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2.5.1.65: O-phosphoserine sulfhydrylase

This is an abbreviated version!
For detailed information about O-phosphoserine sulfhydrylase, go to the full flat file.

Word Map on EC 2.5.1.65

Reaction

O-phospho-L-serine
+
hydrogen sulfide
=
L-cysteine
 +
phosphate

Synonyms

APE1586, ApOPSS, CysK2, CysM, O-acetyl-L-serine sulfhydrylase, O-acetylserine sulfhydrylase, O-phospho-L-serine sulfhydrylase, O-phospho-L-serine-dependent S-sulfocysteine synthase, O-phosphoserine S-sulfocysteine synthase, O-phosphoserine specific cysteine synthase, O-phosphoserine(thiol)-lyase, OASS, OPSS, Rv1336, S-sulfocysteine synthase

ECTree

     2 Transferases
         2.5 Transferring alkyl or aryl groups, other than methyl groups
             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
                2.5.1.65 O-phosphoserine sulfhydrylase

Engineering

Engineering on EC 2.5.1.65 - O-phosphoserine sulfhydrylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F225A
site-directed mutagenesis, the Km value toward O-phospho-L-serine is not significantly different between the wild-type ApOPSS and the F225A mutant, the kcat value of the wild-type ApOPSS is 4.2fold higher toward O-phospho-L-serine and 15fold higher toward O-acetyl-L-erine than that of the F225A mutant, respectively. The mutation from phenylalanine to alanine at position 225 affects the catalytic activity, not substrate binding
K127A
mutant is inactive for cysteine synthesis and does not form the alpha-aminoacrylate intermediate
Q224A
0.04% of wild-type activity
R297A
R297E
11% of wild-type activity
R297K
0.2% of wild-type activity
S153A
0.4% of wild-type activity
S153T
0.2% of wild-type activity
T152A
0.2% of wild-type activity
T152S
71% of wild-type activity
T203A
36% of wild-type activity
T203M
0.3% of wild-type activity
F225A
-
site-directed mutagenesis, the Km value toward O-phospho-L-serine is not significantly different between the wild-type ApOPSS and the F225A mutant, the kcat value of the wild-type ApOPSS is 4.2fold higher toward O-phospho-L-serine and 15fold higher toward O-acetyl-L-erine than that of the F225A mutant, respectively. The mutation from phenylalanine to alanine at position 225 affects the catalytic activity, not substrate binding
-
K204A
-
to improve crystallization of CysM alone, a putative surface residue in CysM (Lys204) is mutated to alanine using site-directed mutagenesis
R220A
R243A
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
K204A
-
to improve crystallization of CysM alone, a putative surface residue in CysM (Lys204) is mutated to alanine using site-directed mutagenesis
-
R220A
-
significant loss in specificity for substrate O-phosphoserine. The purified R220A mutant shows an absorption spectrum identical to wild type CysM with an absorption band at 412 nm reflecting the Schiff base between Lys51 and PLP. Formation of the aminoacrylate intermediate from O-phospho-L-serine in the mutant is severely compromised, with an approximately 700fold slower rate
-
R243A
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
additional information