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4.4.1.13: cysteine-S-conjugate beta-lyase

This is an abbreviated version!
For detailed information about cysteine-S-conjugate beta-lyase, go to the full flat file.

Word Map on EC 4.4.1.13

Reaction

2-aminoprop-2-enoate
=
2-iminopropanoate

Synonyms

AAR, beta-cystathionase, beta-lyase, C-DES, C-S lyase, CBL, CBL/ALR, CBS, CCBL2, Ctl1, Ctl2, cystathionine beta-lyase, cystathionine beta/gamma-lyase, cystathionine lyase, cysteine conjugate beta-lyase, cysteine conjugate. beta.-lyase, cysteine lyase, cysteine S-conjugate beta-lyase, cysteine-S-conjugate beta-lyase, cystine C-S lyase, cystine lyase, EC 4.4.1.6, EC 4.4.1.8, EcCBL, glutamine transaminase K, glutamine transaminase K/cysteine conjugate beta-lyase, GTK, Irc7p, KAT, KAT III, KYAT3, kynurenine aminotransferase, kynurenine-oxoglutarate transaminase 3, L-cystine C-S lyase, LACBS_00576, lyase, cystathionine beta-, lyase, cysteine conjugate.beta., MalY, MetC, More, Mp CBL, ORF5, osteotoxin, patB, PatB protein, Str3p, TmCBL, TTHA1620, wMelCBL

ECTree

     4 Lyases
         4.4 Carbon-sulfur lyases
             4.4.1 Carbon-sulfur lyases (only sub-subclass identified to date)
                4.4.1.13 cysteine-S-conjugate beta-lyase

Engineering

Engineering on EC 4.4.1.13 - cysteine-S-conjugate beta-lyase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C117G
-
inactive protein, pyridoxal 5'-phosphate is not detectable in the mutant protein, enhanced susceptibility to chymotrypsin digestion
C279
-
activity is comparable with that of the native enzyme
C309A
-
inactive protein, pyridoxal 5'-phosphate is not detectable in the mutant protein, enhanced susceptibility to chymotrypsin digestion
C88A
-
activity is comparable with that of the native enzyme
D116A
-
mutant with reduced catalytic efficiency
D116N
-
mutant with reduced catalytic efficiency
F55D
-
the mutant shows 74fold reduced catalytic efficiency compared to the wild type enzyme
F55D/Y338E
-
the mutant shows 58000fold reduced catalytic efficiency compared to the wild type enzyme
K42A
site-directed mutagenesis, the mutant shows slightly reduced catalytic efficiency compared to the wild-type enzyme
R372A
-
mutant with reduced catalytic efficiency
R372K
-
mutant with reduced catalytic efficiency
R372L
-
mutant with reduced catalytic efficiency
R58A
-
mutant with reduced catalytic efficiency
R58K
-
mutant with reduced catalytic efficiency
R59A
-
mutant with reduced catalytic efficiency
R59K
-
mutant with reduced catalytic efficiency
S32A
site-directed mutagenesis, the mutant shows slightly reduced catalytic efficiency compared to the wild-type enzyme
S33A
site-directed mutagenesis, the mutant shows slightly reduced catalytic efficiency compared to the wild-type enzyme
W131F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W131F/W188F/W230F/W276F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W131F/W188F/W230F/W276F/W300F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W131F/W188F/W230F/W276F/W340F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W131F/W188F/W230F/W300F/W340F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W131F/W188F/W276F/W300F/W340F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W131F/W230F/W276F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W131F/W230F/W276F/W300F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W131F/W230F/W276F/W300F/W340F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W131F/W230F/W276F/W340F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W188F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by 4.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W188F/W230F/W276F/W300F/W340F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W230F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W276F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W300F
site-directed mutagenesis, below 2fold increase in KM and kcat for L-cystathionine and by less than 1.7°C reduced midpoint of thermal denaturation, monitored by circular dichroism spectroscopy, compared to the wild-type enzyme
W340F
Y338E
-
the mutant shows 2850fold reduced catalytic efficiency compared to the wild type enzyme
K233A
site-directed mutagenesis, the mutant is only active with D-Ser, but inactive with L- or D-Cys, and L-Ser, in contrast to the wild-type enzyme
Y123A
site-directed mutagenesis, the mutant shows highly reduced activity with L-Cys compared to the wild-type enzyme, and is active with L-Ser in contrast to wild-type
K233A
-
site-directed mutagenesis, the mutant is only active with D-Ser, but inactive with L- or D-Cys, and L-Ser, in contrast to the wild-type enzyme
-
Y123A
-
site-directed mutagenesis, the mutant shows highly reduced activity with L-Cys compared to the wild-type enzyme, and is active with L-Ser in contrast to wild-type
-
K223A
-
inactive mutant enzyme
additional information
construction of 12 chimeric mutants of cystathionine gamma-synthase, EC 2.5.1.48, and cystathionine beta-lyase to probe the roles of two structurally distinct, about 25-residue segments situated in proximity to the amino and carboxy termini and located at the entrance of the active-site. The exchange of the targeted regions impairs the activity of the resulting enzymes, but does not produce a corresponding interchange of reaction specificity, catalytic efficiency of the native reactions is reduced by at least 95fold, and alpha,beta versus alpha,gamma-elimination specificity is not modified. The chimeric enzymes adopt a stable folded structure