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Information on EC 4.4.1.17 - Holocytochrome-c synthase and Organism(s) Mus musculus and UniProt Accession P53702

for references in articles please use BRENDA:EC4.4.1.17
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EC Tree
IUBMB Comments
In the reverse direction, the enzyme catalyses the attachment of heme to two cysteine residues in the protein, forming thioether links.
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This record set is specific for:
Mus musculus
UNIPROT: P53702
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
system iii, heme lyase, cytochrome c heme lyase, cyc2p, holocytochrome c synthase, holocytochrome c-type synthase, ccsa1, holocytochrome c synthetase, cytochrome c synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CCHL
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Cytochrome c heme-lyase
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Cytochrome c synthase
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HCCS
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Holocytochrome c synthetase
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Holocytochrome c-type synthase
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Holocytochrome-C synthase
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-
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Holocytochrome-C-type synthase
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Synthetase, holocytochrome c
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
covalent attachment of heme
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-
PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
holocytochrome-c apocytochrome-c-lyase (heme-forming)
In the reverse direction, the enzyme catalyses the attachment of heme to two cysteine residues in the protein, forming thioether links.
CAS REGISTRY NUMBER
COMMENTARY hide
75139-03-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Apocytochrome c + heme
Holocytochrome c
show the reaction diagram
-
-
?
apocytochrome c1 + heme
holocytochrome c1
show the reaction diagram
-
-
?
Apocytochrome c + heme
Holocytochrome c
show the reaction diagram
-
-
-
-
?
apocytochrome c1 + heme
holocytochrome c1
show the reaction diagram
-
-
-
-
?
additional information
?
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-
during apoptotic stimuli, enzyme translocates to outside the mitochondria, and binds to and suppresses the X-linked inhibitor of apoptosis protein XIAP, leading to activation of caspase-3. The N-terminus of the neuronal glutamate transporter excitatory amino-acid carrier 1 EAAC1 can bind to enzyme which interferes with the enzyme-XIAP association
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
during apoptotic stimuli, enzyme translocates to outside the mitochondria, and binds to and suppresses the X-linked inhibitor of apoptosis protein XIAP, leading to activation of caspase-3. The N-terminus of the neuronal glutamate transporter excitatory amino-acid carrier 1 EAAC1 can bind to enzyme which interferes with the enzyme-XIAP association
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
during apoptotic stimuli, enzyme translocates to outside the mitochondria, and binds to and suppresses the X-linked inhibitor of apoptosis protein XIAP, leading to activation of caspase-3. The N-terminus of the neuronal glutamate transporter excitatory amino-acid carrier 1 EAAC1 can bind to enzyme which interferes with the enzyme-XIAP association
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CCHL_MOUSE
272
0
30978
Swiss-Prot
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the N-terminus of the neuronal glutamate transporter excitatory amino-acid carrier 1 EAAC1 can bind to enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning in Escherichia coli
heterologous expression in a multicopy yeast vector
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schaefer, L.; Ballabio, A.; Zoghbi, H.Y.
Cloning and characterization of a putative human holocytochrome c-type synthetase gene (HCCS) isolated from the critical region for microphthalmia with linear skin defects (MLS)
Genomics
34
166-172
1996
Homo sapiens (P53701), Mus musculus (P53702)
Manually annotated by BRENDA team
Bernard, D.G.; Gabilly, S.T.; Dujardin, G.; Merchant, S.; Hamel, P.P.
Overlapping specificities of the mitochondrial cytochrome c and c1 heme lyases
J. Biol. Chem.
278
49732-49742
2003
Homo sapiens (P53701), Homo sapiens, Mus musculus (P53702), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Kiryu-Seo, S.; Gamo, K.; Tachibana, T.; Tanaka, K.; Kiyama, H.
Unique anti-apoptotic activity of EAAC1 in injured motor neurons
EMBO J.
25
3411-3421
2006
Mus musculus
Manually annotated by BRENDA team
Drenckhahn, J.D.; Schwarz, Q.P.; Gray, S.; Laskowski, A.; Kiriazis, H.; Ming, Z.; Harvey, R.P.; Du, X.J.; Thorburn, D.R.; Cox, T.C.
Compensatory growth of healthy cardiac cells in the presence of diseased cells restores tissue homeostasis during heart development
Dev. Cell
15
521-533
2008
Mus musculus
Manually annotated by BRENDA team