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Information on EC 2.7.7.87 - L-threonylcarbamoyladenylate synthase and Organism(s) Bacillus subtilis and UniProt Accession P39153

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IUBMB Comments
The enzyme is involved in the synthesis of N6-threonylcarbamoyladenosine37 in tRNAs, with the anticodon NNU, i.e. tRNAIle, tRNAThr, tRNAAsn, tRNALys, tRNASer and tRNAArg .
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This record set is specific for:
Bacillus subtilis
UNIPROT: P39153
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The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
sua5 protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:L-threonyl,bicarbonate adenylyltransferase
The enzyme is involved in the synthesis of N6-threonylcarbamoyladenosine37 in tRNAs, with the anticodon NNU, i.e. tRNAIle, tRNAThr, tRNAAsn, tRNALys, tRNASer and tRNAArg [6].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-threonine + ATP + CO2
L-threonylcarbamoyl-AMP + diphosphate
show the reaction diagram
catalyzed by YwlC(TsaC)
L-threonylcarbamoyl-AMP i.e. TC-AMP, isolated by HPLC and characterized by mass spectrometry and 1H-NMR
-
?
L-threonylcarbamoyl-AMP + tRNA
t6A37-tRNA
show the reaction diagram
catalyzed by YdiBCE(TsaEBD), a study of RNA substrate specificity shows that tRNA(Thr) and tRNA(Lys) are modified, whereas tRNA(Phe) is not modified
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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
L-threonine + ATP + CO2
L-threonylcarbamoyl-AMP + diphosphate
show the reaction diagram
catalyzed by YwlC(TsaC)
L-threonylcarbamoyl-AMP i.e. TC-AMP, isolated by HPLC and characterized by mass spectrometry and 1H-NMR
-
?
L-threonylcarbamoyl-AMP + tRNA
t6A37-tRNA
show the reaction diagram
catalyzed by YdiBCE(TsaEBD), a study of RNA substrate specificity shows that tRNA(Thr) and tRNA(Lys) are modified, whereas tRNA(Phe) is not modified
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
attempts to purify the native forms of YdiC and YdiE by specific cleavage of the fusion proteins with thrombin or Factor Xa protease lead to multiple products, perhaps because the proteins are not completely stable in the cleavage reaction conditions
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
SDS-PAGE, cloning of ywlC and ydiB as His6 N-fusion proteins and highly expression in Escherichia coli BL21(DE3), because of inclusion bodies construction of N-terminal thioredoxin (trxA) fusion proteins of ydiC and ydiE, which allow good expression and sufficient solubility for in vitro studies
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lauhon, C.T.
Mechanism of N6-threonylcarbamoyladenonsine (t6A) biosynthesis: isolation and characterization of the intermediate threonylcarbamoyl-AMP
Biochemistry
51
8950-8963
2012
Bacillus subtilis (P39153), Bacillus subtilis 168 (P39153)
Manually annotated by BRENDA team