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Information on EC 6.1.1.23 - aspartate-tRNAAsn ligase and Organism(s) Bacillus subtilis and UniProt Accession O32038

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EC Tree
IUBMB Comments
When this enzyme acts on tRNAAsp, it catalyses the same reaction as EC 6.1.1.12, aspartate---tRNA ligase. It has, however, diminished discrimination, so that it can also form aspartyl-tRNAAsn. This relaxation of specificity has been found to result from the absence of a loop in the tRNA that specifically recognizes the third position of the anticodon . This accounts for the ability of this enzyme in, for example, Thermus thermophilus, to recognize both tRNAAsp (GUC anticodon) and tRNAAsn (GUU anticodon). The aspartyl-tRNAAsn is not used in protein synthesis until it is converted by EC 6.3.5.6, asparaginyl-tRNA synthase (glutamine-hydrolysing), into asparaginyl-tRNAAsn.
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This record set is specific for:
Bacillus subtilis
UNIPROT: O32038
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Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Synonyms
nd-asprs, aspartyl trna synthetase, nondiscriminating aspartyl-trna synthetase, nondiscriminating asprs, aspartate trna synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Aspartyl-tRNA synthetase
-
aspartate tRNA synthetase
-
-
-
-
Aspartic acid translase
-
-
-
-
Aspartyl ribonucleic synthetase
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-
-
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aspartyl tRNA synthetase
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-
-
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aspartyl-transfer ribonucleate synthetase
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-
-
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Aspartyl-transfer ribonucleic acid synthetase
-
-
-
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Aspartyl-transfer RNA synthetase
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-
-
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nondiscriminating aspartyl-tRNA synthetase
-
-
-
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Synthetase, aspartyl-transfer ribonucleate
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
-
-
-
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Aminoacylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
L-aspartate:tRNAAsx ligase (AMP-forming)
When this enzyme acts on tRNAAsp, it catalyses the same reaction as EC 6.1.1.12, aspartate---tRNA ligase. It has, however, diminished discrimination, so that it can also form aspartyl-tRNAAsn. This relaxation of specificity has been found to result from the absence of a loop in the tRNA that specifically recognizes the third position of the anticodon [1]. This accounts for the ability of this enzyme in, for example, Thermus thermophilus, to recognize both tRNAAsp (GUC anticodon) and tRNAAsn (GUU anticodon). The aspartyl-tRNAAsn is not used in protein synthesis until it is converted by EC 6.3.5.6, asparaginyl-tRNA synthase (glutamine-hydrolysing), into asparaginyl-tRNAAsn.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-32-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
show the reaction diagram
about 20% activity compared to tRNAAsp
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
show the reaction diagram
additional information
?
-
the enzyme shows no activity with tRNAGln
-
-
?
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
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0016
tRNAAsn
at pH 7.2 and 37°C
0.0016
tRNAAsp
at pH 7.2 and 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.058
tRNAAsn
at pH 7.2 and 37°C
0.36
tRNAAsp
at pH 7.2 and 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
40
tRNAAsn
at pH 7.2 and 37°C
220
tRNAAsp
at pH 7.2 and 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli JF448 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nair, N.; Raff, H.; Islam, M.T.; Feen, M.; Garofalo, D.M.; Sheppard, K.
The Bacillus subtilis and Bacillus halodurans aspartyl-tRNA synthetases retain recognition of tRNAAsn
J. Mol. Biol.
428
618-630
2016
Borreliella burgdorferi, Bacillus subtilis (O32038), Halalkalibacterium halodurans (Q9KDG1), Bacillus subtilis 168 (O32038)
Manually annotated by BRENDA team