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

BRENDA support

Literature summary for 3.4.21.102 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)

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

Protein Variants

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

Localization

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
pre-LHCP protein + H2O Pisum sativum
-
LHCP protein + transit peptide
-
?
pre-RBCS protein + H2O Chlamydomonas reinhardtii
-
RBCS protein + transit peptide
-
?

Organism

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

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 reaction mechanism, process model, substrate recognition, overview Chlamydomonas reinhardtii
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
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
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.
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.
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
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
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
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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. ?
-
?
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. ?
-
?
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 ?
-
?
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 ?
-
?
additional information substrate recognition by specific protein-protein interaction, endoprotease activity, overview Chlamydomonas reinhardtii ?
-
?
additional information substrate recognition by specific protein-protein interaction, endoprotease activity, overview Lotus japonicus ?
-
?
additional information substrate recognition by specific protein-protein interaction, endoprotease activity, overview Oryza sativa ?
-
?
additional information substrate recognition by specific protein-protein interaction, endoprotease activity, overview Anabaena sp. ?
-
?
additional information substrate recognition by specific protein-protein interaction, endoprotease activity, overview Synechocystis sp. ?
-
?
additional information substrate recognition by specific protein-protein interaction, endoprotease activity, overview Medicago truncatula ?
-
?
additional information substrate recognition by specific protein-protein interaction, endoprotease activity, overview Pisum sativum ?
-
?
additional information substrate recognition by specific protein-protein interaction, endoprotease activity, overview Arabidopsis thaliana ?
-
?
additional information substrate recognition by specific protein-protein interaction, endoprotease activity, overview Plasmodium falciparum ?
-
?
pre-LHCP protein + H2O
-
Pisum sativum LHCP protein + transit peptide
-
?
pre-RBCS protein + H2O
-
Chlamydomonas reinhardtii RBCS protein + transit peptide
-
?

Subunits

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

Synonyms

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