
Homo sapiens
UNIPROT: Q9Y3E5 not found.
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Word Map
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminoacyl-transfer ribonucleate hydrolase
-
-
-
-
hydrolase, aminoacyl-transfer ribonucleate
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-
-
-
ICT1
immature colon carcinoma transcript-1 with PTH activity
N-substituted aminoacyl transfer RNA hydrolase
-
-
-
-
peptidyl-tRNA hydrolase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
aminoacyl-tRNA aminoacylhydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9054-98-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
diacetyl-Lys-tRNA + H2O
diacetyl-Lys + tRNA
show the reaction diagram
-
-
-
?
diacetyl-Lys-tRNALys + H2O
diacetyl-Lys + tRNA
show the reaction diagram
-
-
-
?
diacetyl-lysine-tRNA + H2O
diacetyl-lysine + tRNA
show the reaction diagram
-
-
?
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
?
Flag-tagged CRPNSKn-tRNA + H2O
Flag-tagged CRPNSKn + tRNA
show the reaction diagram
purified recombinant Ankzf1 catalyzes deacylation
-
-
?
N-acetyl-Leu-tRNA + H2O
N-acetyl-Leu + tRNA
show the reaction diagram
-
-
-
-
?
peptidyl-tRNA + H2O
peptide + tRNA
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
show the reaction diagram
-
-
?
peptidyl-tRNA + H2O
peptide + tRNA
show the reaction diagram
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00022
diacetyl-lysine-tRNA
27°C, pH 7.5
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3
diacetyl-Lys-tRNA
pH 7.5, 27°C
1.3
diacetyl-lysine-tRNA
27°C, pH 7.5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
paraproerythroblast, low activity
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
mitochondiral ribosome
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PTH2_HUMAN
179
1
19194
Swiss-Prot
Secretory Pathway (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23000
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Q246L
site-directed mutagenesis, inactive active site mutant
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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.
29
1116-1125
2010
Homo sapiens (Q14197), Homo sapiens
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team