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Information on EC 3.1.1.29 - aminoacyl-tRNA hydrolase

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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:
UNIPROT: O57848 not found.
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Word Map
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The enzyme appears in 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
alanyl-tRNA editing protein AlaX-M
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AlaX-M trans-editing enzyme
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aminoacyl-transfer ribonucleate hydrolase
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hydrolase, aminoacyl-transfer ribonucleate
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N-substituted aminoacyl transfer RNA hydrolase
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peptidyl-tRNA hydrolase
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PTH
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
aminoacyl-tRNA aminoacylhydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9054-98-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Gly-tRNAAla + H2O
Gly + tRNAAla
show the reaction diagram
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?
Ser-tRNAAla + H2O
Ser + tRNAAla
show the reaction diagram
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ALAXM_PYRHO
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
216
0
25299
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
gel filtration
25300
1 * 25300, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 25300, calculated from sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method at 20°C, crystal structure is determined at 2.7 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C703A
mutation abolishes editing activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fukunaga, R.; Yokoyama, S.
Structure of the AlaX-M trans-editing enzyme from Pyrococcus horikoshii
Acta Crystallogr. Sect. D
63
390-400
2007
Pyrococcus horikoshii (O57848), Pyrococcus horikoshii
Manually annotated by BRENDA team