3.4.22.71: sortase B
This is an abbreviated version!
For detailed information about sortase B, go to the full flat file.
Word Map on EC 3.4.22.71
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3.4.22.71
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aureus
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peptidoglycan
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anthracis
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envelope
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transpeptidases
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cross-bridges
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isdc
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pentaglycine
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pilin
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transpeptidation
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analysis
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medicine
- 3.4.22.71
- aureus
- peptidoglycan
- anthracis
- envelope
- transpeptidases
-
cross-bridges
- isdc
- pentaglycine
- pilin
-
transpeptidation
- analysis
- medicine
Reaction
The enzyme catalyses a cell wall sorting reaction in which a surface protein with a sorting signal containing a NPXTN motif is cleaved. The resulting threonine carboxyl end of the protein is covalently attached to a pentaglycine cross-bridge of peptidoglycan. =
Synonyms
CD630_27180, class B sortase, CPE0513, sortase B, Spy0129, SrtB, StrB
ECTree
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Engineering
Engineering on EC 3.4.22.71 - sortase B
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C232S
D225A
site-directed mutagenesis, the mutant exhibits nonspecific proteolytic activity
I182A
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the inhibitory effect of coptisine on mutants decreases in the order wild-type > R115A > I182A > N116A
N116A
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the inhibitory effect of coptisine on mutants decreases in the order wild-type > R115A > I182A > N116A
R115A
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the inhibitory effect of coptisine on mutants decreases in the order wild-type > R115A > I182A > N116A
I182A
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the inhibitory effect of coptisine on mutants decreases in the order wild-type > R115A > I182A > N116A
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N116A
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the inhibitory effect of coptisine on mutants decreases in the order wild-type > R115A > I182A > N116A
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R115A
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the inhibitory effect of coptisine on mutants decreases in the order wild-type > R115A > I182A > N116A
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C221S
additional information
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marked changes in the specificity profile of SrtA are obtained by replacing the beta6/beta7 loop in SrtA with the corresponding domain from SrtB
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the single residue mutation does not have noticeable effect on the secondary structure of the enzyme
C221S
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the single residue mutation does not have noticeable effect on the secondary structure of the enzyme
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