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Information on EC 3.1.1.96 - D-aminoacyl-tRNA deacylase and Organism(s) Haemophilus influenzae and UniProt Accession P44814

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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:
Haemophilus influenzae
UNIPROT: P44814
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Word Map
The taxonomic range for the selected organisms is: Haemophilus influenzae
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
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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-aminoacyl-tRNA + H2O
D-amino acid + tRNA
show the reaction diagram
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-
-
?
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-aminoacyl-tRNA + H2O
D-amino acid + tRNA
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme helps maintain the fidelity of protein synthesis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the crystal structure is determined at a 1.64 A resolution. Comparison of the structures of the Escherichioa coli enzyme and the enzyme from Haemophilus influenzae together with modeling of the enzyme/D-Tyr-tRNA complex provides the structural basis for a proposed catalytic mechanism and explains the enzyme specificity data
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rigden, D.J.
Archaea recruited D-Tyr-tRNATyr deacylase for editing in Thr-tRNA synthetase
RNA
10
1845-1851
2004
Azotobacter vinelandii, Escherichia coli, Haemophilus influenzae (P44814)
Manually annotated by BRENDA team
Lim, K.; Tempczyk, A.; Bonander, N.; Toedt, J.; Howard, A.; Eisenstein, E.; Herzberg, O.
A catalytic mechanism for D-Tyr-tRNATyr deacylase based on the crystal structure of Hemophilus influenzae HI0670
J. Biol. Chem.
278
13496-13502
2003
Haemophilus influenzae (P44814), Haemophilus influenzae, Haemophilus influenzae DSM 11121 (P44814)
Manually annotated by BRENDA team