Any feedback?
Information on EC 2.5.1.65 - O-phosphoserine sulfhydrylase
for references in articles please use BRENDA:EC2.5.1.65Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.5.1.65 O-phosphoserine sulfhydrylaseIUBMB Comments
A pyridoxal-phosphate protein. The enzyme from Aeropyrum pernix acts on both O-phospho-L-serine and O3-acetyl-L-serine, in contrast with EC 2.5.1.47, cysteine synthase, which acts only on O3-acetyl-L-serine.
Specify your search results
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
opss, apopss, o-phosphoserine sulfhydrylase, o-phospho-l-serine sulfhydrylase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ApOPSS
CysK2
CysM
O-phospho-L-serine sulfhydrylase
O-phospho-L-serine-dependent S-sulfocysteine synthase
O-phosphoserine S-sulfocysteine synthase
OPSS
Rv1336
S-sulfocysteine synthase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate
ping-pong bi-bi mechanism
-
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate
ping-pong bi-bi mechanism
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate
a pyridoxal-phosphate protein, the enzyme from Aeropyrum pernix acts on both O-phospho-L-serine and O3-acetyl-L-serine, in contrast with EC 2.5.1.47, cysteine synthase, which acts only on O3-acetyl-L-serine
-
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate
active site structure, modeling of substrate binding at the active site with Arg297 being crucial for activity
-
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate
catalytic cycle of CysK2 and related cysteine synthases, catalytic raction mechanism of enzyme CysK2 via formation of the enzyme-aminoacrylate intermediate, accompanied by the release of a phosphate ion, commonly observed in the class of pyridoxal 5'-phosphate-dependent enzymes, overview
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate
ping-pong bi-bi mechanism, the active site of ApOPSS contains pyridoxal 5'-phosphate linked to lysine 127 as an internal Schiff base. Binding of the primary substrate O-phospho-L-serine displaces the lysine and forms an external Schiff base, initiating the first half-reaction that yields an alpha-aminoacrylate intermediate linked to pyridoxal 5'-phosphate. The second half-reaction involves the addition of a secondary substrate to the alpha-aminoacrylate intermediate and generates an external Schiff base with cysteine. The active-site lysine reacts with this external Schiff base, releasing cysteine and regenerating the internal Schiff base with K127. When other nucleophiles are used instead of sulfide, enzyme ApOPSS produces the corresponding non-natural amino acid
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate
ping-pong bi-bi mechanism
-
-
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate
ping-pong bi-bi mechanism, the active site of ApOPSS contains pyridoxal 5'-phosphate linked to lysine 127 as an internal Schiff base. Binding of the primary substrate O-phospho-L-serine displaces the lysine and forms an external Schiff base, initiating the first half-reaction that yields an alpha-aminoacrylate intermediate linked to pyridoxal 5'-phosphate. The second half-reaction involves the addition of a secondary substrate to the alpha-aminoacrylate intermediate and generates an external Schiff base with cysteine. The active-site lysine reacts with this external Schiff base, releasing cysteine and regenerating the internal Schiff base with K127. When other nucleophiles are used instead of sulfide, enzyme ApOPSS produces the corresponding non-natural amino acid
-
-
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate
catalytic cycle of CysK2 and related cysteine synthases, catalytic raction mechanism of enzyme CysK2 via formation of the enzyme-aminoacrylate intermediate, accompanied by the release of a phosphate ion, commonly observed in the class of pyridoxal 5'-phosphate-dependent enzymes, overview
-
-
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
O-phospho-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase
A pyridoxal-phosphate protein. The enzyme from Aeropyrum pernix acts on both O-phospho-L-serine and O3-acetyl-L-serine, in contrast with EC 2.5.1.47, cysteine synthase, which acts only on O3-acetyl-L-serine.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
37290-89-4
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-chloro-L-alanine + sulfide
?
-
heat-labile substrate, 173% of activity compared with O-acetyl-L-serine as substrate
-
-
?
L-azaserine + hydrogen sulfide
?
-
O-phospho-L-serine is a heat-stable substrate
-
-
ir
L-azaserine + sulfide
?
-
same activity as with O-acetyl-L-serine as substrate
-
-
?
L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + sulfide
-
OASS has a high activity in the L-cysteine desulfurization reaction
-
-
?
O-phospho-L-serine + sulfide
L-cysteine + phosphate
-
heat-stabile substrate, 219% of activity compared with O-acetyl-L-serine as substrate, best substrate at pH 6.7 and 60°C, formation of an alpha-aminoacrylate intermediate between O-phospho-L-serine and pyridoxal 5-phosphate
-
-
?
O3-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
low activity
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
enzyme is involved in L-cysteine biosynthesis, pathway overview
-
-
ir
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
O-acetyl-L-serine is a heat-labile substrate
-
-
ir
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
low activity
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + sulfide
L-cysteine + acetic acid
-
heat-labile substrate
-
-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
-
-
-
-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
-
-
-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
best substrate
-
-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
-
enzyme is involved in L-cysteine biosynthesis
-
-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
-
enzyme is involved in L-cysteine biosynthesis, pathway overview
-
-
ir
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
-
O-phospho-L-serine is a heat-stable substrate
-
-
ir
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
residue Arg297 near the entrance of the active site and is important for O-phospho-L-serine substrate recognition
-
-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
-
-
-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
residue Arg297 near the entrance of the active site and is important for O-phospho-L-serine substrate recognition
-
-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
-
-
-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
best substrate
-
-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
-
-
-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
-
-
-
?
O-phospho-L-serine + thiosulfate
S-sulfocysteine + phosphate
-
-
-
?
O-phospho-L-serine + thiosulfate
S-sulfocysteine + phosphate
-
-
-
?
O-phospho-L-serine + thiosulfate
S-sulfocysteine + phosphate
CysK2 utilizes O-phospho-L-serine and thiosulfate as acceptor and preferred sulfur donor substrates in a pyridoxal 5'-phosphate-dependent reaction resulting in the formation of S-sulfocysteine
-
-
?
O-phospho-L-serine + thiosulfate
S-sulfocysteine + phosphate
-
-
-
?
O-phospho-L-serine + thiosulfate
S-sulfocysteine + phosphate
CysK2 utilizes O-phospho-L-serine and thiosulfate as acceptor and preferred sulfur donor substrates in a pyridoxal 5'-phosphate-dependent reaction resulting in the formation of S-sulfocysteine
-
-
?
additional information
?
-
-
enzyme with cystathionine beta-synthase and O-acetylserine sulfhydrylase activity in vitro, OASS has also L-serine sulfhydrylation and S-sulfo-L-cysteine synthesis activity
-
-
?
additional information
?
-
-
not: 3-chloro-D-alanine, 3-cyano-L-alanine, O-benzyl-L-serine, O-tert-butyl-L-serine, O-phospho-D-serine, O-succinyl-L-homoserine, L-homoserine
-
-
?
additional information
?
-
-
substrate specificity, no activity with 3-chloro-D-alanine, 3-cyano-L-alanine, O-benzyl-L-serine, O-tert-butyl-L-serine, O-phospho-D-serine, O-succinyl-L-homoserine, and L-homoserine
-
-
?
additional information
?
-
-
the enzyme also shows low L-cystathionine forming activity
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of EC 2.5.1.47, cysteine synthase
-
-
?
additional information
?
-
OPSS is able to catalyze the synthetic reactions of various unnatural amino acids from OPS and nucleophiles that can substitute for sulfide
-
-
?
additional information
?
-
the enzyme is also active with O-acetyl-L-serine, cf. EC 2.5.1.47. When other nucleophiles are used instead of sulfide, enzyme ApOPSS produces the corresponding non-natural amino acid, when thiosulfate is used as nucleophile, for example, S-sulfocysteine is produced. In absence of sulfide, the primary substrate reacts with to pyridoxal 5'-phosphate in enzyme OPSS to yield an alpha-aminoacrylate intermediate, which is formed through an external Schiff base with the elimination of phosphate or acetate, the intermediate is finally degraded to pyruvate and pyridoxal 5'-phosphate by a water molecule without a nucleophile
-
-
?
additional information
?
-
OPSS is able to catalyze the synthetic reactions of various unnatural amino acids from OPS and nucleophiles that can substitute for sulfide
-
-
?
additional information
?
-
the enzyme is also active with O-acetyl-L-serine, cf. EC 2.5.1.47. When other nucleophiles are used instead of sulfide, enzyme ApOPSS produces the corresponding non-natural amino acid, when thiosulfate is used as nucleophile, for example, S-sulfocysteine is produced. In absence of sulfide, the primary substrate reacts with to pyridoxal 5'-phosphate in enzyme OPSS to yield an alpha-aminoacrylate intermediate, which is formed through an external Schiff base with the elimination of phosphate or acetate, the intermediate is finally degraded to pyruvate and pyridoxal 5'-phosphate by a water molecule without a nucleophile
-
-
?
additional information
?
-
-
enzyme is involved in an O-phosphoserine based cysteine biosynthesis pathway in Mycobacterium tuberculosis that is independent of both O-acetylserine and the sulphate reduction pathway
-
-
?
additional information
?
-
enzyme is involved in an O-phosphoserine based cysteine biosynthesis pathway in Mycobacterium tuberculosis that is independent of both O-acetylserine and the sulphate reduction pathway
-
-
?
additional information
?
-
-
O-acetylserine is not a substrate. Enzyme does not catalyze the reaction of EC 2.5.1.47, O-acetylserine sulfhydrolases
-
-
?
additional information
?
-
O-acetylserine is not a substrate. Enzyme does not catalyze the reaction of EC 2.5.1.47, O-acetylserine sulfhydrolases
-
-
?
additional information
?
-
-
specificity of CysM for its amino acid substrate is more than 500-fold greater for O-phospho-L-serine than for O-acetyl-L-serine. Specificity of CysM for this physiological sulfide equivalent, sulfur carrier protein CysO-COSH, is more than 3 orders of magnitude greater than that for bisulfide. CysM active site with the bound aminoacrylate intermediate is protected from solvent and that binding of CysO-COSH produces a conformational change allowing rapid sulfur transfer
-
-
?
additional information
?
-
the enzyme uses a mechanism via a central aminoacrylate intermediate that is similar to that of other members of this pyridoxal 5'-phosphate-dependent enzyme family. Enzyme CysK2 does not utilize thiocarboxylated CysO as a sulfur donor but accepts thiosulfate and sulfide as donor substrates, the specificity constant kcat/Km of CysK2 for thiosulfate is 40fold higher than for sulfide, suggesting an annotation as S-sulfocysteine synthase. No significant activity with O-acetyl-L-serine, Asp, Val, Gln, Glu, Ser, Asn, Cys, Ser, Leu, homocysteine, ketoacids such as pyruvate and 2-oxoglutarate, amino acid precursors like 3-phosphoglycerate and succinate, and derivatives like N-acetylcysteine and diaminopimelic acid
-
-
?
additional information
?
-
-
the enzyme uses a mechanism via a central aminoacrylate intermediate that is similar to that of other members of this pyridoxal 5'-phosphate-dependent enzyme family. Enzyme CysK2 does not utilize thiocarboxylated CysO as a sulfur donor but accepts thiosulfate and sulfide as donor substrates, the specificity constant kcat/Km of CysK2 for thiosulfate is 40fold higher than for sulfide, suggesting an annotation as S-sulfocysteine synthase. No significant activity with O-acetyl-L-serine, Asp, Val, Gln, Glu, Ser, Asn, Cys, Ser, Leu, homocysteine, ketoacids such as pyruvate and 2-oxoglutarate, amino acid precursors like 3-phosphoglycerate and succinate, and derivatives like N-acetylcysteine and diaminopimelic acid
-
-
?
additional information
?
-
enzyme is involved in an O-phosphoserine based cysteine biosynthesis pathway in Mycobacterium tuberculosis that is independent of both O-acetylserine and the sulphate reduction pathway
-
-
?
additional information
?
-
O-acetylserine is not a substrate. Enzyme does not catalyze the reaction of EC 2.5.1.47, O-acetylserine sulfhydrolases
-
-
?
additional information
?
-
the enzyme uses a mechanism via a central aminoacrylate intermediate that is similar to that of other members of this pyridoxal 5'-phosphate-dependent enzyme family. Enzyme CysK2 does not utilize thiocarboxylated CysO as a sulfur donor but accepts thiosulfate and sulfide as donor substrates, the specificity constant kcat/Km of CysK2 for thiosulfate is 40fold higher than for sulfide, suggesting an annotation as S-sulfocysteine synthase. No significant activity with O-acetyl-L-serine, Asp, Val, Gln, Glu, Ser, Asn, Cys, Ser, Leu, homocysteine, ketoacids such as pyruvate and 2-oxoglutarate, amino acid precursors like 3-phosphoglycerate and succinate, and derivatives like N-acetylcysteine and diaminopimelic acid
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
enzyme is involved in L-cysteine biosynthesis, pathway overview
-
-
ir
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
-
-
-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
-
enzyme is involved in L-cysteine biosynthesis
-
-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
-
enzyme is involved in L-cysteine biosynthesis, pathway overview
-
-
ir
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
-
-
-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
-
-
-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
-
-
-
?
O-phospho-L-serine + thiosulfate
S-sulfocysteine + phosphate
CysK2 utilizes O-phospho-L-serine and thiosulfate as acceptor and preferred sulfur donor substrates in a pyridoxal 5'-phosphate-dependent reaction resulting in the formation of S-sulfocysteine
-
-
?
O-phospho-L-serine + thiosulfate
S-sulfocysteine + phosphate
CysK2 utilizes O-phospho-L-serine and thiosulfate as acceptor and preferred sulfur donor substrates in a pyridoxal 5'-phosphate-dependent reaction resulting in the formation of S-sulfocysteine
-
-
?
additional information
?
-
-
enzyme is involved in an O-phosphoserine based cysteine biosynthesis pathway in Mycobacterium tuberculosis that is independent of both O-acetylserine and the sulphate reduction pathway
-
-
?
additional information
?
-
enzyme is involved in an O-phosphoserine based cysteine biosynthesis pathway in Mycobacterium tuberculosis that is independent of both O-acetylserine and the sulphate reduction pathway
-
-
?
additional information
?
-
enzyme is involved in an O-phosphoserine based cysteine biosynthesis pathway in Mycobacterium tuberculosis that is independent of both O-acetylserine and the sulphate reduction pathway
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
OASS contains 1.2 molecules pyridoxal 5'-phosphate per subunit, enzyme forms a Schiff base with pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
binding site in the cleft between middle and C-terminal domains through a covalent link to Lys127
pyridoxal 5'-phosphate
bound via a covalent linkage to the side chain of Lys51
pyridoxal 5'-phosphate
linked to lysine K127 as an internal Schiff base at the active site
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-chloro-D-alanine
-
18% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
3-Cyano-L-alanine
-
42% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Cd2+
-
slightly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation
CdCl2
-
25°C, 10 min, 26% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 15% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Co2+
-
strongly inhibits O-acetyl-L-serine sulfhydrylation, moderately inhibites O-phospho-L-serine sulfhydrylation
CoCl2
-
25°C, 10 min, 61% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 98.8% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Cu2+
-
strongly inhibits O-acetyl-L-serine sulfhydrylation, moderately inhibites O-phospho-L-serine sulfhydrylation
CuCl2
-
25°C, 10 min, 79% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 98.7% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Fe2+
-
slightly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation
Fe3+
-
strongly inhibits O-acetyl-L-serine sulfhydrylation, slightly inhibites O-phospho-L-serine sulfhydrylation
FeCl2
-
25°C, 10 min, 20% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 27% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
FeCl3
-
25°C, 10 min, 25% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 96.1% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Hg2+
-
strongly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation
HgCl2
-
25°C, 10 min, 98.3% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 80% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Ni2+
-
strongly inhibits O-acetyl-L-serine sulfhydrylation, slightly inhibites O-phospho-L-serine sulfhydrylation
NiCl2
-
25°C, 10 min, 15% inhibition of the O-phospho-L-serine sulfhydrylation reaction, almost complete inhibition of the O-acetyl-L-serine sulfhydrylation reaction
O-benzyl-L-serine
-
36% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
O-tert-butyl-L-serine
-
49% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Pb(CH3COO)2
-
25°C, 10 min, 95% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 88% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Pb2+
-
strongly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation
Zn2+
-
slightly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation
ZnCl2
-
25°C, 10 min, 23% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 25% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
additional information
-
no inhibition by O-phospho-D-serine, EDTA, 2-mercaptoethanol, DTT, NEM, PCMB, and Gd3+, while Ca2+, K+, Na+, Mn2+, and Mg2+ are poor inhibitors; no inhibition of the O-acetyl-L-serine sulfhydrylation reaction by O-phospho-D-serine
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
slightly activates the O-phospho-L-serine sulfhydrylation reaction
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Anaphylaxis
Life-threatening asthma and anaphylaxis in schools: a treatment model for school-based programs.
Asthma
Life-threatening asthma and anaphylaxis in schools: a treatment model for school-based programs.
Hypersensitivity
Life-threatening asthma and anaphylaxis in schools: a treatment model for school-based programs.
Influenza, Human
Comparing the yield of oropharyngeal swabs and sputum for detection of 11 common pathogens in hospitalized children with lower respiratory tract infection.
Lung Diseases
The clinical significance of oropharyngeal cultures in young children with cystic fibrosis.
Paramyxoviridae Infections
Comparing the yield of oropharyngeal swabs and sputum for detection of 11 common pathogens in hospitalized children with lower respiratory tract infection.
Tuberculosis
CysK2 from Mycobacterium tuberculosis Is an O-Phospho-l-Serine-Dependent S-Sulfocysteine Synthase.
Tuberculosis
Cysteine synthase (CysM) of Mycobacterium tuberculosis is an O-phosphoserine sulfhydrylase: evidence for an alternative cysteine biosynthesis pathway in mycobacteria.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.39
hydrogen sulfide
pH 7.5, 80°C, wild-type enzyme, with O-acetyl-L-serine
1.6
hydrogen sulfide
pH 7.5, 80°C, mutant F225A, with O-phospho-L-serine
3.8
hydrogen sulfide
pH 7.5, 80°C, wild-type enzyme, with O-phospho-L-serine
0.135
O-phospho-L-serine
dephosphorylation, pH 7.0, 22°C, recombinant wild-type enzyme
0.485
O-phospho-L-serine
pH 7.0, 22°C, recombinant mutant R243A enzyme
1.085
O-phospho-L-serine
dephosphorylation, pH 7.0, 22°C, recombinant mutant R243A enzyme
1.086
O-phospho-L-serine
pH 7.0, 22°C, recombinant wild-type enzyme
0.044
thiosulfate
pH 7.0, 22°C, recombinant wild-type enzyme
0.214
thiosulfate
pH 7.0, 22°C, recombinant mutant R243A enzyme
0.374
thiosulfate
dephosphorylation, pH 7.0, 22°C, recombinant wild-type enzyme
additional information
additional information
steady-state kinetics, 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
-
additional information
additional information
stopped-flow and Michaelis-Menten kinetic analysis, overview. The amino acrylate reaction intermediate is not stable and decomposes with a pseudo-first-order rate constant kobs of 0.12/s
-
additional information
additional information
-
stopped-flow and Michaelis-Menten kinetic analysis, overview. The amino acrylate reaction intermediate is not stable and decomposes with a pseudo-first-order rate constant kobs of 0.12/s
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.025
O3-acetyl-L-serine
-
formation of the aminoacrylate intermediate
17
O3-phospho-L-serine
-
formation of the aminoacrylate intermediate
33
hydrogen sulfide
pH 7.5, 80°C, wild-type enzyme, with O-acetyl-L-serine
130
hydrogen sulfide
pH 7.5, 80°C, mutant F225A, with O-phospho-L-serine
730
hydrogen sulfide
pH 7.5, 80°C, wild-type enzyme, with O-phospho-L-serine
0.0067
O-phospho-L-serine
dephosphorylation, pH 7.0, 22°C, recombinant mutant R243A enzyme
0.2
O-phospho-L-serine
dephosphorylation, pH 7.0, 22°C, recombinant wild-type enzyme
0.457
O-phospho-L-serine
pH 7.0, 22°C, recombinant mutant R243A enzyme
0.913
O-phospho-L-serine
pH 7.0, 22°C, recombinant wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
81
hydrogen sulfide
pH 7.5, 80°C, mutant F225A, with O-phospho-L-serine
85
hydrogen sulfide
pH 7.5, 80°C, wild-type enzyme, with O-acetyl-L-serine
190
hydrogen sulfide
pH 7.5, 80°C, wild-type enzyme, with O-phospho-L-serine
0.841
O-phospho-L-serine
pH 7.0, 22°C, recombinant wild-type enzyme
0.942
O-phospho-L-serine
pH 7.0, 22°C, recombinant mutant R243A enzyme
1.16
O-phospho-L-serine
dephosphorylation, pH 7.0, 22°C, recombinant wild-type enzyme
3.97
O-phospho-L-serine
apparent second-order rate of the first half-reaction, pH 7.0, 21°C, recombinant wild-type enzyme
additional information
additional information
the specificity constant kcat/Km of CysK2 for thiosulfate is 40fold higher than for sulfide
-
additional information
additional information
-
the specificity constant kcat/Km of CysK2 for thiosulfate is 40fold higher than for sulfide
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM