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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

Purification

Purification on EC 4.2.1.22 - cystathionine beta-synthase

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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CBSdeltaC143
-
full length enzyme exhibits a strong tendency toward aggregation during the course of purification as well as in the purified state
-
full length protein and truncated variant lacking 143 amino acid residues at the C-terminus
-
glutathione-linked resin chromatography, HiTrap Q Fast Flow column chromatography, GST-Sepharose column chromatography, and Superose 12 gel-filtration
-
glutathione-Sepharose column chromatography
-
GST Trap FF column chromatography and Mono Q column chromatography
N-terminal cystathionine beta-synthase domain fused to the C-terminal Zn ribbon domain overexpressed in Escherichia coli
Ni-NTA column chromatography
-
recombinant cystathionine beta-synthase from Escherichia coli strain BL21(DE3) by anion exchange and hydroxyapatite chromatography
-
recombinant GST-tagged wild-type and Co-subsituted CBS from Escherichia coli strain Rosetta 2 (DE3) by glutathione affinity and anion exchange chromatography
-
recombinant mutant 45CBS and wild-type CBS from Escherichia coli to homogeneity
-
truncated human CBS lacking 143 amino acids at the C-terminus is purified as a fusion protein with glutathione S-transferase using the Escherichia coli expression vector pGEXCBSN. The protein is purified through affinity chromatography with glutathione sepharose and anion exchange chromatography. The glutathione Stransferase tag was cleaved by limited proteolysis using thrombin
two patient-derived forms S466L and I435T, 95% purity
-
using a glutathione sepharose column
-
using Ni-NTA chromatography
-
wild type and truncated human cystathionine beta-synthase expressed in Escherichia coli
-