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

BRENDA support

4.2.1.22: cystathionine beta-synthase

This is an abbreviated version!
For detailed information about cystathionine beta-synthase, go to the full flat file.

Word Map on EC 4.2.1.22

Reaction

L-serine
+
L-homocysteine
=
L-cystathionine
 +
H2O

Synonyms

Beta-thionase, CBS, CBS424, CDCP2, CNNM2, Cys4, CysB, cystathionine beta synthase, cystathionine beta-synthase, cystathionine beta-synthase domain-containing protein, cystathionine-beta-synthase, Cysteine synthase, EC 4.2.1.21, hCBS, Hemoprotein H-450, LbrM.17.0230, Methylcysteine synthase, osmoprotectant transporter OpuC, PF1953, PH0267, Serine sulfhydrase, Serine sulfhydrylase, Serine sulphhydrase, TA0289, TM0935, TV1335, yCBS, ytCBS

ECTree

     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.22 cystathionine beta-synthase

Crystallization

Crystallization on EC 4.2.1.22 - cystathionine beta-synthase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 3.2 A resolution, space group P212121
hanging drop vapour diffusion method, 100 mM phosphate-acetate pH 4.2, 200 mM NaCl and 20% (w/v) PEG 8000
-
to 2.2 A resolution
A0A1J9VES8
enzyme free or in complex with a carbanion and an aminoacrylate intermediate, X-ray diffraction structure determination and analysis at 1.70 A and 1.55 A resolution, respectively
two AMP molecules, in C3'- and C2'-endo conformations respectively, simultaneously bind to a cystathionine-beta-synthase domain dimer of the magnesium and cobalt efflux protein CorC. The C2'-endo AMP molecule assumes the higher sugar pucker energy and one more hydrogen bond with the protein than the C3'-endo molecule does
-
catalytic core, hanging drop vapor diffusion method
mutant lacking the S-adenosyl-L-methionine binding site and heme-free crystals, hanging drop vapor diffusion method
-
role of surface electrostatics. The kinetic stability of the catalytic and regulatory domains is significantly affected by the modulation of surface electrostatics through noticeable structural and energetic changes along their denaturation pathways. Surface electrostatics strongly affect SAM binding properties to those sites responsible for either enzyme activation or kinetic stabilization
structure of CBS with bound AdoMet. Binding of AdoMet triggers a conformational change in the Bateman module of the regulatory domain that favors its association with a Bateman module of the complementary subunit to form an antiparallel CBS module. In the presence of AdoMet, the autoinhibition exerted by the regulatory region is eliminated
truncated form
with heme and pyridoxal 5'-phosphate, hanging drop vapor diffusion method
-
crystallization of truncated enzyme, lacking amino acids 345-507, leads to two different crystal forms belonging to space groups P41212 and P212121, to 2.7 and 3.1 A resolution, respectively
structure of the catalytic core, residues 1-353, to 1.5 A resolution, and structures with pyridoxal 5'-phosphate-L-serine external aldimine, aminoacrylate intermediate, cycloserine and hydrazine. Two monomers form a tight dimer. The monomer contains two structurally conserved salt bridges, residues E174/K42 and E44/R55, on the si side of the pyridoxal 5'-phosphate cofactor
crystal structures of both mercury- and iron-bound TA0289 (1.5–2.0 A resolution) reveals a dimeric protein whose intersubunit contacts are formed exclusively by the alpha-helices of two cystathionine beta-synthase subdomains, whereas the C-terminal domain has a classical Zn ribbon planar architecture
-
nanodropletvapor diffusion method, crystal structure of a tandem cystathionine-beta-synthase domain protein (TM0935) from Thermotoga maritima at 1.87 A resolution
-
to 2.45 A resolution, space group P6222. Enzyme display tetrameric structure with several inter-domain interactions