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Literature summary for 3.4.21.102 extracted from

  • Richter, S.; Lamppa, G.K.
    Structural properties of the chloroplast stromal processing peptidase required for its function in transit peptide removal (2003), J. Biol. Chem., 278, 39497-39502.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
E97Q no enzymic activity, but binding of transit peptide is not disturbed Pisum sativum
H94L no enzymic activity, but binding of transit peptide is not disturbed Pisum sativum

Organism

Organism UniProt Comment Textmining
Pisum sativum Q40983
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification contains an transit peptide of 142 amino acids, precursor is proteolytically inactive Pisum sativum

Reaction

Reaction Comment Organism Reaction ID
the enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-/-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II mechanism, transit peptide binding and removal are two separable steps of the reaction Pisum sativum

Synonyms

Synonyms Comment Organism
SPP
-
Pisum sativum