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Information on EC 3.1.1.96 - D-aminoacyl-tRNA deacylase and Organism(s) Pyrococcus abyssi and UniProt Accession Q9V2R8

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.96 D-aminoacyl-tRNA deacylase
IUBMB Comments
The enzyme, found in all domains of life, can cleave mischarged glycyl-tRNAAla . The enzyme from Escherichia coli can cleave D-tyrosyl-tRNATyr, D-aspartyl-tRNAAsp and D-tryptophanyl-tRNATrp . Whereas the enzyme from the archaeon Pyrococcus abyssi is a zinc protein, the enzyme from Escherichia coli does not carry any zinc .
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This record set is specific for:
Pyrococcus abyssi
UNIPROT: Q9V2R8
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Word Map
The taxonomic range for the selected organisms is: Pyrococcus abyssi
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
a D-aminoacyl-tRNA
+
=
+
glycyl-tRNAAla
+
=
+
Synonyms
d-aminoacyl-trna deacylase, d-tyr-trna(tyr) deacylase, h-dtd, d-tyr-trnatyr deacylase, ss02234, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-Tyr-tRNATyr deacylase
-
SYSTEMATIC NAME
IUBMB Comments
D-aminoacyl-tRNA aminoacylhydrolase
The enzyme, found in all domains of life, can cleave mischarged glycyl-tRNAAla [5]. The enzyme from Escherichia coli can cleave D-tyrosyl-tRNATyr, D-aspartyl-tRNAAsp and D-tryptophanyl-tRNATrp [1]. Whereas the enzyme from the archaeon Pyrococcus abyssi is a zinc protein, the enzyme from Escherichia coli does not carry any zinc [2].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-tyrosyl-tRNATyr + H2O
D-tyrosine + tRNATyr
show the reaction diagram
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
D-tyrosyl-tRNATyr + H2O
D-tyrosine + tRNATyr
show the reaction diagram
the enzyme can recycle misaminoacylated D-Tyr-tRNATyr
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
200 mM, markedly stimulates hydrolysis of D-Tyr-tRNATyr
Mg2+
markedly improves initial rate of D-Tyr-tRNATyr hydrolysis. Optimal concentration: 16 mM
Zn2+
contains strongly bound Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
spermidine
0.8 mM, markedly stimulates hydrolysis of D-Tyr-tRNATyr
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30781
1 * 30781, calculated from sequence
30907
1 * 30907, mass spectrometry, SDS-PAGE
35000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20 mM Tris-HCl buffer, pH 7.8, containing 60% glycerol and 0.05 mM zinc acetate
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ferri-Fioni, M.L.; Fromant, M.; Bouin, A.P.; Aubard, C.; Lazennec, C.; Plateau, P.; Blanquet, S.
Identification in archaea of a novel D-Tyr-tRNATyr deacylase
J. Biol. Chem.
281
27575-27585
2006
Archaeoglobus fulgidus (O29630), Archaeoglobus fulgidus, Saccharolobus solfataricus (Q97WI2), Saccharolobus solfataricus, Pyrococcus abyssi (Q9V2R8), Pyrococcus abyssi, Saccharolobus solfataricus P2 (Q97WI2), Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543 (Q9V2R8)
Manually annotated by BRENDA team