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Information on EC 3.4.21.47 - alternative-complement-pathway C3/C5 convertase

for references in articles please use BRENDA:EC3.4.21.47
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UNIPROT: P01024 not found.
Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Cleavage of Arg-/-Ser bond in complement component C3 alpha-chain to yield C3a and C3b, and Arg-/- bond in complement component C5 alpha-chain to yield C5a and C5b
Synonyms
(C3b)n,Bb, (CVF)-dependent glycine-rich-beta-glucoprotein, alternative C3 convertase, alternative C5 convertase, alternative complement pathway C3 convertase, alternative complement pathway C3(C5) convertase, alternative pathway C3 convertase, alternative pathway C3 convertase complex, alternative pathway C3-convertase, alternative pathway C5 convertase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(C3b)n,Bb
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(CVF)-dependent glycine-rich-beta-glucoprotein
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alternative complement pathway C3(C5) convertase
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C3 convertase
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C3 proactivator
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C3/C5 convertase
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C3b,Bb
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C5 convertase
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cobra venom factor-dependent C3 convertase
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complement C 3(C 5) convertase (amplification)
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complement component C3/C5 convertase (alternative)
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convertase, complement C3(C5) (amplification)
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CVF,Bb
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GBG
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Glycine-rich beta glycoprotein
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heat-labile factor
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PBF2
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proenzyme factor B
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properdin factor B
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Cleavage of Arg-/-Ser bond in complement component C3 alpha-chain to yield C3a and C3b, and Arg-/- bond in complement component C5 alpha-chain to yield C5a and C5b
show the reaction diagram
factor B binding to C3b forms an open activation state of C3bB. Factor D specifically binds the open conformation of factor B through a site distant from the catalytic center and is activated by the substrate, which displaces factor D's self-inhibitory loop. This concerted proteolytic mechanism, which is cofactor-dependent and substrate-induced, restricts complement amplification to C3b-tagged target cells
CAS REGISTRY NUMBER
COMMENTARY hide
80295-67-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
CO3_HUMAN
1663
0
187148
Swiss-Prot
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
crystal structures of the pro-convertase C3bB at 4 A resolution and its complex with factor D at 3.5 A resolution. Factor B binding to C3b forms an open activation state of C3bB. Factor D specifically binds the open conformation of factor B through a site distant from the catalytic center and is activated by the substrate, which displaces factor Ds self-inhibitory loop. This concerted proteolytic mechanism, which is cofactordependent and substrate-induced, restricts complement amplification to C3b-tagged target cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Forneris, F.; Ricklin, D.; Wu, J.; Tzekou, A.; Wallace, R.; Lambris, J.; Gros, P.
Structures of C3b in complex with factors B and D give insight into complement convertase formation
Science
330
1816-1820
2010
Homo sapiens (P01024)
Manually annotated by BRENDA team
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