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BRENDA support

6.1.1.15: proline-tRNA ligase

This is an abbreviated version!
For detailed information about proline-tRNA ligase, go to the full flat file.

Word Map on EC 6.1.1.15

Reaction

ATP
+
L-proline
+
tRNAPro
=
AMP
+
diphosphate
+
L-prolyl-tRNAPro

Synonyms

bifunctional aminoacyl-tRNA synthetase, bifunctional glutamate/proline-tRNA ligase, class II prolyl-tRNA synthetase, class II ProRS, dual-specificity prolyl-cysteinyl-tRNA synthetase, dual-specificity prolyl-tRNA synthetase, EPRS, Global RNA synthesis factor, GluProRS, glutamyl-/prolyl-tRNA synthetase, glutamyl-prolyl tRNA synthetase, glutamyl-prolyl-tRNA synthetase, More, MSMEG_2621, Pro-tRNA synthetase, ProCysRS, Proline translase, Proline--tRNA ligase, proline/cysteine-tRNA ligase, Prolyl RNA synthetase, prolyl tRNA synthetase, prolyl-cysteinyl-tRNA synthetase, Prolyl-transfer ribonucleate synthetase, Prolyl-transfer ribonucleic acid synthetase, Prolyl-transfer RNA synthetase, Prolyl-tRNA synthetase, ProRS, ProRS-Cyt, ProRS-Org, ProRSTT, proS, PRS

ECTree

     6 Ligases
         6.1 Forming carbon-oxygen bonds
             6.1.1 Ligases forming aminoacyl-tRNA and related compounds
                6.1.1.15 proline-tRNA ligase

Localization

Localization on EC 6.1.1.15 - proline-tRNA ligase

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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
isozyme ProRS-Cyt
Manually annotated by BRENDA team
-
2.9% of total activity in the cell, enzyme participates in a large and stable multienzyme complex
Manually annotated by BRENDA team
additional information
-
the particulate form of the synthetases reflect true association of the enzymes with a high molecular weight cellular component common to both tissues
-
Manually annotated by BRENDA team