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 | 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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | - |
Homo sapiens | 5739 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
Apocytochrome c + heme | Homo sapiens | - |
Holocytochrome c | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P53701 | - |
- |
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 | 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 | Comment | Organism |
---|---|---|
HCCS | - |
Homo sapiens |
holocytochrome c synthase | - |
Homo sapiens |
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 |