3.4.22.10: streptopain
This is an abbreviated version!
For detailed information about streptopain, go to the full flat file.
Word Map on EC 3.4.22.10
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3.4.22.10
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speb
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streptococci
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glomerulonephritis
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zymogen
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fasciitis
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superantigens
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streptolysin
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nephritogenic
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streptokinase
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poststreptococcal
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scarlet
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apsgn
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shock-like
- 3.4.22.10
- speb
- streptococci
- glomerulonephritis
- zymogen
- fasciitis
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superantigens
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streptolysin
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nephritogenic
- streptokinase
-
poststreptococcal
-
scarlet
-
apsgn
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shock-like
Reaction
preferential cleavage with hydrophobic residues at P2, P1 and P1' =
Synonyms
EC 3.4.4.18, IdeS, IgG-degrading enzyme of Streptococcus pyogenes, interleukin-1beta convertase, More, proteinase, streptococcal, pyrogenic exotoxin B, SCP, SpcCEP, Spe B, SPE B protease, SPE B/SCP, SpeB, SPP, Steptococcus proteinase, streptococcal cysteine protease, Streptococcal cysteine proteinase, streptococcal erythrogenic toxin B, streptococcal proteinase, streptococcal pyogenic exotoxin B, streptococcal pyrogenic exotoxin B, streptococcal pyrogenic exotoxin B/cysteine protease, Streptococcus peptidase A, Streptococcus protease, streptopain
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3.4.22.10 streptopainAdvanced search results
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results (Posttranslational Modification
Posttranslational Modification on EC 3.4.22.10 - streptopain
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POSTTRANSLATIONAL MODIFICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
proteolytic modification
side-chain modification
proteolytic modification
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SpeB is secreted as a 40000 Da proenzyme that is converted into a mature 28000 Da active proteinase by autocatalytic cleavage
proteolytic modification
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the enzyme performs autolytic processing to the 28 kDa mature protein, the 12 kDa pro-sequence domain, residues 28-145, directs the folding of the mature enzyme, overview
proteolytic modification
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the enzyme performs autolytic processing to the mature 28 kDa protein by removal of an about 117 amino-acid peptide from the N-terminus
proteolytic modification
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SPE B produced from group A Streptococcus (GAS) is released extracellularly to culture medium as a zymogen (proSPE B) with a molecular mass of 40 kDa. The conversion of proSPE B to the 28 kDa active mature SPE B (mSPE B) is achieved by autoproteolysis and exogenous proteases
proteolytic modification
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Spe is expressed as a propeptide. Zinc blocks the maturation of the SpeB zymogen and thereby the proteolytic degradation of proteins by SpeB
proteolytic modification
streptopain is initially expressed as a 40 kDa zymogen. Maturation is caused by cleavage of the 138 N-terminal amino acids, resulting in a 28000 active protease
proteolytic modification
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the enzyme performs autolytic processing to the mature 28 kDa protein by removal of an about 117 amino-acid peptide from the N-terminus
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side-chain modification
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complete removal of the 118 amino acids from the SCP zymogen results in formation of SCP
side-chain modification
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autocatalytic maturation of the zymogen proceeds through the sequential appearance of at least six intermediates, resulting from cleavage after Lys26, Asn41, Lys101, Ala112 and Lys118
side-chain modification
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autocatalytic processing of the 40000 Da zymogen to the 28000 Da mature form
side-chain modification
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autocatalytic maturation of the zymogen proceeds through the sequential appearance of at least six intermediates, resulting from cleavage after Lys26, Asn41, Lys101, Ala112 and Lys118
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