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Information on EC 3.1.1.96 - D-aminoacyl-tRNA deacylase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9ZPQ3

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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 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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Select one or more organisms in this record:
This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q9ZPQ3
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
The taxonomic range for the selected organisms is: Arabidopsis thaliana
Reaction Schemes
a D-aminoacyl-tRNA
+
=
+
Synonyms
D-aminoacyl-tRNA deacylase, D-Tyr-tRNA(Tyr) deacylase, D-Tyr-tRNATyr deacylase, D-Tyr-tRNATyr-deacylase, D-tyrosyl-tRNATyr deacylase, DTD, dtd2, DTD3, dtdA, GEK1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-aminoacyl-tRNA deacylase
300069
-
SYSTEMATIC NAME
IUBMB Comments
D-aminoacyl-tRNA aminoacylhydrolase
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-aspartyl-tRNAAsp + H2O
D-aspartate + tRNAAsp
show the reaction diagram
initial rate of hydrolysis is very close to that obtained with D-tyrosyl-tRNATyr
-
-
?
D-tyrosyl-tRNATyr + H2O
D-tyrosine + tRNATyr
show the reaction diagram
no activity with L-tyrosyl-tRNATyr and diacetyl-L-Lys-tRNALys
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
zinc ions are essential to the activity of the protein
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0011
D-tyrosyl-tRNATyr
pH 7.8, 27°C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
300
D-tyrosyl-tRNATyr
pH 7.8, 27°C
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
272700
D-tyrosyl-tRNATyr
pH 7.8, 27°C
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
GEK1_ARATH
317
0
34732
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34726
x * 34726, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 34726, calculated from sequence
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wydau, S.; Ferri-Fioni, M.L.; Blanquet, S.; Plateau, P.
GEK1, a gene product of Arabidopsis thaliana involved in ethanol tolerance, is a D-aminoacyl-tRNA deacylase
Nucleic Acids Res.
35
930-938
2007
Arabidopsis thaliana, Arabidopsis thaliana (Q9ZPQ3)
Manually annotated by BRENDA team
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