3.4.21.102: C-terminal processing peptidase
This is an abbreviated version!
For detailed information about C-terminal processing peptidase, go to the full flat file.
Word Map on EC 3.4.21.102
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3.4.21.102
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krabbe
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thylakoids
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leukodystrophy
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globoid
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twitcher
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psychosine
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galactosylceramide
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photoinhibition
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oxygen-evolving
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galactocerebroside
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agriculture
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drug development
- 3.4.21.102
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krabbe
- thylakoids
-
leukodystrophy
-
globoid
-
twitcher
- psychosine
- galactosylceramide
-
photoinhibition
-
oxygen-evolving
- galactocerebroside
- agriculture
- drug development
Reaction
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 =
Synonyms
At4g17740, C-terminal processing peptidase, C-terminal processing protease, C-terminal protease, carboxy terminal-processing proteinase, carboxyl terminal processing protease of D1 protein, carboxyl-terminal processing protease, carboxyl-terminal protease, carboxyl-terminal-processing peptidase 2, carboxyterminal processing protease, carboxyterminal processing protease of D1 protein, chloroplast processing enzyme, chloroplast protein precursor processing proteinase, CPE, CtpA, CtpA gene product, CtpB, D1 preprotein-processing proteinase, D1 protein-processing enzyme, D1P, More, PA5734, photosystem D1 protein precursor carboxyl-terminal processing protease, photosystem II D1 C-terminal processing protease, photosystem II D1 protein, photosystem II D1 protein processing proteinase, photosystem II protein D1, photosystem II protein D1 2, PrC, Prc protease, PRC protein, processing peptidase, protease Re, proteinase CtpA, proteinase, chloroplast protein precursor-processing, PsbA4, PXO_04290, SPP, stromal processing peptidase, tail-specific protease, thylakoid protein precursor processing peptidase, Tsp protease
ECTree
3.4.21.102 C-terminal processing peptidaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.4.21.102 - C-terminal processing peptidase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala + H2O
2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala + Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala
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-
-
?
Arc repressor + H2O
?
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C-terminal sequence: GRIGA, endoproteolyric cleavage
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-
?
C-terminal 19 amino acids of preD1 protein + H2O
pre-peptide of D1 + oligomer of 11 amino acids
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replacement of Ala at the cleaving site by Gly, Val, Pro reduces the rate of proteolysis to 50, 30 and 0% of the control
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?
cytochrome-b562-WVAAA + H2O
?
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cytochrome b562 with a C-terminal attachment, fast hydrolysis
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-
?
cytochrome-b562-WVAAK + H2O
?
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cytochrome b562 with a C-terminal attachment, no hydrolysis
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-
?
cytochrome-b562-WVAAV + H2O
?
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cytochrome b562 with a C-terminal attachment, slow hydrolysis
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-
?
cytochrome-b562-WVAGA + H2O
?
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cytochrome b562 with a C-terminal attachment, slow hydrolysis
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-
?
cytochrome-b562-WVAYA + H2O
?
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cytochrome b562 with a C-terminal attachment, fast hydrolysis
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-
?
cytochrome-b562-WVLAA + H2O
?
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cytochrome b562 with a C-terminal attachment, fast hydrolysis
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-
?
cytochrome-b562-WVQAA + H2O
?
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cytochrome b562 with a C-terminal attachment, slow hydrolysis
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-
?
maize preOEC17
OEC17 + presequence
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precursor of thylakoid lumen protein OEC17
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?
P-24 peptide + H2O
?
peptide substrate comprising the 24 C-terminal residues of spinach pre-D1 protein
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-
?
pre-D1 protein + H2O
D1 protein + peptide
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catalyzes the conversion of the nascent pre-D1 (pD1) protein into the active form of D1 by cleaving the 9 C-terminal residues in spinach, required to maintain the function of the photosystem II complex
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-
?
prePsbO + H2O
PsbO + presequence
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precursor of thylakoid lumen protein PsbO or OEC33
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?
ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit precursor + H2O
?
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-
-
-
?
anti-sigma factor MucA + H2O
?
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the Prc protease degrades mutants forms of MucA, the enzyme activity does not affect alginate production in strains with wild-type MucA, but MucA22 mutants show the mucoid phenotype, overview
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-
?
D1 polypeptide of photosystem II + H2O
?
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enzymatic cleavage occurs on the C-terminal site of Ala344
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?
D1 polypeptide of photosystem II + H2O
?
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investigation of substrate recognition sites
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?
D1 polypeptide of photosystem II + H2O
?
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determination of the catalytic important residues
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?
D1 polypeptide of photosystem II + H2O
?
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removal of the C-terminal extension
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?
D1 polypeptide of photosystem II + H2O
?
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removal of the C-terminal extension
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?
D1 polypeptide of photosystem II + H2O
?
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in vivo proteolytic processing of pre-D1, no other protease can compensate for its loss
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?
F-24 peptide + H2O
?
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peptide substrate comprising the 24 C-terminal residues of spinach pre-D1 protein, N-terminally fluorescence-labeled with a fluorescein isothiocyanate group
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?
F-24 peptide + H2O
?
peptide substrate comprising the 24 C-terminal residues of spinach pre-D1 protein, N-terminally fluorescence-labeled with a fluorescein isothiocyanate group
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-
?
membrane protein SpoIVFA + H2O
?
sequenctial processing by the enzyme together with protease 4B. The 4FA regulatory protein is composed of a globular N-terminal domain, a transmembrane helix (residues 73-90), an unstructured linker region and a compact C-terminal domain (residues 160-255, LytM-like) extending into the intermembrane space. 4B/CtpB-mediated removal of 4FA residues 131-154 induces sK maturation
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?
NIpI protein + H2O
?
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processing of wild-type substrate and mutants lacking up to 11 amino acids of the C-terminus in vivo, a mutant NIpI protein lacking 12 C-terminal amino acids is not processed, overview, the enzyme activates the substrate
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?
NIpI protein + H2O
?
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processing of wild-type substrate and mutants lacking up to 11 amino acids of the C-terminus, a mutant NIpI protein lacking 12 C-terminal amino acids is not processed, overview
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?
Protein + H2O
?
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endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal positions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third postion from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position
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?
Protein + H2O
?
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endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal postions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third position from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position.
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?
Protein + H2O
?
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endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal positions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third postion from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position
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?
Protein + H2O
?
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endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal postions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third position from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position.
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?
Protein + H2O
?
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endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal positions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third postion from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position
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?
Protein + H2O
?
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endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal postions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third position from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position.
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-
?
Protein + H2O
?
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Tsp is a component of the ssrA RNA protein-tagging pathway for the removal of incorrectly synthesized proteins
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-
?
Protein + H2O
?
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endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal positions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third postion from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position
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-
?
Protein + H2O
?
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endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal postions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third position from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position.
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-
?
Protein + H2O
?
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endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal positions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third postion from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position
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?
Protein + H2O
?
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endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal postions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third position from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position.
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-
?
SP-4 peptide + H2O
?
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peptide substrate comprising the 16 C-terminal residues of spinach pre-D1 protein with an inserted Lys between position 6 and 7 from the C-terminus, the Lys is fluorescence-labeled with a fluorescein isothiocyanate group at the epsilon-amino function, N-terminally biotin-labeled
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-
?
SP-4 peptide + H2O
?
peptide substrate comprising the 16 C-terminal residues of spinach pre-D1 protein with an inserted Lys between position 6 and 7 from the C-terminus, the Lys is fluorescence-labeled with a fluorescein isothiocyanate group at the epsilon-amino function, N-terminally biotin-labeled
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?
Suc-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Suc-Ala-Ala-Pro-Phe + 4-nitroaniline
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-
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?
Suc-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Suc-Ala-Ala-Pro-Phe + 4-nitroaniline
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-
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-
?
variant of the lambda repressor + H2O
?
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C-terminal sequence: WVAAA, endoproteolytic cleavage
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?
variant of the lambda repressor + H2O
?
C-terminal sequence: WVAAA, endoproteolytic cleavage
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-
?
additional information
?
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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
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?
additional information
?
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substrate recognition by specific protein-protein interaction, endoprotease activity, overview
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-
?
additional information
?
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O48870
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
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-
?
additional information
?
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O48870
substrate recognition by specific protein-protein interaction, endoprotease activity, overview
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-
?
additional information
?
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the enzyme belongs to the family of endoproteases involved in the maturation of proteins destined for the cell envelope
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?
additional information
?
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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
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?
additional information
?
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substrate recognition by specific protein-protein interaction, endoprotease activity, overview
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-
?
additional information
?
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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
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-
?
additional information
?
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substrate recognition by specific protein-protein interaction, endoprotease activity, overview
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-
?
additional information
?
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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
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-
?
additional information
?
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substrate recognition by specific protein-protein interaction, endoprotease activity, overview
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-
?
additional information
?
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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
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-
?
additional information
?
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substrate recognition by specific protein-protein interaction, endoprotease activity, overview
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-
?
additional information
?
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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
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-
?
additional information
?
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substrate recognition by specific protein-protein interaction, endoprotease activity, overview
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?
additional information
?
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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
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?
additional information
?
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substrate recognition by specific protein-protein interaction, endoprotease activity, overview
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-
?
additional information
?
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critical for the viability when cells are grown on complex semi-solid media, not essential when cells are grown in complex liquid media, enzyme function affects the permeability of the cell wall
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?
additional information
?
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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
?
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-
substrate recognition by specific protein-protein interaction, endoprotease activity, overview
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-
?
additional information
?
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Thermosynechococcus vestitus
the geometry of the TyrZ phenol group and its environment, likely the Tyr-O-H-Nepsilon-His bonding, are modified in isoform PsbA2-PSII when compared with isoforms PsbA(1/3)-PSII. They also point to the dynamics of the proton-coupled electron transfer processes associated with the oxidation of TyrZ being affected. The C144P and P173M substitutions in isoform PsbA2-PSII versus PsbA(1/3)-PSII, respectively located upstream of the alpha-helix bearing TyrZ and between the two alpha-helices bearing TyrZ and its hydrogen-bonded partner, His-190, are responsible for these changes
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-
?
