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Literature summary for 3.4.24.64 extracted from

  • Sj๖ling, S.; Eriksson, A.C.; Glaaser, E.
    A helical element in the C-terminal domain of the N. plumbaginifolia F1 beta presequence is important for recognition by the mitochondrial processing peptidase (1994), J. Biol. Chem., 269, 32059-32062.
    View publication on PubMed
Search for more literature for 3.4.24.64

Inhibitors

Inhibitors Comment Organism Structure
additional information arginine, synthetic helical 22 amino acid peptide derived from heparin-binding domain of antithrombin III (ATIII); pF1beta(51-54), pF1beta(49-54) or pF1beta(44-54) Spinacia oleracea
Peptide pF1beta(1-18) derived from prepeptide of beta-subunit of F1-ATP-synthase, much less effective than pF1beta(38-54), N-terminal presequence Spinacia oleracea
Peptide pF1beta(38-54) derived from prepeptide of beta-subunit of F1-ATP-synthase, C-terminal presequence Spinacia oleracea

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion integral part of bc1-complex of respiratory chain Spinacia oleracea 5739
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Organism

Organism UniProt Comment Textmining
Spinacia oleracea
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 spinach
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Source Tissue

Source Tissue Comment Organism Textmining
leaf
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 Spinacia oleracea
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
F1-ATPase beta-subunit precursor + H2O F0F1-ATP-synthase F1beta subunit precursor from Nicotiana plumbaginifolia Spinacia oleracea F1-ATPase beta-subunit
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 ?
additional information substrate recognition specificity Spinacia oleracea ?
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 ?