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3.4.22.70: sortase A

This is an abbreviated version!
For detailed information about sortase A, go to the full flat file.

Word Map on EC 3.4.22.70

Reaction

The enzyme catalyses a cell wall sorting reaction in which a surface protein with a sorting signal containing a LPXTG motif is cleaved between the Thr and Gly residue. The resulting threonine carboxyl end of the protein is covalently attached to a pentaglycine cross-bridge of peptidoglycan. =

Synonyms

C60.001, sortase A, sortase A transpeptidase, sortase SrtA, sortase transpeptidase, SrtA, SrtA protein, SrtA sortase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.70 sortase A

Engineering

Engineering on EC 3.4.22.70 - sortase A

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H126A
-
inactive
C184A
C184Hcy
-
site-directed mutagenesis, generation of a sortase mutant with Cys184 replaced by homocysteine (Hcy). Mutant Hcy-sortase is a poor catalyst with less than 1% of wild-type activity. The sensitivity of the active site nucleophiles towards an alkylation reagent correlates with the pKa values of the mutated residues
C184S
-
2700fold decrease in kcat/Km compared to wild-type value
C184Sec
-
site-directed mutagenesis, generation of a sortase mutant with Cys184 replaced by selenocysteine (Sec). Mutant Sec-sortase shows a moderate 2-3fold reduction in catalytic activity. The sensitivity of the active site nucleophiles towards an alkylation reagent correlates with the pKa values of the mutated residues. The pH-profile of mutant Sec-sortase is shifted to more acidic conditions when compared to the wild-type enzyme
D170A
D185A 1.3
-
fold decrease in kcat/Km compared to wild-type value
D186A
-
1.8fold decrease in kcat/Km compared to wild-type value
DELTA N59
E108A
-
turnover-number for o-aminobenzoyl-LPETG-2,4-dinitrophenyl is 43.8fold lower than wild-type value
E171A
G167A
-
Tm is 0.5°C lower than the Tm-value of wild-type enzyme. No change in kcat/KM compared to wild-type enzyme
H120A
-
96000fold decrease in kcat/Km compared to wild-type value
H120Q
-
36000fold decrease in kcat/Km compared to wild-type value
I123G
-
mutant is generated by using wild type truncated protein SrtADELTAN59 as a template. Mutation reduces dimerization
I182A
-
mutation produces modest decreases in SrtA activity and leds to substrate inhibition. 28fold decrease in kcat/Km compared to wild-type value
I182S
-
74fold decrease in kcat/Km compared to wild-type value
K137A
-
mutant is generated by using wild type truncated protein SrtADELTAN59 as a template. Mutation completely disrupts dimerization
K152A
-
mutant is generated by using wild type truncated protein SrtADELTAN59 as a template. Mutation increases dimerization
K62A
-
mutant is generated by using wild type truncated protein SrtADELTAN59 as a template
L169A
-
Tm is 1.8°C lower than the Tm-value of wild-type enzyme. kcat/Km is 93fold lower than wild-type value
L181A
-
mutation produces modest decreases in SrtA activity and leds to substrate inhibition. 7.6fold decrease in kcat/Km compared to wild-type value
N132A
-
mutant is generated by using wild type truncated protein SrtADELTAN59 as a template. Mutation completely disrupts dimerization
N98A
-
kcat/Km is 1.2fold lower than wild-type value
N98Q
-
kcat/Km is 1.1fold higher than wild-type value
P126G
-
mutant is generated by using wild type truncated protein SrtADELTAN59 as a template. Mutation reduces dimerization
Q172A
-
Tm is 1.2°C lower than the Tm-value of wild-type enzyme. kcat/Km is 1.4fold lower than wild-type value
R197A
R197Cit
R197H
-
kcat/Km is 610fold lower than wild-type value
R197K
T180A
-
mutation produces modest decreases in SrtA activity and leds to substrate inhibition. 14fold decrease in kcat/Km compared to wild-type value
T183A
-
1200fold decrease in kcat/Km compared to wild-type value
V168A
-
Tm is 1.7°C lower than the Tm-value of wild-type enzyme. kcat/Km is 5.5fold lower than wild-type value
Y143A
-
mutant is generated by using wild type truncated protein SrtADELTAN59 as a template. Mutation completely disrupts dimerization
additional information