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Literature summary extracted from

  • Richter, S.; Zhong, R.; Lamppa, G.
    Function of the stromal processing peptidase in the chloroplast import pathway (2005), Physiol. Plant., 123, 362-368.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.102 ORFs SLL2008 and SLL2009 encoding the C- and N-terminal enzyme part, respectively, operon organization Synechocystis sp.
3.4.21.102 sequence analysis Lotus japonicus
3.4.21.102 sequence analysis Oryza sativa
3.4.21.102 sequence analysis Medicago truncatula
3.4.21.102 sequence analysis Pisum sativum
3.4.21.102 single gene, sequence analysis, expression analysis Arabidopsis thaliana

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.102 additional information downregulation of the enzyme by antisense technique in transgenic plants results in many lines with lethal seedlings Arabidopsis thaliana
3.4.21.102 additional information the [1-874] deletion mutant lacking the C-terminus is inactive Pisum sativum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.102 apicoplast
-
Plasmodium falciparum 20011
-
3.4.21.102 chloroplast stroma
-
Lotus japonicus 9570
-
3.4.21.102 chloroplast stroma
-
Oryza sativa 9570
-
3.4.21.102 chloroplast stroma
-
Medicago truncatula 9570
-
3.4.21.102 chloroplast stroma
-
Pisum sativum 9570
-
3.4.21.102 chloroplast stroma
-
Arabidopsis thaliana 9570
-
3.4.21.102 thylakoid
-
Chlamydomonas reinhardtii 9579
-
3.4.21.102 thylakoid
-
Anabaena sp. 9579
-
3.4.21.102 thylakoid
-
Synechocystis sp. 9579
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.21.102 Zn2+ the enzyme contains a HXXEH zinc-binding motif Chlamydomonas reinhardtii
3.4.21.102 Zn2+ the enzyme contains a HXXEH zinc-binding motif Lotus japonicus
3.4.21.102 Zn2+ the enzyme contains a HXXEH zinc-binding motif Oryza sativa
3.4.21.102 Zn2+ the enzyme contains a HXXEH zinc-binding motif Anabaena sp.
3.4.21.102 Zn2+ the enzyme contains a HXXEH zinc-binding motif Synechocystis sp.
3.4.21.102 Zn2+ the enzyme contains a HXXEH zinc-binding motif Medicago truncatula
3.4.21.102 Zn2+ the enzyme contains a HXXEH zinc-binding motif Arabidopsis thaliana
3.4.21.102 Zn2+ the enzyme contains a HXXEH zinc-binding motif Plasmodium falciparum
3.4.21.102 Zn2+ the enzyme contains a HXXEH zinc-binding motif, metalloendopeptidase Pisum sativum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.21.102 additional information Arabidopsis thaliana broad substrate specificity, overview, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview, the enzyme is essential for plant survival, regulation of expression in vivo ?
-
?
3.4.21.102 additional information Plasmodium falciparum broad substrate specificity, the stromal processing peptidase has a function in the apicoplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview ?
-
?
3.4.21.102 additional information Chlamydomonas reinhardtii broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview ?
-
?
3.4.21.102 additional information Lotus japonicus broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview ?
-
?
3.4.21.102 additional information Oryza sativa broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview ?
-
?
3.4.21.102 additional information Anabaena sp. broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview ?
-
?
3.4.21.102 additional information Synechocystis sp. broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview ?
-
?
3.4.21.102 additional information Medicago truncatula broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview ?
-
?
3.4.21.102 additional information Pisum sativum broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview ?
-
?
3.4.21.102 pre-LHCP protein + H2O Pisum sativum
-
LHCP protein + transit peptide
-
?
3.4.21.102 pre-RBCS protein + H2O Chlamydomonas reinhardtii
-
RBCS protein + transit peptide
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.102 Anabaena sp.
-
strain PCC 7120, ORF ALL1021
-
3.4.21.102 Arabidopsis thaliana O48870
-
-
3.4.21.102 Chlamydomonas reinhardtii
-
-
-
3.4.21.102 Lotus japonicus
-
-
-
3.4.21.102 Medicago truncatula
-
-
-
3.4.21.102 Oryza sativa
-
-
-
3.4.21.102 Pisum sativum Q40983 metalloendopeptidase; gene psa
-
3.4.21.102 Plasmodium falciparum Q8MVZ1 putative stromal processing peptidase
-
3.4.21.102 Synechocystis sp.
-
strain PCC 6803, ORFs SLL2008 and SLL2009 encoding the C- and N-terminal enzyme part, respectively
-

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 reaction mechanism, process model, substrate recognition, overview Chlamydomonas reinhardtii
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 reaction mechanism, process model, substrate recognition, overview Lotus japonicus
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 reaction mechanism, process model, substrate recognition, overview Oryza sativa
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 reaction mechanism, process model, substrate recognition, overview Anabaena sp.
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 reaction mechanism, process model, substrate recognition, overview Synechocystis sp.
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 reaction mechanism, process model, substrate recognition, overview Medicago truncatula
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 reaction mechanism, process model, substrate recognition, overview Pisum sativum
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 reaction mechanism, process model, substrate recognition, overview Arabidopsis thaliana
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 reaction mechanism, process model, substrate recognition, overview Plasmodium falciparum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.102 additional information broad substrate specificity, overview, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview, the enzyme is essential for plant survival, regulation of expression in vivo Arabidopsis thaliana ?
-
?
3.4.21.102 additional information broad substrate specificity, the stromal processing peptidase has a function in the apicoplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview Plasmodium falciparum ?
-
?
3.4.21.102 additional information broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview Chlamydomonas reinhardtii ?
-
?
3.4.21.102 additional information broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview Lotus japonicus ?
-
?
3.4.21.102 additional information broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview Oryza sativa ?
-
?
3.4.21.102 additional information broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview Anabaena sp. ?
-
?
3.4.21.102 additional information broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview Synechocystis sp. ?
-
?
3.4.21.102 additional information broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview Medicago truncatula ?
-
?
3.4.21.102 additional information broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview Pisum sativum ?
-
?
3.4.21.102 additional information substrate recognition by specific protein-protein interaction, endoprotease activity, overview Chlamydomonas reinhardtii ?
-
?
3.4.21.102 additional information substrate recognition by specific protein-protein interaction, endoprotease activity, overview Lotus japonicus ?
-
?
3.4.21.102 additional information substrate recognition by specific protein-protein interaction, endoprotease activity, overview Oryza sativa ?
-
?
3.4.21.102 additional information substrate recognition by specific protein-protein interaction, endoprotease activity, overview Anabaena sp. ?
-
?
3.4.21.102 additional information substrate recognition by specific protein-protein interaction, endoprotease activity, overview Synechocystis sp. ?
-
?
3.4.21.102 additional information substrate recognition by specific protein-protein interaction, endoprotease activity, overview Medicago truncatula ?
-
?
3.4.21.102 additional information substrate recognition by specific protein-protein interaction, endoprotease activity, overview Pisum sativum ?
-
?
3.4.21.102 additional information substrate recognition by specific protein-protein interaction, endoprotease activity, overview Arabidopsis thaliana ?
-
?
3.4.21.102 additional information substrate recognition by specific protein-protein interaction, endoprotease activity, overview Plasmodium falciparum ?
-
?
3.4.21.102 pre-LHCP protein + H2O
-
Pisum sativum LHCP protein + transit peptide
-
?
3.4.21.102 pre-RBCS protein + H2O
-
Chlamydomonas reinhardtii RBCS protein + transit peptide
-
?

Subunits

EC Number Subunits Comment Organism
3.4.21.102 ? x * 143000-145000, two isozymes Pisum sativum

Synonyms

EC Number Synonyms Comment Organism
3.4.21.102 chloroplast processing enzyme
-
Pisum sativum
3.4.21.102 chloroplast processing enzyme
-
Arabidopsis thaliana
3.4.21.102 CPE
-
Arabidopsis thaliana
3.4.21.102 More the enzyme probably belongs to the M16 peptidase family Chlamydomonas reinhardtii
3.4.21.102 More the enzyme probably belongs to the M16 peptidase family Lotus japonicus
3.4.21.102 More the enzyme probably belongs to the M16 peptidase family Oryza sativa
3.4.21.102 More the enzyme probably belongs to the M16 peptidase family Anabaena sp.
3.4.21.102 More the enzyme probably belongs to the M16 peptidase family Synechocystis sp.
3.4.21.102 More the enzyme probably belongs to the M16 peptidase family Medicago truncatula
3.4.21.102 More the enzyme probably belongs to the M16 peptidase family Arabidopsis thaliana
3.4.21.102 More the enzyme probably belongs to the M16 peptidase family Plasmodium falciparum
3.4.21.102 SPP
-
Chlamydomonas reinhardtii
3.4.21.102 SPP
-
Lotus japonicus
3.4.21.102 SPP
-
Oryza sativa
3.4.21.102 SPP
-
Anabaena sp.
3.4.21.102 SPP
-
Synechocystis sp.
3.4.21.102 SPP
-
Medicago truncatula
3.4.21.102 SPP
-
Pisum sativum
3.4.21.102 SPP
-
Arabidopsis thaliana
3.4.21.102 SPP
-
Plasmodium falciparum
3.4.21.102 stromal processing peptidase
-
Chlamydomonas reinhardtii
3.4.21.102 stromal processing peptidase
-
Lotus japonicus
3.4.21.102 stromal processing peptidase
-
Oryza sativa
3.4.21.102 stromal processing peptidase
-
Anabaena sp.
3.4.21.102 stromal processing peptidase
-
Synechocystis sp.
3.4.21.102 stromal processing peptidase
-
Medicago truncatula
3.4.21.102 stromal processing peptidase
-
Pisum sativum
3.4.21.102 stromal processing peptidase
-
Arabidopsis thaliana
3.4.21.102 stromal processing peptidase
-
Plasmodium falciparum