Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • 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 (2008), Biochemistry, 47, 11606-11615.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.113 O-phospho-L-serine + [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH Mycobacterium tuberculosis the specificity of the enzyme for the physiological sulfide equivalent [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH is more than 3 orders of magnitude greater than that for bisulfide [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
-
 isoform CysM
-
2.5.1.113 Mycobacterium tuberculosis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.113 nickel affinity column chromatography Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.65 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 Mycobacterium tuberculosis ?
-
 ?
2.5.1.65 O-acetyl-L-serine + hydrogen sulfide
-
 Mycobacterium tuberculosis L-cysteine + acetate
-
 ?
2.5.1.65 O3-phospho-L-serine + hydrogen sulfide
-
 Mycobacterium tuberculosis L-cysteine + phosphate
-
 ?
2.5.1.113 O-acetyl-L-serine + [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH 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 Mycobacterium tuberculosis ?
-
 ?
2.5.1.113 O-phospho-L-serine + [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH the specificity of the enzyme for the physiological sulfide equivalent [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH is more than 3 orders of magnitude greater than that for bisulfide Mycobacterium tuberculosis [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-cysteine + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.113 CysM
-
 Mycobacterium tuberculosis
2.5.1.113 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 0.025
-
 O3-acetyl-L-serine formation of the aminoacrylate intermediate Mycobacterium tuberculosis
2.5.1.65 17
-
 O3-phospho-L-serine formation of the aminoacrylate intermediate Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
2.5.1.113 pyridoxal 5'-phosphate
-
 Mycobacterium tuberculosis