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Literature summary for 4.4.1.17 extracted from

  • Stevens, J.M.; Zhang, Y.; Muthuvel, G.; Sam, K.A.; Allen, J.W.; Ferguson, S.J.
    The mitochondrial cytochrome c N-terminal region is critical for maturation by holocytochrome c synthase (2011), FEBS Lett., 585, 1891-1896.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
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Saccharomyces cerevisiae 5739
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Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
apo-iso-1 cytochrome c + heme single residue variants of five conserved N-terminal residues G6A, K10A, G11A, F15A and R18A of Saccharomyces cerevisiae iso-1 cytochrome c. F15A replacement, corresponding to F10 in the horse cytochrome c, is not matured at all. G6A, K10A, G11A, and R18A variants are matured Saccharomyces cerevisiae holocytochrome c
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Apocytochrome c + heme chimeric substrate comprising a short Saccharomyces cerevisiae mitochondrial cytochrome c N-terminal region plus the C-terminal sequence, including the CXXCH heme-binding motif, of Paracoccus denitrificans cytochrome c that is not otherwise processed by HCCS. Saccharomyces cerevisiae HCCS is able to attach heme to the chimeric protein Saccharomyces cerevisiae Holocytochrome c
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Apocytochrome c + heme chorse cytochrome c, recombinant substrate with mutations D2A, E4A, K5A, G6A, K7A, K8A and F10A. For the D2A, E4A and K7A variants, heme attachment is not attenuated by the amino acid replacements. The G6A and F10A variants are not matured at detectable levels.K5A and K8A variants of horse cytochrome c are also matured at similar levels to the wild type protein Saccharomyces cerevisiae Holocytochrome c
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Synonyms

Synonyms Comment Organism
HCCS
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Saccharomyces cerevisiae
heme lyase
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Saccharomyces cerevisiae