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Literature summary extracted from
- Structural properties of the chloroplast stromal processing peptidase required for its function in transit peptide removal (2003), J. Biol. Chem., 278, 39497-39502.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.4.21.102 | E97Q | no enzymic activity, but binding of transit peptide is not disturbed | Pisum sativum |
| 3.4.21.102 | H94L | no enzymic activity, but binding of transit peptide is not disturbed | Pisum sativum |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.21.102 | Pisum sativum | Q40983 | - |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.4.21.102 | proteolytic modification | contains an transit peptide of 142 amino acids, precursor is proteolytically inactive | Pisum sativum |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 3.4.21.102 | 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 |
aSynonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.21.102 | SPP | - |
Pisum sativum |
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Release 2023.1 (January 2023)
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