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B6db activities: 2.5.1.134

2.5.1.134
Description Cystathionine β-synthase (O-acetyl-L-serine)
Alternative names Cystathionine beta-synthase, O-acetylserine dependent;
MccB;
OAS-dCBS
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).
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
 
 
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
 
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.

Articles on 2.5.1.134
 
last changed 2019/06/21 13:03

B6db activities