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Literature summary for 2.5.1.65 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
Search for more literature for 2.5.1.65

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Mycobacterium tuberculosis
expression in Escherichia coli Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment) Organism
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
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

Protein Variants

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 ?
-
 ?
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 ?
-
 ?
O-phospho-L-serine + hydrogen sulfide Mycobacterium tuberculosis
-
 L-cysteine + phosphate
-
 ?
O-phospho-L-serine + hydrogen sulfide Mycobacterium tuberculosis H37Rv
-
 L-cysteine + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-
Mycobacterium tuberculosis P9WP53
-
-
Mycobacterium tuberculosis H37Rv P9WP53
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography and Superdex-200 gel filtration Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
O-acetyl-L-serine + hydrogen sulfide
-
 Mycobacterium tuberculosis L-cysteine + acetate
-
 ?
O-phospho-L-serine + hydrogen sulfide
-
 Mycobacterium tuberculosis L-cysteine + phosphate
-
 ?
O-phospho-L-serine + hydrogen sulfide
-
 Mycobacterium tuberculosis H37Rv L-cysteine + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
CysM
-
 Mycobacterium tuberculosis
O-phosphoserine specific cysteine synthase
-
 Mycobacterium tuberculosis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.1
-
 O-phospho-L-serine 37°C Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Mycobacterium tuberculosis
pyridoxal 5'-phosphate bound via a covalent linkage to the side chain of Lys51 Mycobacterium tuberculosis