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Information on EC 2.5.1.113 - [CysO sulfur-carrier protein]-thiocarboxylate-dependent cysteine synthase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WP53

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IUBMB Comments
A pyridoxal-phosphate protein. The enzyme participates in an alternative pathway for L-cysteine biosynthesis that involves a protein-bound thiocarboxylate as the sulfide donor. The enzyme from the bacterium Mycobacterium tuberculosis also has very low activity with O3-acetyl-L-serine (cf. EC 2.5.1.65, O-phosphoserine sulfhydrylase).
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This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: P9WP53
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Word Map
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  • 2.5.1.113
  • tubulin
  • microtubule
  • polyglutamylation
  • glutamylation
  • ligase-like
  • deglutamylated
  • cilia
  • purkinje
  • carboxypeptidase
The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
O-phospho-L-serine
+
[CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH
=
[CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-cysteine
+
phosphate
+
[CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH
=
[CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-cysteine
+
Synonyms
o-phosphoserine-specific cysteine synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
O-phosphoserine sulfhydrylase
-
O-phosphoserine-specific cysteine synthase
-
Cysteine synthase
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
O-phospho-L-serine:thiocarboxylated [CysO sulfur-carrier protein] 2-amino-2-carboxyethyltransferase
A pyridoxal-phosphate protein. The enzyme participates in an alternative pathway for L-cysteine biosynthesis that involves a protein-bound thiocarboxylate as the sulfide donor. The enzyme from the bacterium Mycobacterium tuberculosis also has very low activity with O3-acetyl-L-serine (cf. EC 2.5.1.65, O-phosphoserine sulfhydrylase).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
O-phospho-L-serine + [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH
[CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-cysteine + phosphate
show the reaction diagram
-
-
-
?
O-acetyl-L-serine + [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH
?
show the reaction diagram
-
the specificity of the enzyme for its amino acid substrate is more than 500fold greater for O-phospho-L-serine than for O-acetyl-L-serine
-
-
?
O-acetyl-L-serine + [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH
[CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-cysteine + acetate
show the reaction diagram
-
-
-
-
?
O-phospho-L-serine + [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH
[CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-cysteine + phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
O-phospho-L-serine + [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH
[CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-cysteine + phosphate
show the reaction diagram
-
-
-
?
O-acetyl-L-serine + [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH
[CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-cysteine + acetate
show the reaction diagram
-
-
-
-
?
O-phospho-L-serine + [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH
[CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-cysteine + phosphate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
O-phospho-L-serine
at pH 7.5 and 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.34 - 8.85
O-phospho-L-serine
0.857 - 146
[CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
x-ray crystallography
homodimer
-
x-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 0.1 M Tris-HCl, pH 7.25-7.5, 0.1 M K2HPO4, 4.3 M NaCl
native enzyme bound to CysO sulfur-carrier protein, hanging drop vapor diffusion method, using 7-10% PEG (w/v) 4000, 0.1 M sodium citrate, pH 5.8, and 0.2 M ammonium acetate at 22°C
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA319-323
the deletion mutant shows increased catalytic efficiency for O-phospho-L-serine and reduced catalytic efficiency for [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH
R220A
the mutant shows reduced activity with O-phospho-L-serine and increased activity with O-acetyl-L-serine compared to the wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA affinity column chromatography and Sephadex 200 gel filtration
Ni-NTA column chromatography, Superdex-200 gel filtration, and Sephadex G-25 gel filtration
Ni-NTA column chromatography
-
nickel affinity column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli B834(DE3) and BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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 (P9WP53), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WP53)
Manually annotated by BRENDA team
Jurgenson, C.T.; Burns, K.E.; Begley, T.P.; Ealick, S.E.
Crystal structure of a sulfur carrier protein complex found in the cysteine biosynthetic pathway of Mycobacterium tuberculosis
Biochemistry
47
10354-10364
2008
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Manually annotated by BRENDA team
Agren, D.; Schnell, R.; Schneider, G.
The C-terminal of CysM from Mycobacterium tuberculosis protects the aminoacrylate intermediate and is involved in sulfur donor selectivity
FEBS Lett.
583
330-336
2009
Mycobacterium tuberculosis (P9WP53), Mycobacterium tuberculosis H37Rv (P9WP53)
Manually annotated by BRENDA team
Burns-Huang, K.; Mundhra, S.
Mycobacterium tuberculosis cysteine biosynthesis genes mec+-cysO-cysM confer resistance to clofazimine
Tuberculosis
115
63-66
2019
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Manually annotated by BRENDA team