Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • White, M.D.; Klecker, M.; Hopkinson, R.J.; Weits, D.A.; Mueller, C.; Naumann, C.; O'Neill, R.; Wickens, J.; Yang, J.; Brooks-Bartlett, J.C.; Garman, E.F.; Grossmann, T.N.; Dissmeyer, N.; Flashman, E.
    Plant cysteine oxidases are dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets (2017), Nat. Commun., 8, 14690 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.3.2.8 plant cysteine oxidases i.e. PCO dioxygenase, dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets Arabidopsis thaliana

Application

EC Number Application Comment Organism
2.3.2.8 agriculture plant cysteine oxidases (PCOs) and enzyme ATE1 may be viable intervention targets to stabilize N-end rule substrates, including ERF-VIIs, to enhance submergence tolerance in agriculture Arabidopsis thaliana

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.2.8 gene ATE1, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3)-RIL Arabidopsis thaliana

Protein Variants

EC Number Protein Variants Comment Organism
2.3.2.8 additional information generation of RAP2.12 stabilization in ate1 ate2 double-null mutant plant lines Arabidopsis thaliana

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.20 Iron about 0.3 mol per mol of protein Arabidopsis thaliana

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.13.11.20 30681
-
 LC-MS Arabidopsis thaliana
1.13.11.20 36513
-
 LC-MS Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.2.8 L-arginyl-tRNAArg + ERF-VII peptide Arabidopsis thaliana after N-terminal Cys-sulfinic acid formation on ERF-VII peptide through plant cysteine oxidase. An ERF-VII peptide with an N-terminal Gly does not accept Arg, whereas an N-terminal Asp accepts Arg, independent of the presence of PCO1 or 4. A peptide comprising an N-terminal Cys-sulfonic acid is also shown to be a substrate for ATE1, again independent of the presence of PCO1 or 4. Proposed arginylation requirements for the Arg/Cys branch of the N-end rule pathway tRNAArg + L-arginyl-[ERF-VII peptide]
-
 ?
2.3.2.8 L-arginyl-tRNAArg + protein Arabidopsis thaliana
-
 tRNAArg + L-arginyl-[protein]
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.20 Arabidopsis thaliana Q9LXG9 isoform PCO1
-
1.13.11.20 Arabidopsis thaliana Q9SJI9 isoform PCO4
-
2.3.2.8 Arabidopsis thaliana Q9ZT48
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.2.8 recombinant N-terminally His6-tagged enzyme ATE1 from Escherichia coli strain BL21-CodonPlus (DE3)-RIL by nickel affinity chromatography, tag cleavage by TEV protease, and ultrafiltration Arabidopsis thaliana

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.20 H2N-CGGAIISDFI-COOH + O2 synthetic 10-mer peptide corresponding to the methionine excised N termini of the ERF-VIIs RAP2.2, RAP2.12 and HRE2 Arabidopsis thaliana H2N-(sulfino-Cys)-GGAIISDFI-COOH + H2N-(sulfono-Cys)-GGAIISDFI-COOH
-
 ?
2.3.2.8 L-arginyl-tRNAArg + ERF-VII peptide after N-terminal Cys-sulfinic acid formation on ERF-VII peptide through plant cysteine oxidase. An ERF-VII peptide with an N-terminal Gly does not accept Arg, whereas an N-terminal Asp accepts Arg, independent of the presence of PCO1 or 4. A peptide comprising an N-terminal Cys-sulfonic acid is also shown to be a substrate for ATE1, again independent of the presence of PCO1 or 4. Proposed arginylation requirements for the Arg/Cys branch of the N-end rule pathway Arabidopsis thaliana tRNAArg + L-arginyl-[ERF-VII peptide]
-
 ?
2.3.2.8 L-arginyl-tRNAArg + ERF-VII peptide after N-terminal Cys-sulfinic acid formation on ERF-VII peeptide through plant cysteine oxidase. C-terminally biotinylated RAP22-13 peptides (H2N-XGGAIISDFIPP(PEG)K(biotin)-NH2) where the N-terminal residue, X, constitutes Gly, Asp, Cys or Cys-sulfonic acid are subjected to the arginylation assay in the presence or absence of PCO1/4. An ERF-VII peptide with an N-terminal Gly does not accept Arg, whereas an N-terminal Asp accepts Arg, independent of the presence of PCO1 or 4. A peptide comprising an N-terminal Cys-sulfonic acid is also shown to be a substrate for ATE1, again independent of the presence of PCO1 or 4. Arginylation of the 12-mer peptide substrates, peptide sequences, overview Arabidopsis thaliana tRNAArg + L-arginyl-[ERF-VII peptide]
-
 ?
2.3.2.8 L-arginyl-tRNAArg + protein
-
 Arabidopsis thaliana tRNAArg + L-arginyl-[protein]
-
 ?

Subunits

EC Number Subunits Comment Organism
1.13.11.20 ? 1 * 30680, calculated from sequence Arabidopsis thaliana
1.13.11.20 ? 1 * 36510, calculated from sequence Arabidopsis thaliana

Synonyms

EC Number Synonyms Comment Organism
1.13.11.20 PCO1
-
 Arabidopsis thaliana
1.13.11.20 PCO4
-
 Arabidopsis thaliana
2.3.2.8 arginyl transferase
-
 Arabidopsis thaliana
2.3.2.8 Ate1
-
 Arabidopsis thaliana

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.2.8 30
-
 assay at Arabidopsis thaliana

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.2.8 7.5
-
 assay at Arabidopsis thaliana

General Information

EC Number General Information Comment Organism
1.13.11.20 physiological function PCO dioxygenase activity produces Cys-sulfinic acid at the N-terminus of ERF-VII peptide, which then undergoes efficient arginylation by arginyl transferase ATE1 Arabidopsis thaliana
2.3.2.8 malfunction RAP2.12 stabilization in ate1 ate2 double-null mutant plant lines implicates ATE1 as an ERF-VII-targeting arginyl transferase in vivo Arabidopsis thaliana
2.3.2.8 metabolism submergence-induced hypoxia in plants (e.g. flooded plants) results in stabilization of group VII ethylene response factors (ERF-VIIs), which aid survival under these adverse conditions. ERF-VII stability is controlled by the N-end rule pathway, which proposes that ERF-VII N-terminal cysteine oxidation in normoxia enables arginylation followed by proteasomal degradation. The plant cysteine oxidases (PCOs) are identified as catalysts of this oxidation. ERF-VII stabilization in hypoxia presumably arises from reduced PCO activity. PCO dioxygenase activity produces Cys-sulfinic acid at the N-terminus of an ERF-VII peptide, which then undergoes efficient arginylation by an arginyl transferase (ATE1). This provides molecular evidence of N-terminal Cys-sulfinic acid formation and arginylation by N-end rule pathway components, and a substrate of ATE1 in plants. PCOs catalyse dioxygenation of the ERF-VII peptides RAP2_2 to RAP2_11 Arabidopsis thaliana
2.3.2.8 physiological function PCO dioxygenase activity produces Cys-sulfinic acid at the N-terminus of an ERF-VII peptide, which then undergoes efficient arginylation by an arginyl transferase (ATE1). This provides molecular evidence of N-terminal Cys-sulfinic acid formation and arginylation by N-end rule pathway components, and a substrate of ATE1 in plants. Proposed arginylation requirements for the Arg/Cys branch of the N-end rule pathway Arabidopsis thaliana