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Information on EC 3.1.1.29 - aminoacyl-tRNA hydrolase
for references in articles please use BRENDA:EC3.1.1.29
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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
The enzyme appears in viruses and cellular organisms
- 3.1.1.29
- peptidyl-trnas
- aminoacyl-trnas
-
drop-off
- trnalys
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infantile-onset
- drug development
showSynonyms
peptidyl-trna hydrolase, ankzf1, ptrhd1, spovc, mspth, bacterial peptidyl-trna hydrolase, peptidyl-trna hydrolase 2, yhr189w, abpth, mj0051, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AbPth
aminoacyl-transfer ribonucleate hydrolase
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Cdc48 adaptor
hydrolase, aminoacyl-transfer ribonucleate
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MsPth
N-substituted aminoacyl transfer RNA hydrolase
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peptidyl-tRNA hydrolase
peptidyl-tRNA hydrolase 1
peptidyl-tRNA hydrolase 2
PH1539
PTH
Pth1
Pth2
SaPth
SSO0175
VcPth
VC_2184
Vms1
peptidyl-tRNA hydrolase
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peptidyl-tRNA hydrolase
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PTH
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA
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N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA
reaction mechanism, active-site residues N10, H20 and D93 are crucial for catalysis
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N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA
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
structure-function relationship, residues Asp95 and His115 are involved in catalysis, overview
N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA
structure-function relationship, residues Asp95 and His115 are involved in catalysis, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
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PATHWAY SOURCE
PATHWAYS
MetaCyc
L-cysteine biosynthesis II (tRNA-dependent)
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SYSTEMATIC NAME
IUBMB Comments
aminoacyl-tRNA aminoacylhydrolase
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CAS REGISTRY NUMBER
COMMENTARY
9054-98-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2'(3')-O-L-(N,N-diacetyl-lysinyl)adenosine + H2O
?
Substrates: minimalist substrate
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5'-dephosphorylated N,N-diacetyl-L-lysyl-tRNALys + H2O
N,N-diacetyl-L-lysine + 5'-dephosphorylated tRNALys
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Substrates: -
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5'-dephosphorylated N-formyl-L-methionyl-tRNA + H2O
N-formyl-L-methionine + 5'-dephosphorylated tRNA
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Substrates: -
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?
acetyl-histidine-tRNA + H2O
acetyl-histidine + tRNA
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Substrates: -
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acetyl-histidyl-tRNAHis + H2O
acetyl-histidine + tRNAHis
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Substrates: -
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dephosphorylated diacyl-lysine-tRNA + H2O
diacyl-lysine + dephosphorylated tRNA
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Substrates: -
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dephosphorylated formyl-Met-tRNAfMet + H2O
formyl-Met + dephosphorylated tRNAfMet
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Substrates: -
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dephosphorylated formyl-methioninyl-tRNA + H2O
formyl-methionine + dephosphorylated tRNA
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Substrates: -
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diacetyl-lysyl-tRNALys
diacetyl-Lys + tRNALys
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Substrates: -
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formyl-Met-tRNAfMet + H2O
formyl-Met + tRNAfMet
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Substrates: -
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formyl-methionine-tRNA + H2O
formyl-methionine + tRNA
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Substrates: -
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formyl-methioninyl-tRNA + H2O
formyl-methionine + tRNA
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Substrates: -
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formyl-methionyl-tRNAfMet + H2O
formyl-methionine + tRNAfMet
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Substrates: Escherichia coli formyl-methionyltRNAfMet, phosphorylated and dephosphorylated substrate
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?
N-acetyl-Ala-tRNA(Ala) + H2O
N-acetyl-Ala + tRNA(Ala)
Substrates: -
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?
N-acetyl-His-tRNA + H2O
N-acetyl-His + tRNA
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Substrates: -
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N-acetyl-Leu-Gly-tRNA + H2O
N-acetyl-Leu-Gly + tRNA
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Substrates: -
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N-acetyl-Phe-Phe-tRNA + H2O
N-acetyl-Phe-Phe + tRNA
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Substrates: -
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N-acetyl-Phe-tRNA + H2O
N-acetyl-L-Phe + tRNA
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Substrates: -
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?
N-acetyl-Phe-Val-tRNA + H2O
N-acetyl-Phe-Val + tRNA
-
Substrates: -
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?
N-acetyl-Trp-tRNA + H2O
N-acetyl-Trp + tRNA
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Substrates: -
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N-benzoyl-Gly-Gly-Phe-tRNA + H2O
N-benzoyl-Gly-Gly-Phe + tRNA
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Substrates: -
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N-benzoyl-Gly-GlyGly-Phe-tRNA + H2O
N-benzoyl-Gly-Gly-Gly-Phe + tRNA
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Substrates: -
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N-carbobenzyloxy-Phe-tRNA + H2O
N-carbobenzyloxy-Phe + tRNA
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Substrates: -
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oligolysyl-tRNA + H2O
oligo-Lys + tRNA
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Substrates: -
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Oregon Green-methionine-tRNA + H2O
Oregon Green-methionine + tRNA
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Substrates: -
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phenyllactyl-Phe-tRNA + H2O
phenyllactyl-Phe + tRNA
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Substrates: -
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D-tyrosine-tRNA + H2O
D-tyrosine + tRNA
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Substrates: -
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diacetyl-Lys-tRNALys + H2O
diacetyl-Lys + tRNA
Substrates: -
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diacetyl-Lys-tRNALys + H2O
diacetyl-Lys + tRNA
Substrates: -
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diacetyl-Lys-tRNALys + H2O
diacetyl-Lys + tRNA
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Substrates: -
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diacetyl-Lys-tRNALys + H2O
diacetyl-Lys + tRNA
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Substrates: diacetyl-Lys-tRNALys from E. coli
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diacetyl-Lys-tRNALys + H2O
diacetyl-Lys + tRNA
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Substrates: -
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diacetyl-lysine-tRNA + H2O
diacetyl-lysine + tRNA
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Substrates: -
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diacetyl-lysine-tRNA + H2O
diacetyl-lysine + tRNA
Substrates: -
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diacetyl-lysine-tRNA + H2O
diacetyl-lysine + tRNA
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Substrates: -
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diacetyl-lysine-tRNA + H2O
diacetyl-lysine + tRNA
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Substrates: -
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diacetyl-lysine-tRNA + H2O
diacetyl-lysine + tRNA
Substrates: -
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diacetyl-lysyl-tRNALys + H2O
diacetyl-lysine + tRNALys
Substrates: diacetyl-lysyl-tRNALys is hydrolyzed by the wild type enzyme 360fold more efficiently than Lys-tRNALys
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diacetyl-lysyl-tRNALys + H2O
diacetyl-lysine + tRNALys
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Substrates: -
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diacetyl-lysyl-tRNALys + H2O
diacetyl-lysine + tRNALys
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Substrates: -
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diacetyl-lysyl-tRNALys + H2O
diacetyl-lysine + tRNALys
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Substrates: -
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diacetyl-lysyl-tRNALys + H2O
diacetyl-lysine + tRNALys
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Substrates: Escherichia coli diacetyl-lysyl-tRNALys, phosphorylated and dephosphorylated substrate
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Flag-tagged CRPNSKn-tRNA + H2O
Flag-tagged CRPNSKn + tRNA
Substrates: purified recombinant Ankzf1 catalyzes deacylation
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Flag-tagged CRPNSKn-tRNA + H2O
Flag-tagged CRPNSKn + tRNA
Substrates: -
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Flag-tagged CRPNSKn-tRNA + H2O
Flag-tagged CRPNSKn + tRNA
Substrates: -
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N-acetyl-Leu-tRNA + H2O
N-acetyl-Leu + tRNA
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Substrates: -
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N-acetyl-Lys-tRNA + H2O
N-acetyl-Lys + tRNA
Substrates: -
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N-acetyl-Lys-tRNA + H2O
N-acetyl-Lys + tRNA
Substrates: -
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N-acetyl-Phe-tRNA + H2O
N-acetyl-Phe + tRNA
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Substrates: enzyme from encysted embryos is specific for acetyl-Phe-tRNA
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N-acetyl-Phe-tRNA + H2O
N-acetyl-Phe + tRNA
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Substrates: enzyme with broad specificity
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N-acetyl-Phe-tRNA + H2O
N-acetyl-Phe + tRNA
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Substrates: enzyme with broad specificity
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N-acetyl-Phe-tRNA + H2O
N-acetyl-Phe + tRNA
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Substrates: -
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N-acetyl-Phe-tRNA + H2O
N-acetyl-Phe + tRNA
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Substrates: enzyme with broad specificity
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N-acetyl-Val-tRNA + H2O
N-acetyl-Val + tRNA
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Substrates: -
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N-acetyl-Val-tRNA + H2O
N-acetyl-Val + tRNA
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Substrates: -
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N-formyl-Val-tRNA + H2O
N-formyl-Val + tRNA
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Substrates: reaction at a lower rate than with the N-acetyl derivative
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N-formyl-Val-tRNA + H2O
N-formyl-Val + tRNA
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Substrates: reaction at a lower rate than with the N-acetyl derivative
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
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Substrates: -
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
Substrates: -
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
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Substrates: -
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
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Substrates: -
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
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Substrates: -
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
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Substrates: -
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
Substrates: -
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
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Substrates: the enzyme or an element directly controlled by the enzyme, is the target for the lethal effect by bacterophage lambda
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
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Substrates: Pth recycles N-acetyl-aminoacyl tRNAs and peptidyl-tRNAs by cleaving the ester bond between tRNA and peptide
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
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Substrates: -
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
Substrates: -
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
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Substrates: -
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
Substrates: -
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
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Substrates: -
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
Substrates: -
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
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Substrates: -
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
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Substrates: -
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
Substrates: -
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
Substrates: -
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
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Substrates: -
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
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Substrates: -
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
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Substrates: -
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
Substrates: -
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
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Substrates: -
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N-substituted aminoacyl-tRNA + H2O
N-substituted amino acid + tRNA
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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Substrates: -
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peptidyl-tRNA + H2O
?
Substrates: -
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peptidyl-tRNA + H2O
?
Substrates: -
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peptidyl-tRNA + H2O
peptide + tRNA
Substrates: -
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peptidyl-tRNA + H2O
peptide + tRNA
Substrates: -
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peptidyl-tRNA + H2O
peptide + tRNA
Substrates: 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
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peptidyl-tRNA + H2O
peptide + tRNA
Substrates: 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
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peptidyl-tRNA + H2O
peptide + tRNA
Substrates: -
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peptidyl-tRNA + H2O
peptide + tRNA
Substrates: -
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peptidyl-tRNA + H2O
peptide + tRNA
Substrates: -
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peptidyl-tRNA + H2O
peptide + tRNA
Substrates: -
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peptidyl-tRNA + H2O
peptide + tRNA
Substrates: -
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peptidyl-tRNA + H2O
peptide + tRNA
Substrates: -
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peptidyl-tRNA + H2O
peptide + tRNA
Substrates: -
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peptidyl-tRNA + H2O
peptide + tRNA
Substrates: -
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peptidyl-tRNA + H2O
peptide + tRNA
Substrates: -
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peptidyl-tRNAL + H2O
peptide + tRNA
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Substrates: 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
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peptidyl-tRNAL + H2O
peptide + tRNA
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Substrates: Pth prefers substrates with two or more peptide bonds compared to those with a single peptide bond
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peptidyl-tRNAL + H2O
peptide + tRNA
Substrates: cleavage of the ester bond between tRNA and the attached peptide in peptidyl-tRNA, substrate binding channel structure, overview
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peptidyl-tRNAL + H2O
peptide + tRNA
Substrates: cleavage of the ester bond between tRNA and the attached peptide in peptidyl-tRNA, substrate binding channel structure, overview
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