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Literature summary extracted from

  • 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 (2008), J. Biol. Chem., 283, 31567-31574.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.65 expressed in Escherichia coli BL21(DE3) cells Mycobacterium tuberculosis
2.5.1.65 expression in Escherichia coli Mycobacterium tuberculosis
2.5.1.113 expressed in Escherichia coli BL21(DE3) cells Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.5.1.65 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 Mycobacterium tuberculosis
2.5.1.65 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
2.5.1.113 sitting drop vapor diffusion method, using 0.1 M Tris-HCl, pH 7.25-7.5, 0.1 M K2HPO4, 4.3 M NaCl Mycobacterium tuberculosis

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.65 R220A 700fold lower activity with O-phospho-L-serine as substrate compared to the wild type enzyme Mycobacterium tuberculosis
2.5.1.65 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 Mycobacterium tuberculosis
2.5.1.113 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 Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.65 additional information Mycobacterium tuberculosis 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 ?
-
 ?
2.5.1.65 additional information Mycobacterium tuberculosis H37Rv 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 ?
-
 ?
2.5.1.65 O-phospho-L-serine + hydrogen sulfide Mycobacterium tuberculosis
-
 L-cysteine + phosphate
-
 ?
2.5.1.65 O-phospho-L-serine + hydrogen sulfide Mycobacterium tuberculosis H37Rv
-
 L-cysteine + phosphate
-
 ?
2.5.1.113 O-phospho-L-serine + [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH Mycobacterium tuberculosis
-
 [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-cysteine + phosphate
-
 ?
2.5.1.113 O-phospho-L-serine + [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH Mycobacterium tuberculosis H37Rv
-
 [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-cysteine + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.65 Mycobacterium tuberculosis
-
-
-
2.5.1.65 Mycobacterium tuberculosis P9WP53
-
-
2.5.1.65 Mycobacterium tuberculosis H37Rv P9WP53
-
-
2.5.1.113 Mycobacterium tuberculosis P9WP53
-
-
2.5.1.113 Mycobacterium tuberculosis H37Rv P9WP53
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.65 Ni-NTA column chromatography and Superdex-200 gel filtration Mycobacterium tuberculosis
2.5.1.113 Ni-NTA column chromatography, Superdex-200 gel filtration, and Sephadex G-25 gel filtration Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.65 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 Mycobacterium tuberculosis ?
-
 ?
2.5.1.65 additional information O-acetylserine is not a substrate. Enzyme does not catalyze the reaction of EC 2.5.1.47, O-acetylserine sulfhydrolases Mycobacterium tuberculosis ?
-
 ?
2.5.1.65 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 Mycobacterium tuberculosis H37Rv ?
-
 ?
2.5.1.65 additional information O-acetylserine is not a substrate. Enzyme does not catalyze the reaction of EC 2.5.1.47, O-acetylserine sulfhydrolases Mycobacterium tuberculosis H37Rv ?
-
 ?
2.5.1.65 O-acetyl-L-serine + hydrogen sulfide
-
 Mycobacterium tuberculosis L-cysteine + acetate
-
 ?
2.5.1.65 O-phospho-L-serine + hydrogen sulfide
-
 Mycobacterium tuberculosis L-cysteine + phosphate
-
 ?
2.5.1.65 O-phospho-L-serine + hydrogen sulfide
-
 Mycobacterium tuberculosis H37Rv L-cysteine + phosphate
-
 ?
2.5.1.113 additional information no activity with O-acetyl-L-serine Mycobacterium tuberculosis ?
-
 ?
2.5.1.113 additional information no activity with O-acetyl-L-serine Mycobacterium tuberculosis H37Rv ?
-
 ?
2.5.1.113 O-phospho-L-serine + [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH
-
 Mycobacterium tuberculosis [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-cysteine + phosphate
-
 ?
2.5.1.113 O-phospho-L-serine + [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH
-
 Mycobacterium tuberculosis H37Rv [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-cysteine + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.65 CysM
-
 Mycobacterium tuberculosis
2.5.1.65 O-phosphoserine specific cysteine synthase
-
 Mycobacterium tuberculosis
2.5.1.113 CysM
-
 Mycobacterium tuberculosis
2.5.1.113 O-phosphoserine sulfhydrylase
-
 Mycobacterium tuberculosis
2.5.1.113 O-phosphoserine-specific cysteine synthase
-
 Mycobacterium tuberculosis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5.1.65 0.1
-
 O-phospho-L-serine 37°C Mycobacterium tuberculosis
2.5.1.113 0.1
-
 O-phospho-L-serine at pH 7.5 and 37°C Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
2.5.1.65 pyridoxal 5'-phosphate
-
 Mycobacterium tuberculosis
2.5.1.65 pyridoxal 5'-phosphate bound via a covalent linkage to the side chain of Lys51 Mycobacterium tuberculosis
2.5.1.113 pyridoxal 5'-phosphate dependent on Mycobacterium tuberculosis