Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli BL21(DE3) cells | Mycobacterium tuberculosis |
expression in Escherichia coli | Mycobacterium tuberculosis |
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 | 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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | - |
- |
- |
Mycobacterium tuberculosis | P9WP53 | - |
- |
Mycobacterium tuberculosis H37Rv | P9WP53 | - |
- |
Purification (Comment) | Organism |
---|---|
Ni-NTA column chromatography and Superdex-200 gel filtration | Mycobacterium tuberculosis |
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 | Comment | Organism |
---|---|---|
CysM | - |
Mycobacterium tuberculosis |
O-phosphoserine specific cysteine synthase | - |
Mycobacterium tuberculosis |
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 | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | - |
Mycobacterium tuberculosis | |
pyridoxal 5'-phosphate | bound via a covalent linkage to the side chain of Lys51 | Mycobacterium tuberculosis |