Information on EC 2.5.1.65 -

Information on EC 2.5.1.65 - O-phosphoserine sulfhydrylase:

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EC NUMBER	COMMENTARY
2.5.1.65	-

RECOMMENDED NAME	GeneOntology No.
O-phosphoserine sulfhydrylase	GO:0033847

REACTION	REACTION DIAGRAM	COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate		-	-	-	-
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	Aeropyrum pernix	-	654085
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate		ping-pong bi-bi mechanism	Aeropyrum pernix	-	655576
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	Aeropyrum pernix	-	659728

REACTION TYPE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
C-O bond cleavage	Aeropyrum pernix	-	-	654085
sulfhydrylation	Aeropyrum pernix	-	-	654085

PATHWAY	KEGG Link	MetaCyc Link
No entries in this field

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.

SYNONYMS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
APE1586	Aeropyrum pernix	-	Aeropyrum pernix K1, open reading frame	637385, 654085
CysM	Mycobacterium tuberculosis	P63873	-	687773
O-acetyl-L-serine sulfhydrylase	Aeropyrum pernix	-	-	654085
O-acetylserine sulfhydrylase	Aeropyrum pernix	-	-	637385, 654085, 655576
O-phosphoserine specific cysteine synthase	Mycobacterium tuberculosis	P63873	-	687773
O-phosphoserine(thiol)-lyase	Aeropyrum pernix	-	-	654085
OASS	Aeropyrum pernix	-	-	637385, 654085, 655576
OPSS	Aeropyrum pernix	-	-	659728

CAS REGISTRY NUMBER	COMMENTARY
37290-89-4	-

ORGANISM	COMMENTARY	LITERATURE	SEQUENCE CODE	SEQUENCE DB	SOURCE
Aeropyrum pernix	strain K1	637385, 654085, 659728	-	-
Aeropyrum pernix	strain K1; strain K1, hyperthermophilic archaeon	655576	-	-
Mycobacterium tuberculosis	-	687773	-	-
Mycobacterium tuberculosis	-	687773	P63873	UniProt
Mycobacterium tuberculosis	isoform CysM	685195	-	-

GENERAL INFORMATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

SUBSTRATE	PRODUCT	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY/ Substrate	LITERATURE/ Substrate	COMMENTARY/ Product	LITERATURE/ Product	Reversibility r=reversible ir=irreversible ?=not specified
3-chloro-L-alanine + hydrogen sulfide	?		Aeropyrum pernix	-	-	655576	-	-	ir
3-chloro-L-alanine + sulfide	?		Aeropyrum pernix	-	heat-labile substrate, 173% of activity compared with O-acetyl-L-serine as substrate	655576	-	-	?
L-azaserine + hydrogen sulfide	?		Aeropyrum pernix	-	O-phospho-L-serine is a heat-stable substrate	655576	-	-	ir
L-azaserine + sulfide	?		Aeropyrum pernix	-	same activity as with O-acetyl-L-serine as substrate	655576	-	-	?
O-acetyl-L-serine + hydrogen sulfide	L-cysteine + acetate		Mycobacterium tuberculosis	-	-	685195	-	-	-
O-acetyl-L-serine + hydrogen sulfide	L-cysteine + acetate		Mycobacterium tuberculosis	P63873	-	687773	-	-	?
O-acetyl-L-serine + hydrogen sulfide	L-cysteine + acetate		Aeropyrum pernix	-	-	654085, 659728	-	-	?
O-acetyl-L-serine + hydrogen sulfide	L-cysteine + acetate		Aeropyrum pernix	-	enzyme is involved in L-cysteine biosynthesis, pathway overview, O-acetyl-L-serine is a heat-labile substrate	655576	-	-	ir
O-acetyl-L-serine + sulfide	L-cysteine + acetic acid		Aeropyrum pernix	-	-	637385, 654085	-	-	?
O-acetyl-L-serine + sulfide	L-cysteine + acetic acid		Aeropyrum pernix	-	heat-labile substrate	655576	-	-	?
O-phospho-L-serine + hydrogen sulfide	L-cysteine + phosphate		Mycobacterium tuberculosis	P63873	-	687773	-	-	?
O-phospho-L-serine + hydrogen sulfide	L-cysteine + phosphate		Aeropyrum pernix	-	-	654085, 659728	-	-	?
O-phospho-L-serine + hydrogen sulfide	L-cysteine + phosphate		Aeropyrum pernix	-	enzyme is involved in L-cysteine biosynthesis	659728	-	-	?
O-phospho-L-serine + hydrogen sulfide	L-cysteine + phosphate		Aeropyrum pernix	-	enzyme is involved in L-cysteine biosynthesis, pathway overview, O-phospho-L-serine is a heat-stable substrate	655576	-	-	ir
O-phospho-L-serine + sulfide	L-cysteine + phosphate		Aeropyrum pernix	-	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	655576	-	-	?
O3-phospho-L-serine + hydrogen sulfide	L-cysteine + phosphate		Mycobacterium tuberculosis	-	-	685195	-	-	?
L-cysteine + dithiothreitol	S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + sulfide		Aeropyrum pernix	-	OASS has a high activity in the L-cysteine desulfurization reaction	637385	-	-	?
additional information	?	-	Aeropyrum pernix	-	biosynthesis of L-cysteine	637385	-	-	-
additional information	?	-	Aeropyrum pernix	-	L-cysteine biosynthesis	654085, 655576	-	-	-
additional information	?	-	Aeropyrum pernix	-	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	637385	-	-	-
additional information	?	-	Aeropyrum pernix	-	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, 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	655576	-	-	-
additional information	?	-	Aeropyrum pernix	-	the enzyme also shows low L-cystathionine forming activity	659728	-	-	-
additional information	?	-	Mycobacterium tuberculosis	P63873	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	687773	-	-	-
additional information	?	-	Mycobacterium tuberculosis	P63873	O-acetylserine is not a substrate. Enzyme does not catalyze the reaction of EC 2.5.1.47, O-acetylserine sulfhydrolases	687773	-	-	-
additional information	?	-	Mycobacterium tuberculosis	-	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	685195	-	-	-

NATURAL SUBSTRATES	NATURAL PRODUCTS	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY SUBSTRATE	LITERATURE (Substrate)	COMMENTARY PRODUCT	LITERATURE (Product)
O-acetyl-L-serine + hydrogen sulfide	L-cysteine + acetate		Aeropyrum pernix	-	-	654085	-	-
O-acetyl-L-serine + hydrogen sulfide	L-cysteine + acetate		Aeropyrum pernix	-	enzyme is involved in L-cysteine biosynthesis, pathway overview	655576	-	-
O-phospho-L-serine + hydrogen sulfide	L-cysteine + phosphate		Aeropyrum pernix	-	-	654085	-	-
O-phospho-L-serine + hydrogen sulfide	L-cysteine + phosphate		Mycobacterium tuberculosis	P63873	-	687773	-	-
O-phospho-L-serine + hydrogen sulfide	L-cysteine + phosphate		Aeropyrum pernix	-	enzyme is involved in L-cysteine biosynthesis	659728	-	-
O-phospho-L-serine + hydrogen sulfide	L-cysteine + phosphate		Aeropyrum pernix	-	enzyme is involved in L-cysteine biosynthesis, pathway overview	655576	-	-
additional information	?	-	Aeropyrum pernix	-	biosynthesis of L-cysteine	637385	-	-
additional information	?	-	Aeropyrum pernix	-	L-cysteine biosynthesis	654085, 655576	-	-
additional information	?	-	Mycobacterium tuberculosis	P63873	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	687773	-	-

COFACTOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
pyridoxal 5'-phosphate	Aeropyrum pernix	-	OASS contains 1.2 molecules pyridoxal 5'-phosphate per subunit, enzyme forms a Schiff base with pyridoxal 5'-phosphate	637385	2D-image
pyridoxal 5'-phosphate	Aeropyrum pernix	-	required	654085	2D-image
pyridoxal 5'-phosphate	Aeropyrum pernix	-	dependent on; pyridoxal 5'-phosphate-dependent	655576	2D-image
pyridoxal 5'-phosphate	Aeropyrum pernix	-	binding site in the cleft between middle and C-terminal domains through a covalent link to Lys127	659728	2D-image
pyridoxal 5'-phosphate	Mycobacterium tuberculosis	P63873	; bound via a covalent linkage to the side chain of Lys51	687773	2D-image

METALS and IONS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

INHIBITORS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
3-chloro-D-alanine	Aeropyrum pernix	-	18% inhibition of the O-acetyl-L-serine sulfhydrylation reaction	655576	2D-image
3-Cyano-L-alanine	Aeropyrum pernix	-	42% inhibition of the O-acetyl-L-serine sulfhydrylation reaction	655576	2D-image
Cd2+	Aeropyrum pernix	-	slightly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation	655576	2D-image
CdCl2	Aeropyrum pernix	-	25�C, 10 min, 26% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 15% inhibition of the O-acetyl-L-serine sulfhydrylation reaction	655576	2D-image
Co2+	Aeropyrum pernix	-	strongly inhibits O-acetyl-L-serine sulfhydrylation, moderately inhibites O-phospho-L-serine sulfhydrylation	655576	2D-image
CoCl2	Aeropyrum pernix	-	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	655576	2D-image
Cu2+	Aeropyrum pernix	-	strongly inhibits O-acetyl-L-serine sulfhydrylation, moderately inhibites O-phospho-L-serine sulfhydrylation	655576	2D-image
CuCl2	Aeropyrum pernix	-	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	655576	2D-image
Fe2+	Aeropyrum pernix	-	slightly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation	655576	2D-image
Fe3+	Aeropyrum pernix	-	strongly inhibits O-acetyl-L-serine sulfhydrylation, slightly inhibites O-phospho-L-serine sulfhydrylation	655576	2D-image
FeCl2	Aeropyrum pernix	-	25�C, 10 min, 20% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 27% inhibition of the O-acetyl-L-serine sulfhydrylation reaction	655576	2D-image
FeCl3	Aeropyrum pernix	-	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	655576	2D-image
Hg2+	Aeropyrum pernix	-	strongly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation	655576	2D-image
Ni2+	Aeropyrum pernix	-	strongly inhibits O-acetyl-L-serine sulfhydrylation, slightly inhibites O-phospho-L-serine sulfhydrylation	655576	2D-image
NiCl2	Aeropyrum pernix	-	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	655576	2D-image
O-benzyl-L-serine	Aeropyrum pernix	-	36% inhibition of the O-acetyl-L-serine sulfhydrylation reaction	655576	2D-image
O-tert-butyl-L-serine	Aeropyrum pernix	-	49% inhibition of the O-acetyl-L-serine sulfhydrylation reaction	655576	2D-image
Pb(CH3COO)2	Aeropyrum pernix	-	25�C, 10 min, 95% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 88% inhibition of the O-acetyl-L-serine sulfhydrylation reaction	655576	2D-image
Pb2+	Aeropyrum pernix	-	strongly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation	655576	2D-image
Zn2+	Aeropyrum pernix	-	slightly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation	655576	2D-image
ZnCl2	Aeropyrum pernix	-	25�C, 10 min, 23% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 25% inhibition of the O-acetyl-L-serine sulfhydrylation reaction	655576	2D-image
HgCl2	Aeropyrum pernix	-	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	655576	2D-image
additional information	Aeropyrum pernix	-	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	655576	-

ACTIVATING COMPOUND	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
dithiothreitol	Aeropyrum pernix	-	slightly activates the O-phospho-L-serine sulfhydrylation reaction	655576	2D-image

KM VALUE [mM]	KM VALUE [mM] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.25	-	hydrogen sulfide	Aeropyrum pernix	-	pH 7.6, 60�C, with O-acetyl-L-serine	655576	2D-image
5	-	hydrogen sulfide	Aeropyrum pernix	-	pH 7.6, 60�C, with O-phospho-L-serine	655576	2D-image
21	-	O-Acetyl-L-serine	Aeropyrum pernix	-	60�C; pH 7.6, 60�C	655576	2D-image
28	-	O-Acetyl-L-serine	Aeropyrum pernix	-	pH 6.7	637385	2D-image
200	-	O-phospho-L-serine	Aeropyrum pernix	-	60�C; pH 7.6, 60�C	655576	2D-image
250	-	O-phospho-L-serine	Aeropyrum pernix	-	85�C; pH 7.6, 85�C	655576	2D-image
0.2	-	Sulfide	Aeropyrum pernix	-	below, pH 6.7	637385	2D-image
0.25	-	Sulfide	Aeropyrum pernix	-	60�C, O-acetyl-L-serine sulfhydrylation reaction	655576	2D-image
5	-	Sulfide	Aeropyrum pernix	-	60�C, O-phospho-L-serine sulfhydrylation reaction	655576	2D-image
12.5	-	Sulfide	Aeropyrum pernix	-	85�C, O-phospho-L-serine sulfhydrylation reaction	655576	2D-image
12.5	-	hydrogen sulfide	Aeropyrum pernix	-	pH 7.6, 85�C, with O-phospho-L-serine	655576	2D-image
additional information	-	additional information	Aeropyrum pernix	-	-	637385	-
additional information	-	additional information	Aeropyrum pernix	-	kinetics; ping-pong bi-bi mechanism	655576	-

TURNOVER NUMBER [1/s]	TURNOVER NUMBER MAXIMUM[1/s]	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
156	-	O-Acetyl-L-serine	Aeropyrum pernix	-	60�C; pH 7.6, 60�C	655576	2D-image
202	-	O-Acetyl-L-serine	Aeropyrum pernix	-	pH 6.7	637385	2D-image
0.1	-	O-phospho-L-serine	Mycobacterium tuberculosis	P63873	37�C	687773	2D-image
3050	-	O-phospho-L-serine	Aeropyrum pernix	-	60�C; pH 7.6, 60�C	655576	2D-image
14000	-	O-phospho-L-serine	Aeropyrum pernix	-	85�C; pH 7.6, 85�C	655576	2D-image
0.025	-	O3-Acetyl-L-serine	Mycobacterium tuberculosis	-	formation of the aminoacrylate intermediate	685195	2D-image
17	-	O3-phospho-L-serine	Mycobacterium tuberculosis	-	formation of the aminoacrylate intermediate	685195	2D-image
additional information	-	additional information	Aeropyrum pernix	-	-	637385	-

kcat/KM VALUE [1/mMs^-1]	kcat/KM VALUE [1/mMs^-1] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

Ki VALUE [mM]	Ki VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

IC50 VALUE [mM]	IC50 VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg]	SPECIFIC ACTIVITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
1	-	Aeropyrum pernix	-	mutant R297A, substrate O-phospho-L-serine	659728
50.9	-	Aeropyrum pernix	-	pH 6.7, 60�C, O-acetyl-L-serine sulfhydrylation	637385
53.1	-	Aeropyrum pernix	-	mutant R297A, substrate O-acetyl-L-serine	659728
54.5	-	Aeropyrum pernix	-	60�C, O-acetyl-L-serine sulfhydrylation reaction, recombinant OASS	655576
72	-	Aeropyrum pernix	-	wild-type enzyme, substrate O-acetyl-L-serine	659728
245	-	Aeropyrum pernix	-	wild-type enzyme, substrate O-phospho-L-serine	659728

pH OPTIMUM	pH MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
6.7	-	Aeropyrum pernix	-	-	637385
7.3	8.1	Aeropyrum pernix	-	at 85�C; dependent on the substrate, overview	655576

pH RANGE	pH RANGE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

TEMPERATURE OPTIMUM	TEMPERATURE OPTIMUM MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
70	-	Aeropyrum pernix	-	sulfhydrylation of 3-chloro-L-alanine; with substrate 3-chloro-L-alanine	655576
80	-	Aeropyrum pernix	-	sulfhydrylation of L-azaserine; with substrate L-azaserine	655576
85	-	Aeropyrum pernix	-	assay at	659728
90	-	Aeropyrum pernix	-	sulfhydrylation of O-phospho-L-serine; with substrate O-phospho-L-serine	655576

TEMPERATURE RANGE	TEMPERATURE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

pI VALUE	pI VALUE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

SOURCE TISSUE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	SOURCE
No entries in this field

LOCALIZATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	GeneOntology No.	LITERATURE	SOURCE
No entries in this field

PDB	SCOP	CATH	ORGANISM
3vsa, download	SCOP (3vsa)	CATH (3vsa)	Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
3vsc, download	SCOP (3vsc)	CATH (3vsc)	Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
3vsd, download	SCOP (3vsd)	CATH (3vsd)	Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
3dki, download	SCOP (3dki)	CATH (3dki)	Mycobacterium tuberculosis
3fgp, download	SCOP (3fgp)	CATH (3fgp)	Mycobacterium tuberculosis

MOLECULAR WEIGHT	MOLECULAR WEIGHT MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
70580	-	Aeropyrum pernix	-	sedimentation equilibrium ultracentrifugation	637385

SUBUNITS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
dimer	Aeropyrum pernix	-	2 * 42000, SDS-PAGE	637385
dimer	Aeropyrum pernix	-	-	654085
dimer	Aeropyrum pernix	-	2 * 42000	655576
additional information	Aeropyrum pernix	-	an enzyme monomer consists of 3 domains, structure overview	659728

POSTTRANSLATIONAL MODIFICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

Crystallization/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
hanging-drop vapor-diffusion method; purified recombinant enzyme, optimization of crystallization method, hanging drop vapour diffusion method, enzyme in 50 mM potassium phosphate buffer pH 7.5, containing 0.2 mM pyridoxal 5'-phosphate and 0.05% sodium azide, 0.0015 ml of enzyme and reservoir solution, containing 0.1 M sodium cacodylate pH 7.4, 0.1 M sodium acetate and 30% v/v PEG 8000, are equilibrated against 0.5 ml of reservoir solution at 295�C, 2 weeks, cryoprotection by 10% v/v glycerol, X-ray diffraction structure determination and analysis at 2.2 A resolution	Aeropyrum pernix	-	654085
wild-type and selennomethionine-labeled enzyme, sitting drop method, 20 mg/ml protein in solution with 0.1 mM pyridoxal 5'-phosphate, 3 mM 2-mercaptoethanol, reservoir solution contains 0.1 M sodium cacodylate, pH 7.0, 0.2 M sodium acetate, 21% w/v poylethylene glycol 8000, and 3 mM 2-mercaptoethanol, mixture of equal volumes of protein and reservoir solution of 0.0035 ml, equilibration against 0.1 ml reservoir solution, 25�C, 2 weeks, crystallization of the selenomethinone enzyme at pH 6.0, multi-wave anomalous dispersion, X-ray diffraction structure determination and analysis at 2.0 A resolution	Aeropyrum pernix	-	659728
2.1 A resolution. A model of O-phosphoserine bound to the enzyme suggests a hydrogen bonding interaction of the side chain of Arg220 with the phosphate group as a key feature in substrate selectivity; sitting drop vapour diffusion method, with 0.1 M Tris-HCl pH 7.25-7.5, 0.1 M K2HPO4, 4.3 M NaCl	Mycobacterium tuberculosis	P63873	687773

pH STABILITY	pH STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
6.1	-	Aeropyrum pernix	-	6 h, 100�C, 10% loss of activity	637385
6.7	-	Aeropyrum pernix	-	6 h, 100�C, 10% loss of activity	637385
7.5	-	Aeropyrum pernix	-	6 h, 100�C, 44% loss of activity	637385
8.5	-	Aeropyrum pernix	-	6 h, 100�C, 89% loss of activity	637385

TEMPERATURE STABILITY	TEMPERATURE STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
90	-	Aeropyrum pernix	-	50% of maximum activity with 3-chloro-L-alanine as substrate	655576
100	-	Aeropyrum pernix	-	6 h, pH 6.1 and 6.7: 10% loss of activity, pH 7.5: 44% loss of activity, pH 8.5: 89% loss of activity	637385

GENERAL STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

ORGANIC SOLVENT	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

OXIDATION STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

STORAGE STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
4�C, enzyme solution, stable	Aeropyrum pernix	-	637385

Purification/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
recombinant enzyme from Escherichia coli; recombinant OASS	Aeropyrum pernix	-	654085
recombinant OASS	Aeropyrum pernix	-	637385, 655576
recombinant wild-type, selenomethinonine-labeled, and mutant R297A enzymes from Escherichia coli	Aeropyrum pernix	-	659728
Ni-NTA column chromatography and Superdex-200 gel filtration	Mycobacterium tuberculosis	P63873	687773

Cloned/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
expression in Escherichia coli Rosetta (DE3)	Aeropyrum pernix	-	655576
expression in Escherichia coli Rosetta (DE3), sequencing	Aeropyrum pernix	-	637385
expression of wild-type, selenomethinonine-labeled, and mutant R297A enzymes in Escherichia coli	Aeropyrum pernix	-	659728
overexpression in Escherichia coli; overexpression in Escherichia coli Rosetta (DE3)	Aeropyrum pernix	-	654085
expressed in Escherichia coli BL21(DE3) cells; expression in Escherichia coli	Mycobacterium tuberculosis	P63873	687773

EXPRESSION	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

ENGINEERING	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
R297A	Aeropyrum pernix	-	site-directed mutagenesis, highly reduced activity with phospho-L-serine compared to the wild-type enzyme	659728
R220A	Mycobacterium tuberculosis	P63873	700fold lower activity with O-phospho-L-serine as substrate compared to the wild type enzyme; 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	687773

Renatured/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

APPLICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

REF.	AUTHORS	TITLE	JOURNAL	VOL.	PAGES	YEAR	ORGANISM	LINK TO PUBMED	SOURCE
637385	Mino, K.; Ishikawa, K.	Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1	J. Bacteriol.	185	2277-2284	2003	Aeropyrum pernix	PubMed
654085	Mino, K.; Oda, Y.; Ataka, M.; Ishikawa, K.	Crystallization and preliminary X-ray diffraction analysis of O-acetylserine sulfhydrylase from Aeropyrum pernix K1	Acta Crystallogr. Sect. D	59	338-340	2003	Aeropyrum pernix	PubMed
655576	Mino, K.; Ishikawa, K.	A novel O-phospho-L-serine sulfhydrylation reaction catalyzed by O-acetylserine sulfhydrylase from Aeropyrum pernix K1	FEBS Lett.	551	133-138	2003	Aeropyrum pernix	PubMed
659728	Oda, Y.; Mino, K.; Ishikawa, K.; Ataka, M.	Three-dimensional structure of a new enzyme, O-phosphoserine sulfhydrylase, involved in l-cysteine biosynthesis by a hyperthermophilic archaeon, Aeropyrum pernix K1, at 2.0 A resolution	J. Mol. Biol.	351	334-344	2005	Aeropyrum pernix	PubMed
685195	OLeary, S.E.; Jurgenson, C.T.; Ealick, S.E.; Begley, T.P.	O-Phospho-l-serine and the thiocarboxylated sulfur carrier protein CysO-COSH are substrates for CysM, a cysteine synthase from Mycobacterium tuberculosis	Biochemistry	47	11606-11615	2008	Mycobacterium tuberculosis	PubMed
687773	Agren, D.; Schnell, R.; Oehlmann, W.; Singh, M.; Schneider, G.	Cysteine synthase (CYSM) of Mycobacterium tuberculosis is an O-phosphoserine sulfhydrylase: Evidence for an alternative cysteine biosynthesis pathway in mycobacteria	J. Biol. Chem.	283	31567-31574	2008	Mycobacterium tuberculosis	PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 2.5.1.65)

NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM

IUBMB Enzyme Nomenclature

PROSITE Database of protein families and domains

SYSTERS

Protein Mutant Database

InterPro (database of protein families, domains and functional sites)

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