Literature summary for 2.7.10.2 extracted from

Horn, M.A.; Walker, J.C.
Biochemical properties of the autophosphorylation of RLK5, a receptor-like protein kinase from Arabidopsis thaliana (1994), Biochim. Biophys. Acta, 1208, 65-74.

Search for more literature for 2.7.10.2

Cloned(Commentary)

Cloned (Comment)	Organism
expression of the catalytic domain as two different recombinant fusion proteins in Escherichia coli	Arabidopsis thaliana

Protein Variants

Protein Variants	Comment	Organism
K711E	substitution in the catalytic domain of RLK5 results in the catalytically inactive protein	Arabidopsis thaliana

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	RLK5 protein contains an extracellular domain that has 21 tandemly repeated leucine-rich motifs linked, via a transmembrane hydrophobic region	Arabidopsis thaliana	16020	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	significantly greater activity in the presence of Mn2+ than Mg2+	Arabidopsis thaliana
Mn2+	significantly greater activity in the presence of Mn2+ than Mg2+	Arabidopsis thaliana

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	P47735	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	several sites in the catalytic domain are phosphorylated	Arabidopsis thaliana

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + a protein	autophosphorylation	Arabidopsis thaliana	ADP + a phosphoprotein	-	?

Synonyms

Synonyms	Comment	Organism
receptor-like protein kinase 5 precursor	-	Arabidopsis thaliana
RLK5	-	Arabidopsis thaliana

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Release 2023.1 (January 2023)