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

BRENDA support

Literature summary for 4.4.1.17 extracted from

  • Babbitt, S.E.; San Francisco, B.; Bretsnyder, E.C.; Kranz, R.G.
    Conserved residues of the human mitochondrial holocytochrome C synthase mediate interactions with heme (2014), Biochemistry, 53, 5261-5271.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant coexpression of GST-tagged wild-type and mutant enzymes with cytochrome c in Escherichia coli strain RK103 membranes Homo sapiens

Protein Variants

Protein Variants Comment Organism
E159A site-directed mutagenesis of a domain II residue, the mutant shows altered heme binding compared to the wild-type enzyme Homo sapiens
E159D site-directed mutagenesis of a domain II residue, the mutant shows altered heme binding compared to the wild-type enzyme Homo sapiens
E159K site-directed mutagenesis of a domain II residue, the mutant shows altered heme binding compared to the wild-type enzyme Homo sapiens
M130A site-directed mutagenesis of a domain I residue, the mutant shows altered heme binding compared to the wild-type enzyme Homo sapiens
additional information the mutants show altered heme binding with and/or without presence of cytochrome c, overview Homo sapiens
N128A site-directed mutagenesis of a domain I residue, the mutant shows altered heme binding compared to the wild-type enzyme Homo sapiens
N128A/M130A site-directed mutagenesis of domain I residues, the mutant shows altered heme binding compared to the wild-type enzyme Homo sapiens
N155A site-directed mutagenesis of a domain II residue, the mutant shows altered heme binding compared to the wild-type enzyme Homo sapiens
P121A site-directed mutagenesis of a domain I residue, the mutant shows altered heme binding compared to the wild-type enzyme Homo sapiens
W118A site-directed mutagenesis of a domain I residue, the mutant shows altered heme binding compared to the wild-type enzyme Homo sapiens
Y120A site-directed mutagenesis of a domain I residue, the mutant shows altered heme binding compared to the wild-type enzyme Homo sapiens
Y120A/P121A site-directed mutagenesis of domain I residues, the mutant shows altered heme binding compared to the wild-type enzyme Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Homo sapiens 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Apocytochrome c + heme Homo sapiens
-
Holocytochrome c
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens P53701
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant GST-tagged wild-type and mutant enzymes and cytochrome c from Escherichia coli strain RK103 membranes by ultracentrifugation, glutahione affinity chromatographyand ultrafiltration Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Apocytochrome c + heme
-
Homo sapiens Holocytochrome c
-
?
Apocytochrome c + heme the catalytic function of the enzyme depends on its ability to coordinate interactions between its substrates: heme and cytochrome c, four-step model describing enzyme-mediated cytochrome c assembly, identifying conserved histidine residue 154 as an axial ligand to the heme iron, overview. The enzyme contains two heme-binding domains, heme contacts mediated by residues within these domains modulate the dynamics of heme binding and contribute to the stability of the enzyme-heme-cytochrome c steady state ternary complex. While some residues are essential for initial heme binding, others impact the subsequent release of the holocytochrome c product Homo sapiens Holocytochrome c
-
?

Synonyms

Synonyms Comment Organism
HCCS
-
Homo sapiens
holocytochrome c synthase
-
Homo sapiens

General Information

General Information Comment Organism
metabolism the enzyme is the primary component of the eukaryotic cytochrome c biogenesis pathway, known as System III Homo sapiens
physiological function C-type cytochromes are distinguished by the covalent attachment of a heme cofactor, a modification that is typically required for its subsequent folding, stability, and function. Heme attachment takes place in the mitochondrial intermembrane space and, in most eukaryotes, is mediated by holocytochrome c synthase Homo sapiens