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2.5.1.134 |
| Description |
Cystathionine β-synthase (O-acetyl-L-serine) |
| Alternative names |
Cystathionine beta-synthase, O-acetylserine dependent;
MccB;
OAS-dCBS
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| Catalyzed reaction |
O-acetyl-L-serine + L-homocysteine = L-cystathionine + acetate |
| Cofactor |
Pyridoxal-phosphate. |
| Comments |
A pyridoxal 5'-phosphate protein. The enzyme, purified from the bacterium Bacillus subtilis, also has a low activity with L-serine (cf. EC 4.2.1.22, cystathionine β-synthase). |
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The enzyme from B. anthracis was found to show CBS activity only with O-acetylserine (OAS) and not with serine, and was also observed to display OAS sulfhydrylase activity but not serine sulfhydrylase activity. |
| PDB |
5XW3; 5B1H; |
| Organisms |
-Eubacteria |
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Family |
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| Links |
Enzyme (activities) 2.5.1.134
BRENDA (activities) 2.5.1.134
KEGG (pathways) 2.5.1.134
PLPMDB (PLP mutants) 2.5.1.134
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| References |
Devi S, Tarique KF, Ali MF, Abdul Rehman SAX, Gourinath S (2019) Identification and characterisation of Helicobacter pylori O-acetylserine-dependent cystathionine β-synthase, a distinct member of the PLP-II family Mol Microbiol 112 718-739. Devi S, Abdul Rehman SA, Tarique KF, Gourinath S (2017) Structural characterization and functional analysis of cystathionine β-synthase: an enzyme involved in the reverse transsulfuration pathway of Bacillus anthracis FEBS J 284 3862-3880. Matoba Y, Yoshida T, Izuhara-Kihara H, Noda M, Sugiyama M
(2017) Crystallographic and mutational analyses of cystathionine β-synthase in the H2 S-synthetic gene cluster in Lactobacillus plantarum
Protein Sci 26 763-783. Hullo MF, Auger S, Soutourina O, Barzu O, Yvon M, Danchin A, Martin-Verstraete I (2007) Conversion of methionine to cysteine in Bacillus subtilis and its regulation J Bacteriol 189 187-97. |
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| last changed |
2019/06/21 13:03 |
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